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Database: PDB
Entry: 3G15
LinkDB: 3G15
Original site: 3G15 
HEADER    TRANSFERASE                             29-JAN-09   3G15              
TITLE     CRYSTAL STRUCTURE OF HUMAN CHOLINE KINASE ALPHA IN COMPLEX WITH       
TITLE    2 HEMICHOLINIUM-3 AND ADP                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLINE KINASE ALPHA;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 75-457;                                       
COMPND   5 SYNONYM: CK, CHETK-ALPHA;                                            
COMPND   6 EC: 2.7.1.32;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CHKA, CHK, CKI;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)RIL;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28ALIC                                 
KEYWDS    NON-PROTEIN KINASE, CHOLINE KINASE, STRUCTURAL GENOMICS CONSORTIUM,   
KEYWDS   2 SGC, HEMICHOLINIUM-3, KINASE, TRANSFERASE                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.S.HONG,W.TEMPEL,W.M.RABEH,F.MACKENZIE,C.H.ARROWSMITH,A.M.EDWARDS,   
AUTHOR   2 C.BOUNTRA,J.WEIGELT,A.BOCHKAREV,H.W.PARK,STRUCTURAL GENOMICS         
AUTHOR   3 CONSORTIUM (SGC)                                                     
REVDAT   5   06-SEP-23 3G15    1       REMARK                                   
REVDAT   4   21-OCT-20 3G15    1       REMARK SEQADV LINK                       
REVDAT   3   01-NOV-17 3G15    1       REMARK                                   
REVDAT   2   01-SEP-10 3G15    1       JRNL                                     
REVDAT   1   10-FEB-09 3G15    0                                                
SPRSDE     10-FEB-09 3G15      3F2S                                             
JRNL        AUTH   B.S.HONG,A.ALLALI-HASSANI,W.TEMPEL,P.J.FINERTY,F.MACKENZIE,  
JRNL        AUTH 2 S.DIMOV,M.VEDADI,H.W.PARK                                    
JRNL        TITL   CRYSTAL STRUCTURES OF HUMAN CHOLINE KINASE ISOFORMS IN       
JRNL        TITL 2 COMPLEX WITH HEMICHOLINIUM-3: SINGLE AMINO ACID NEAR THE     
JRNL        TITL 3 ACTIVE SITE INFLUENCES INHIBITOR SENSITIVITY.                
JRNL        REF    J.BIOL.CHEM.                  V. 285 16330 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   20299452                                                     
JRNL        DOI    10.1074/JBC.M109.039024                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0069                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 93409                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : THIN SHELLS (SFTOOLS)           
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.221                           
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.272                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2122                            
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) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4998                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 70.89                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3370                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 0                            
REMARK   3   BIN FREE R VALUE                    : 0.2980                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5354                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 149                                     
REMARK   3   SOLVENT ATOMS            : 324                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.16                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.52200                                             
REMARK   3    B22 (A**2) : 1.29200                                              
REMARK   3    B33 (A**2) : -0.77000                                             
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): 0.112         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.113         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.079         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.363         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5670 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3911 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7696 ; 1.388 ; 1.992       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9476 ; 2.189 ; 3.007       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   669 ; 5.454 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   257 ;32.119 ;23.424       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   961 ;12.758 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    31 ;13.077 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   802 ; 0.083 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6164 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1241 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  3322 ; 2.012 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1327 ; 0.586 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5332 ; 2.992 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2348 ; 2.410 ; 2.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2357 ; 3.479 ; 3.000       
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 BULK SOLVENT                                    
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. HEMICHOLINIUM-3 RESTRAINTS WERE PREPARED BY THE          
REMARK   3  PRODRG SERVER.                                                      
REMARK   4                                                                      
REMARK   4 3G15 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000051291.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-FEB-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.96863                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 93657                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
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     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.06900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 75.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.79700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE                                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2I7Q                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG-3350, 0.2M LITHIUM SULFATE,      
