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Database: PDB
Entry: 1CM8
LinkDB: 1CM8
Original site: 1CM8 
HEADER    TRANSFERASE                             17-MAY-99   1CM8              
TITLE     PHOSPHORYLATED MAP KINASE P38-GAMMA                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHORYLATED MAP KINASE P38-GAMMA;                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: STRESS-ACTIVATED PROTEIN KINASE-3, ERK6, ERK5;              
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    P38-GAMMA, GAMMA, PHOSPHORYLATION, MAP KINASE, TRANSFERASE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.BELLON,M.J.FITZGIBBON,T.FOX,H.M.HSIAO,K.P.WILSON                    
REVDAT   2   24-FEB-09 1CM8    1       VERSN                                    
REVDAT   1   17-MAY-00 1CM8    0                                                
JRNL        AUTH   S.BELLON,M.J.FITZGIBBON,T.FOX,H.M.HSIAO,K.P.WILSON           
JRNL        TITL   THE STRUCTURE OF PHOSPHORYLATED P38GAMMA IS                  
JRNL        TITL 2 MONOMERIC AND REVEALS A CONSERVED ACTIVATION-LOOP            
JRNL        TITL 3 CONFORMATION.                                                
JRNL        REF    STRUCTURE FOLD.DES.           V.   7  1057 1999              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   10508788                                                     
JRNL        DOI    10.1016/S0969-2126(99)80173-7                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.2                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 79.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 27840                          
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 SET) : 0.232                           
REMARK   3   FREE R VALUE                     : 0.283                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2768                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5190                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 66                                      
REMARK   3   SOLVENT ATOMS            : 186                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.010                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.60                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : RESTRAINTS                                              
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:  THE DATA ARE EXTREMELY ANISOTROPIC.      
REMARK   3  THIS RESULTED IN LESS THAN 100% COMPLETENESS FOR THE NATIVE         
REMARK   3  DATA.                                                               
REMARK   4                                                                      
REMARK   4 1CM8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB001073.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 110                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X25                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.100                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31732                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
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     (%) : 89.9                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 6.70000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0, VAPOR DIFFUSION                  
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       31.75000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      103.01000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.41000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      103.01000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.75000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.41000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     PRO A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     GLY A    34                                                      
REMARK 465     SER A    35                                                      
REMARK 465     GLY A    36                                                      
REMARK 465     ALA A    37                                                      
REMARK 465     TYR A    38                                                      
REMARK 465     GLY A    39                                                      
REMARK 465     ASP A   316                                                      
REMARK 465     THR A   317                                                      
REMARK 465     GLU A   318                                                      
REMARK 465     ASP A   319                                                      
REMARK 465     GLU A   320                                                      
REMARK 465     PRO A   321                                                      
REMARK 465     PHE A   330                                                      
REMARK 465     ASP A   331                                                      
REMARK 465     ASP A   332                                                      
REMARK 465     VAL A   333                                                      
REMARK 465     ASP A   334                                                      
REMARK 465     PRO A   354                                                      
REMARK 