REMARK 280  0.1M HEPES. CRYSTALLIZATION SAMPLE BUFFER: 0.01M TRIS PH 8.0,       
REMARK 280  0.5M SODIUM CHLORIDE, 0.005M MAGNESIUM CHLORIDE, 0.01M DTT,         
REMARK 280  0.003M HEMICHOLINIUM-3, 0.005M ADP., VAPOR DIFFUSION,               
REMARK 280  TEMPERATURE 291K, PH 7.5                                            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       27.90100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.51950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       59.49300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.51950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.90100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       59.49300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -109.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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    57                                                      
REMARK 465     SER A    58                                                      
REMARK 465     SER A    59                                                      
REMARK 465     HIS A    60                                                      
REMARK 465     HIS A    61                                                      
REMARK 465     HIS A    62                                                      
REMARK 465     HIS A    63                                                      
REMARK 465     HIS A    64                                                      
REMARK 465     HIS A    65                                                      
REMARK 465     SER A    66                                                      
REMARK 465     SER A    67                                                      
REMARK 465     GLY A    68                                                      
REMARK 465     LEU A    69                                                      
REMARK 465     VAL A    70                                                      
REMARK 465     PRO A    71                                                      
REMARK 465     ARG A    72                                                      
REMARK 465     GLY A    73                                                      
REMARK 465     SER A    74                                                      
REMARK 465     PRO A    75                                                      
REMARK 465     GLN A    76                                                      
REMARK 465     PRO A    77                                                      
REMARK 465     PRO A    78                                                      
REMARK 465     ALA A    79                                                      
REMARK 465     ASP A    80                                                      
REMARK 465     ILE A   151                                                      
REMARK 465     LEU A   152                                                      
REMARK 465     GLN A   153                                                      
REMARK 465     MET A   154                                                      
REMARK 465     ARG A   155                                                      
REMARK 465     SER A   156                                                      
REMARK 465     CYS A   157                                                      
REMARK 465     ASN A   158                                                      
REMARK 465     LYS A   159                                                      
REMARK 465     GLU A   160                                                      
REMARK 465     GLY A   161                                                      
REMARK 465     SER A   162                                                      
REMARK 465     GLU A   163                                                      
REMARK 465     GLN A   164                                                      
REMARK 465     ALA A   165                                                      
REMARK 465     GLN A   166                                                      
REMARK 465     LYS A   167                                                      
REMARK 465     GLU A   168                                                      
REMARK 465     ASN A   169                                                      
REMARK 465     GLU A   170                                                      
REMARK 465     PHE A   171                                                      
REMARK 465     GLN A   172                                                      
REMARK 465     GLY A   173                                                      
REMARK 465     GLY B    57                                                      
REMARK 465     SER B    58                                                      
REMARK 465     SER B    59                                                      
REMARK 465     HIS B    60                                                      
REMARK 465     HIS B    61                                                      
REMARK 465     HIS B    62                                                      
REMARK 465     HIS B    63                                                      
REMARK 465     HIS B    64                                                      
REMARK 465     HIS B    65                                                      
REMARK 465     SER B    66                                                      
REMARK 465     SER B    67                                                      
REMARK 465     GLY B    68                                                      
REMARK 465     LEU B    69                                                      
REMARK 465     VAL B    70                                                      
REMARK 465     PRO B    71                                                      
REMARK 465     ARG B    72                                                      
REMARK 465     GLY B    73                                                      
REMARK 465     SER B    74                                                      
REMARK 465     PRO B    75                                                      
REMARK 465     GLN B    76                                                      
REMARK 465     PRO B    77                                                      
REMARK 465     PRO B    78                                                      
REMARK 465     ALA B    79                                                      
REMARK 465     ASP B    80                                                      
REMARK 465     GLU B    81                                                      
REMARK 465     GLN B    82                                                      
REMARK 465     PRO B    83                                                      
REMARK 465     GLU B    84                                                      
REMARK 465     PRO B    85                                                      
REMARK 465     ARG B    86                                                      
REMARK 465     THR B    87                                                      
REMARK 465     GLY B   101                                                      
REMARK 465     ARG B   104                                                      
REMARK 465     GLY B   105                                                      
REMARK 465     LEU B   106                                                      
REMARK 465     ARG B   107                                                      
REMARK 465     GLU B   108                                                      
REMARK 465     ASP B   109                                                      
REMARK 465     GLU B   110                                                      
REMARK 465     PHE B   111                                                      
REMARK 465     HIS B   112                                                      
REMARK 465     ILE B   113                                                      
REMARK 465     SER B   114                                                      
REMARK 465     VAL B   115                                                      
REMARK 465     ILE B   116                                                      
REMARK 465     ARG B   117                                                      
REMARK 465     GLY B   118                                                      
REMARK 465     GLY B   119                                                      
REMARK 465     LEU B   120                                                      
REMARK 465     SER B   121                                                      
REMARK 465     ASN B   122                                                      
REMARK 465     SER B   128                                                      
REMARK 465     LEU B   129                                                      
REMARK 465     PRO B   130                                                      
REMARK 465     ASP B   131                                                      
REMARK 465     THR B   132                                                      
REMARK 465     THR B   133                                                      
REMARK 465     ALA B   134                                                      
REMARK 465     THR B   135                                                      
REMARK 465     LEU B   136                                                      
REMARK 465     GLY B   137                                                      
REMARK 465     ASP B   138                                                      
REMARK 465     GLU B   139                                                      
REMARK 465     PRO B   140                                                      
REMARK 465     ARG B   141                                                      
REMARK 465     LYS B   142                                                      
REMARK 465     TYR B   148                                                      
REMARK 465     GLY B   149                                                      
REMARK 465     ALA B   150                                                      
REMARK 465     ILE B   151                                                      
REMARK 465     LEU B   152                                                      
REMARK 465     GLN B   153                                                      
REMARK 465     MET B   154                                                      
REMARK 465     ARG B   155                                                      
REMARK 465     SER B   156                                                      
REMARK 465     CYS B   157                                                      
REMARK 465     ASN B   158                                                      
REMARK 465     LYS B   159                                                      
REMARK 465     GLU B   160                                                      
REMARK 465     GLY B   161                                                      
REMARK 465     SER B   162                                                      
REMARK 465     GLU B   163                                                      
REMARK 465     GLN B   164                                                      
REMARK 465     ALA B   165                                                      
REMARK 465     GLN B   166                                                      
REMARK 465     LYS B   167                                                      
REMARK 465     GLU B   168                                                      
REMARK 465     ASN B   169                                                      
REMARK 465     GLU B   170                                                      
REMARK 465     PHE B   171                                                      
REMARK 465     GLN B   172                                                      
REMARK 465     GLY B   173                                                      
REMARK 465     ALA B   174                                                      
REMARK 465     GLU B   175                                                      
REMARK 465     ALA B   176                                                      
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  81    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  89    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  90    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 142    CG   CD   CE   NZ                                   
REMARK 470     GLU A 175    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 195    CD   CE   NZ                                        
REMARK 470     ARG A 213    NE   CZ   NH1  NH2                                  
REMARK 470     GLU A 217    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 230    CD   OE1  OE2                                       
REMARK 470     LYS A 239    CD   CE   NZ                                        
REMARK 470     LYS A 255    CD   CE   NZ                                        
REMARK 470     LYS A 258    CG   CD   CE   NZ                                   
REMARK 470     GLU A 259    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 262    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 272    CG   CD   CE   NZ                                   
REMARK 470     GLU A 294    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 320    CG   OD1  ND2                                       
REMARK 470     GLU A 357    CD   OE1  OE2                                       
REMARK 470     LYS A 358    CG   CD   CE   NZ                                   
REMARK 470     ARG A 363    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 388    CG   OD1  ND2                                       
REMARK 470     GLU A 391    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 403    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  88    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  89    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  90    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  96    CG   CD   CE   NZ                                   
REMARK 470     LEU B 147    CG   CD1  CD2                                       
REMARK 470     GLU B 180    CD   OE1  OE2                                       
REMARK 470     LYS B 195    CE   NZ                                             
REMARK 470     ARG B 213    NE   CZ   NH1  NH2                                  
REMARK 470     LYS B 264    CD   CE   NZ                                        
REMARK 470     GLU B 268    CD   OE1  OE2                                       
REMARK 470     LYS B 272    CD   CE   NZ                                        
REMARK 470     GLU B 322    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 357    CD   OE1  OE2                                       
REMARK 470     LYS B 358    CE   NZ                                             
REMARK 470     ARG B 367    NE   CZ   NH1  NH2                                  
REMARK 470     LYS B 368    CD   CE   NZ                                        
REMARK 470     LYS B 373    CE   NZ                                             
REMARK 470     ASN B 388    CG   OD1  ND2                                       
REMARK 470     GLU B 397    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 454    CE   NZ                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CD2  LEU B   192     CE   MET B   238              1.98            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 211      170.31    178.24                                   
REMARK 500    PRO A 241       44.17    -80.49                                   
REMARK 500    ASN A 281       76.67     54.02                                   
REMARK 500    ASN A 305       -1.50     79.18                                   
REMARK 500    ASP A 306       47.74   -155.21                                   
REMARK 500    ASP A 330       77.39     70.17                                   
REMARK 500    SER B 211      173.38    179.30                                   
REMARK 500    PRO B 241       45.35    -83.76                                   
REMARK 500    ASP B 306       47.75   -157.91                                   
REMARK 500    GLN B 324       57.92   -140.57                                   
REMARK 500    ASP B 330       82.51     66.48                                   
REMARK 500    PHE B 435      145.68   -172.43                                   
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 605  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A  39   O                                                      
REMARK 620 2 ASP A 330   OD1  68.7                                              
REMARK 620 3 ASP A 330   OD2  66.4  52.5                                        
REMARK 620 4 GLU A 332   OE2 105.1 152.0  99.7                                  
REMARK 620 5 ADP A 601   O1B 149.5  84.9  85.7  91.0                            
REMARK 620 6 SO4 A 604   O4   88.5  92.7 141.9 114.8 108.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 602  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A  49   O                                                      
REMARK 620 2 ASN A 311   OD1  84.7                                              
REMARK 620 3 ASP A 330   OD1 173.3  88.6                                        
REMARK 620 4 ADP A 601   O2B  89.6 174.3  97.1                                  
REMARK 620 5 ADP A 601   O2A  89.0  89.7  90.9  89.9                            
REMARK 620 6 SO4 A 604   O2   91.8  88.7  88.1  91.8 178.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 605  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B   1   O                                                      
REMARK 620 2 ASP B 330   OD2  76.8                                              
REMARK 620 3 ASP B 330   OD1  69.6  55.2                                        
REMARK 620 4 GLU B 332   OE2 100.4 163.9 108.8                                  
REMARK 620 5 ADP B 601   O3B 158.3  84.0  91.1  95.2                            
REMARK 620 6 SO4 B 604   O3   87.0  91.1 141.9 104.7 103.6                      
REMARK 620 N                    1     2     3     4     5                       
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 HOH B   2   O                                                      
REMARK 620 2 ASN B 311   OD1  87.1                                              
REMARK 620 3 ASP B 330   OD2 174.8  87.9                                        
REMARK 620 4 ADP B 601   O1B  91.0 173.3  94.1                                  
REMARK 620 5 ADP B 601   O2A  88.5  89.4  92.7  84.1                            
REMARK 620 6 SO4 B 604   O2   87.6  93.5  91.5  92.8 174.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HC6 A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 605                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 3                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 4                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 12                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 13                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 14                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 16                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 17                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 19                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX A 20                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HC6 B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 605                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 5                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 6                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 7                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 8                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 9                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 10                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 15                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNX B 18                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3F2S   RELATED DB: PDB                                   
REMARK 900 SUPERSEDES PDB ENTRY 3F2S.                                           
DBREF  3G15 A   75   457  UNP    P35790   CHKA_HUMAN      75    457             
DBREF  3G15 B   75   457  UNP    P35790   CHKA_HUMAN      75    457             
SEQADV 3G15 GLY A   57  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 SER A   58  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 SER A   59  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 HIS A   60  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 HIS A   61  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 HIS A   62  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 HIS A   63  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 HIS A   64  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 HIS A   65  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 SER A   66  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 SER A   67  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 GLY A   68  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 LEU A   69  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 VAL A   70  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 PRO A   71  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 ARG A   72  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 GLY A   73  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 SER A   74  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 MET A  154  UNP  P35790    VAL   154 VARIANT                        
SEQADV 3G15 SER A  220  UNP  P35790    GLY   220 VARIANT                        
SEQADV 3G15 LEU A  422  UNP  P35790    GLN   422 VARIANT                        
SEQADV 3G15 GLY B   57  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 SER B   58  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 SER B   59  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 HIS B   60  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 HIS B   61  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 HIS B   62  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 HIS B   63  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 HIS B   64  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 HIS B   65  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 SER B   66  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 SER B   67  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 GLY B   68  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 LEU B   69  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 VAL B   70  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 PRO B   71  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 ARG B   72  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 GLY B   73  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 SER B   74  UNP  P35790              EXPRESSION TAG                 
SEQADV 3G15 MET B  154  UNP  P35790    VAL   154 VARIANT                        
SEQADV 3G15 SER B  220  UNP  P35790    GLY   220 VARIANT                        
SEQADV 3G15 LEU B  422  UNP  P35790    GLN   422 VARIANT                        
SEQRES   1 A  401  GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU          
SEQRES   2 A  401  VAL PRO ARG GLY SER PRO GLN PRO PRO ALA ASP GLU GLN          
SEQRES   3 A  401  PRO GLU PRO ARG THR ARG ARG ARG ALA TYR LEU TRP CYS          
SEQRES   4 A  401  LYS GLU PHE LEU PRO GLY ALA TRP ARG GLY LEU ARG GLU          
SEQRES   5 A  401  ASP GLU PHE HIS ILE SER VAL ILE ARG GLY GLY LEU SER          
SEQRES   6 A  401  ASN MET LEU PHE GLN CYS SER LEU PRO ASP THR THR ALA          
SEQRES   7 A  401  THR LEU GLY ASP GLU PRO ARG LYS VAL LEU LEU ARG LEU          
SEQRES   8 A  401  TYR GLY ALA ILE LEU GLN MET ARG SER CYS ASN LYS GLU          
SEQRES   9 A  401  GLY SER GLU GLN ALA GLN LYS GLU ASN GLU PHE GLN GLY          
SEQRES  10 A  401  ALA GLU ALA MET VAL LEU GLU SER VAL MET PHE ALA ILE          
SEQRES  11 A  401  LEU ALA GLU ARG SER LEU GLY PRO LYS LEU TYR GLY ILE          
SEQRES  12 A  401  PHE PRO GLN GLY ARG LEU GLU GLN PHE ILE PRO SER ARG          
SEQRES  13 A  401  ARG LEU ASP THR GLU GLU LEU SER LEU PRO ASP ILE SER          
SEQRES  14 A  401  ALA GLU ILE ALA GLU LYS MET ALA THR PHE HIS GLY MET          
SEQRES  15 A  401  LYS MET PRO PHE ASN LYS GLU PRO LYS TRP LEU PHE GLY          
SEQRES  16 A  401  THR MET GLU LYS TYR LEU LYS GLU VAL LEU ARG ILE LYS          
SEQRES  17 A  401  PHE THR GLU GLU SER ARG ILE LYS LYS LEU HIS LYS LEU          
SEQRES  18 A  401  LEU SER TYR ASN LEU PRO LEU GLU LEU GLU ASN LEU ARG          
SEQRES  19 A  401  SER LEU LEU GLU SER THR PRO SER PRO VAL VAL PHE CYS          
SEQRES  20 A  401  HIS ASN ASP CYS GLN GLU GLY ASN ILE LEU LEU LEU GLU          
SEQRES  21 A  401  GLY ARG GLU ASN SER GLU LYS GLN LYS LEU MET LEU ILE          
SEQRES  22 A  401  ASP PHE GLU TYR SER SER TYR ASN TYR ARG GLY PHE ASP          
SEQRES  23 A  401  ILE GLY ASN HIS PHE CYS GLU TRP MET TYR ASP TYR SER          
SEQRES  24 A  401  TYR GLU LYS TYR PRO PHE PHE ARG ALA ASN ILE ARG LYS          
SEQRES  25 A  401  TYR PRO THR LYS LYS GLN GLN LEU HIS PHE ILE SER SER          
SEQRES  26 A  401  TYR LEU PRO ALA PHE GLN ASN ASP PHE GLU ASN LEU SER          
SEQRES  27 A  401  THR GLU GLU LYS SER ILE ILE LYS GLU GLU MET LEU LEU          
SEQRES  28 A  401  GLU VAL ASN ARG PHE ALA LEU ALA SER HIS PHE LEU TRP          
SEQRES  29 A  401  GLY LEU TRP SER ILE VAL GLN ALA LYS ILE SER SER ILE          
SEQRES  30 A  401  GLU PHE GLY TYR MET ASP TYR ALA GLN ALA ARG PHE ASP          
SEQRES  31 A  401  ALA TYR PHE HIS GLN LYS ARG LYS LEU GLY VAL                  
SEQRES   1 B  401  GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU          
SEQRES   2 B  401  VAL PRO ARG GLY SER PRO GLN PRO PRO ALA ASP GLU GLN          
SEQRES   3 B  401  PRO GLU PRO ARG THR ARG ARG ARG ALA TYR LEU TRP CYS          
SEQRES   4 B  401  LYS GLU PHE LEU PRO GLY ALA TRP ARG GLY LEU ARG GLU          
SEQRES   5 B  401  ASP GLU PHE HIS ILE SER VAL ILE ARG GLY GLY LEU SER          
SEQRES   6 B  401  ASN MET LEU PHE GLN CYS SER LEU PRO ASP THR THR ALA          
SEQRES   7 B  401  THR LEU GLY ASP GLU PRO ARG LYS VAL LEU LEU ARG LEU          
SEQRES   8 B  401  TYR GLY ALA ILE LEU GLN MET ARG SER CYS ASN LYS GLU          
SEQRES   9 B  401  GLY SER GLU GLN ALA GLN LYS GLU ASN GLU PHE GLN GLY          
SEQRES  10 B  401  ALA GLU ALA MET VAL LEU GLU SER VAL MET PHE ALA ILE          
SEQRES  11 B  401  LEU ALA GLU ARG SER LEU GLY PRO LYS LEU TYR GLY ILE          
SEQRES  12 B  401  PHE PRO GLN GLY ARG LEU GLU GLN PHE ILE PRO SER ARG          
SEQRES  13 B  401  ARG LEU ASP THR GLU GLU LEU SER LEU PRO ASP ILE SER          
SEQRES  14 B  401  ALA GLU ILE ALA GLU LYS MET ALA THR PHE HIS GLY MET          
SEQRES  15 B  401  LYS MET PRO PHE ASN LYS GLU PRO LYS TRP LEU PHE GLY          
SEQRES  16 B  401  THR MET GLU LYS TYR LEU LYS GLU VAL LEU ARG ILE LYS          
SEQRES  17 B  401  PHE THR GLU GLU SER ARG ILE LYS LYS LEU HIS LYS LEU          
SEQRES  18 B  401  LEU SER TYR ASN LEU PRO LEU GLU LEU GLU ASN LEU ARG          
SEQRES  19 B  401  SER LEU LEU GLU SER THR PRO SER PRO VAL VAL PHE CYS          
SEQRES  20 B  401  HIS ASN ASP CYS GLN GLU GLY ASN ILE LEU LEU LEU GLU          
SEQRES  21 B  401  GLY ARG GLU ASN SER GLU LYS GLN LYS LEU MET LEU ILE          
SEQRES  22 B  401  ASP PHE GLU TYR SER SER TYR ASN TYR ARG GLY PHE ASP          
SEQRES  23 B  401  ILE GLY ASN HIS PHE CYS GLU TRP MET TYR ASP TYR SER          
SEQRES  24 B  401  TYR GLU LYS TYR PRO PHE PHE ARG ALA ASN ILE ARG LYS          
SEQRES  25 B  401  TYR PRO THR LYS LYS GLN GLN LEU HIS PHE ILE SER SER          
SEQRES  26 B  401  TYR LEU PRO ALA PHE GLN ASN ASP PHE GLU ASN LEU SER          
SEQRES  27 B  401  THR GLU GLU LYS SER ILE ILE LYS GLU GLU MET LEU LEU          
SEQRES  28 B  401  GLU VAL ASN ARG PHE ALA LEU ALA SER HIS PHE LEU TRP          
SEQRES  29 B  401  GLY LEU TRP SER ILE VAL GLN ALA LYS ILE SER SER ILE          
SEQRES  30 B  401  GLU PHE GLY TYR MET ASP TYR ALA GLN ALA ARG PHE ASP          
SEQRES  31 B  401  ALA TYR PHE HIS GLN LYS ARG LYS LEU GLY VAL                  
HET    ADP  A 601      27                                                       
HET     MG  A 602       1                                                       
HET    HC6  A 603      30                                                       
HET    SO4  A 604       5                                                       
HET     MG  A 605       1                                                       
HET    UNX  A 606       1                                                       
HET    UNX  A   1       1                                                       
HET    UNX  A   2       1                                                       
HET    UNX  A   3       1                                                       
HET    UNX  A   4       1                                                       
HET    UNX  A  12       1                                                       
HET    UNX  A  13       1                                                       
HET    UNX  A  14       1                                                       
HET    UNX  A  16       1                                                       
HET    UNX  A  17       1                                                       
HET    UNX  A  19       1                                                       
HET    UNX  A  20       1                                                       
HET    ADP  B 601      27                                                       
HET     MG  B 602       1                                                       
HET    HC6  B 603      30                                                       
HET    SO4  B 604       5                                                       
HET     MG  B 605       1                                                       
HET    UNX  B 606       1                                                       
HET    UNX  B   5       1                                                       
HET    UNX  B   6       1                                                       
HET    UNX  B   7       1                                                       
HET    UNX  B   8       1                                                       
HET    UNX  B   9       1                                                       
HET    UNX  B  10       1                                                       
HET    UNX  B  15       1                                                       
HET    UNX  B  18       1                                                       
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     HC6 (2S,2'S)-2,2'-BIPHENYL-4,4'-DIYLBIS(2-HYDROXY-4,4-               
HETNAM   2 HC6  DIMETHYLMORPHOLIN-4-IUM)                                        
HETNAM     SO4 SULFATE ION                                                      
HETNAM     UNX UNKNOWN ATOM OR ION                                              
FORMUL   3  ADP    2(C10 H15 N5 O10 P2)                                         
FORMUL   4   MG    4(MG 2+)                                                     
FORMUL   5  HC6    2(C24 H34 N2 O4 2+)                                          
FORMUL   6  SO4    2(O4 S 2-)                                                   
FORMUL   8  UNX    21(X)                                                        
FORMUL  34  HOH   *324(H2 O)                                                    
HELIX    1   1 GLU A   84  LEU A   99  1                                  16    
HELIX    2   2 PRO A  100  ARG A  104  5                                   5    
HELIX    3   3 ARG A  107  PHE A  111  5                                   5    
HELIX    4   4 ALA A  174  ARG A  190  1                                  17    
HELIX    5   5 ASP A  215  SER A  220  5                                   6    
HELIX    6   6 LEU A  221  GLY A  237  1                                  17    
HELIX    7   7 LYS A  247  ILE A  263  1                                  17    
HELIX    8   8 GLU A  267  SER A  279  1                                  13    
HELIX    9   9 ASN A  281  SER A  295  1                                  15    
HELIX   10  10 GLN A  308  GLY A  310  5                                   3    
HELIX   11  11 GLY A  317  SER A  321  5                                   5    
HELIX   12  12 ARG A  339  TRP A  350  1                                  12    
HELIX   13  13 ILE A  366  TYR A  369  5                                   4    
HELIX   14  14 THR A  371  GLN A  387  1                                  17    
HELIX   15  15 ASN A  388  LEU A  393  5                                   6    
HELIX   16  16 SER A  394  SER A  431  1                                  38    
HELIX   17  17 GLY A  436  VAL A  457  1                                  22    
HELIX   18  18 ARG B   88  LEU B   99  1                                  12    
HELIX   19  19 MET B  177  ARG B  190  1                                  14    
HELIX   20  20 ASP B  215  SER B  220  5                                   6    
HELIX   21  21 LEU B  221  GLY B  237  1                                  17    
HELIX   22  22 LYS B  247  LEU B  261  1                                  15    
HELIX   23  23 GLU B  267  SER B  279  1                                  13    
HELIX   24  24 ASN B  281  SER B  295  1                                  15    
HELIX   25  25 GLN B  308  GLY B  310  5                                   3    
HELIX   26  26 ARG B  339  TRP B  350  1                                  12    
HELIX   27  27 ILE B  366  TYR B  369  5                                   4    
HELIX   28  28 THR B  371  GLN B  387  1                                  17    
HELIX   29  29 ASP B  389  LEU B  393  5                                   5    
HELIX   30  30 SER B  394  SER B  431  1                                  38    
HELIX   31  31 GLY B  436  GLY B  456  1                                  21    
SHEET    1   A 5 HIS A 112  ARG A 117  0                                        
SHEET    2   A 5 SER A 121  SER A 128 -1  O  LEU A 124   N  ILE A 116           
SHEET    3   A 5 LYS A 142  GLY A 149 -1  O  LEU A 145   N  PHE A 125           
SHEET    4   A 5 GLY A 203  GLN A 207 -1  O  GLU A 206   N  LEU A 144           
SHEET    5   A 5 LEU A 196  PHE A 200 -1  N  TYR A 197   O  LEU A 205           
SHEET    1   B 3 SER A 211  ARG A 213  0                                        
SHEET    2   B 3 ILE A 312  LEU A 315 -1  O  LEU A 314   N  ARG A 212           
SHEET    3   B 3 LEU A 326  LEU A 328 -1  O  MET A 327   N  LEU A 313           
SHEET    1   C 2 VAL A 300  CYS A 303  0                                        
SHEET    2   C 2 SER A 335  TYR A 338 -1  O  SER A 335   N  CYS A 303           
SHEET    1   D 2 TYR A 352  ASP A 353  0                                        
SHEET    2   D 2 ARG A 363  ALA A 364 -1  O  ARG A 363   N  ASP A 353           
SHEET    1   E 4 LEU B 124  PHE B 125  0                                        
SHEET    2   E 4 LEU B 144  ARG B 146 -1  O  LEU B 145   N  PHE B 125           
SHEET    3   E 4 GLY B 203  GLU B 206 -1  O  GLU B 206   N  LEU B 144           
SHEET    4   E 4 LEU B 196  PHE B 200 -1  N  TYR B 197   O  LEU B 205           
SHEET    1   F 3 SER B 211  ARG B 213  0                                        
SHEET    2   F 3 ILE B 312  LEU B 315 -1  O  LEU B 314   N  ARG B 212           
SHEET    3   F 3 LEU B 326  LEU B 328 -1  O  MET B 327   N  LEU B 313           
SHEET    1   G 2 VAL B 300  CYS B 303  0                                        
SHEET    2   G 2 SER B 335  TYR B 338 -1  O  ASN B 337   N  VAL B 301           
SHEET    1   H 2 TYR B 352  ASP B 353  0                                        
SHEET    2   H 2 ARG B 363  ALA B 364 -1  O  ARG B 363   N  ASP B 353           
LINK         O   HOH A  39                MG    MG A 605     1555   1555  2.57  
LINK         O   HOH A  49                MG    MG A 602     1555   1555  2.15  
LINK         OD1 ASN A 311                MG    MG A 602     1555   1555  2.09  
LINK         OD1 ASP A 330                MG    MG A 602     1555   1555  2.11  
LINK         OD1 ASP A 330                MG    MG A 605     1555   1555  2.24  
LINK         OD2 ASP A 330                MG    MG A 605     1555   1555  2.68  
LINK         OE2 GLU A 332                MG    MG A 605     1555   1555  1.74  
LINK         O2B ADP A 601                MG    MG A 602     1555   1555  2.05  
LINK         O2A ADP A 601                MG    MG A 602     1555   1555  2.06  
LINK         O1B ADP A 601                MG    MG A 605     1555   1555  2.11  
LINK        MG    MG A 602                 O2  SO4 A 604     1555   1555  2.10  
LINK         O4  SO4 A 604                MG    MG A 605     1555   1555  1.76  
LINK         O   HOH B   1                MG    MG B 605     1555   1555  2.23  
LINK         O   HOH B   2                MG    MG B 602     1555   1555  2.16  
LINK         OD1 ASN B 311                MG    MG B 602     1555   1555  2.16  
LINK         OD2 ASP B 330                MG    MG B 602     1555   1555  2.15  
LINK         OD2 ASP B 330                MG    MG B 605     1555   1555  2.22  
LINK         OD1 ASP B 330                MG    MG B 605     1555   1555  2.52  
LINK         OE2 GLU B 332                MG    MG B 605     1555   1555  1.84  
LINK         O1B ADP B 601                MG    MG B 602     1555   1555  2.07  
LINK         O2A ADP B 601                MG    MG B 602     1555   1555  2.06  
LINK         O3B ADP B 601                MG    MG B 605     1555   1555  2.14  
LINK        MG    MG B 602                 O2  SO4 B 604     1555   1555  2.21  
LINK         O3  SO4 B 604                MG    MG B 605     1555   1555  2.28  
CISPEP   1 TYR A  359    PRO A  360          0         6.06                     
CISPEP   2 TYR B  359    PRO B  360          0         8.86                     
SITE     1 AC1 18 HOH A  49  ARG A 117  LEU A 124  LEU A 144                    
SITE     2 AC1 18 ARG A 146  PRO A 194  GLN A 207  ILE A 209                    
SITE     3 AC1 18 ARG A 213  GLY A 310  ASN A 311  ILE A 329                    
SITE     4 AC1 18 ASP A 330  GLU A 332  HOH A 490   MG A 602                    
SITE     5 AC1 18 SO4 A 604   MG A 605                                          
SITE     1 AC2  6 HOH A  49  ASN A 311  ASP A 330  ADP A 601                    
SITE     2 AC2  6 SO4 A 604   MG A 605                                          
SITE     1 AC3 13 UNX A   2  ASP A 306  GLN A 308  TYR A 333                    
SITE     2 AC3 13 TYR A 354  PHE A 361  TRP A 420  TRP A 423                    
SITE     3 AC3 13 ILE A 433  GLU A 434  PHE A 435  TYR A 440                    
SITE     4 AC3 13 SO4 A 604                                                     
SITE     1 AC4 12 HOH A  39  HOH A  49  HOH A  50  ASP A 306                    
SITE     2 AC4 12 GLN A 308  ASN A 311  ASP A 330  GLU A 332                    
SITE     3 AC4 12 ADP A 601   MG A 602  HC6 A 603   MG A 605                    
SITE     1 AC5  6 HOH A  39  ASP A 330  GLU A 332  ADP A 601                    
SITE     2 AC5  6  MG A 602  SO4 A 604                                          
SITE     1 AC6  3 GLU A 309  GLU A 349  TYR A 352                               
SITE     1 AC7  3 PRO A  85  ARG A  86  ASN B 365                               
SITE     1 AC8  4 TYR A 354  TYR A 356  PHE A 361  HC6 A 603                    
SITE     1 AC9  3 UNX A   4  TYR A 437  MET A 438                               
SITE     1 BC1  7 UNX A   3  LYS A 273  TYR A 359  GLY A 436                    
SITE     2 BC1  7 TYR A 437  MET A 438  ASP A 439                               
SITE     1 BC2  5 TYR A 148  MET A 177  ILE A 199  PHE A 200                    
SITE     2 BC2  5 GLY A 203                                                     
SITE     1 BC3  7 HIS A 304  ASP A 306  ASP A 330  PHE A 331                    
SITE     2 BC3  7 GLU A 332  TYR A 333  SER A 334                               
SITE     1 BC4  3 PRO A  83  GLU A  84  THR A  87                               
SITE     1 BC5  4 PHE A 184  ALA A 188  GLY A 193  PRO A 194                    
SITE     1 BC6  4 ASP A 215  THR A 216  GLU A 217  HOH A 532                    
SITE     1 BC7  2 LEU A 455  HOH A 471                                          
SITE     1 BC8  1 ARG A 104                                                     
SITE     1 BC9 19 HOH B   2  LEU B 124  LEU B 144  ARG B 146                    
SITE     2 BC9 19 PRO B 194  GLN B 207  PHE B 208  ILE B 209                    
SITE     3 BC9 19 GLY B 310  ASN B 311  ILE B 329  ASP B 330                    
SITE     4 BC9 19 GLU B 332  HOH B 488  HOH B 501  HOH B 557                    
SITE     5 BC9 19  MG B 602  SO4 B 604   MG B 605                               
SITE     1 CC1  5 HOH B   2  ASN B 311  ASP B 330  ADP B 601                    
SITE     2 CC1  5 SO4 B 604                                                     
SITE     1 CC2 11 ASP B 306  TYR B 333  TYR B 354  PHE B 361                    
SITE     2 CC2 11 TRP B 420  TRP B 423  ILE B 433  GLU B 434                    
SITE     3 CC2 11 PHE B 435  TYR B 440  SO4 B 604                               
SITE     1 CC3 11 HOH B   2  ASP B 306  GLN B 308  ASN B 311                    
SITE     2 CC3 11 ASP B 330  GLU B 332  HOH B 549  ADP B 601                    
SITE     3 CC3 11  MG B 602  HC6 B 603   MG B 605                               
SITE     1 CC4  5 HOH B   1  ASP B 330  GLU B 332  ADP B 601                    
SITE     2 CC4  5 SO4 B 604                                                     
SITE     1 CC5  3 GLU B 309  GLU B 349  TYR B 352                               
SITE     1 CC6  2 ARG B 212  ARG B 213                                          
SITE     1 CC7  2 PRO B 222  ASP B 223                                          
SITE     1 CC8  4 PHE B 265  THR B 266  GLU B 267  ARG B 270                    
SITE     1 CC9  2 PHE B 265  ILE B 271                                          
SITE     1 DC1  3 ARG B 270  TYR B 437  MET B 438                               
SITE     1 DC2  3 ARG A  86  THR A  87  ASN B 365                               
SITE     1 DC3  2 PRO B 246  PHE B 250                                          
SITE     1 DC4  2 TYR B 356  GLU B 357                                          
CRYST1   55.802  118.986  131.039  90.00  90.00  90.00 P 21 21 21    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      0.017921  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008404  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007631        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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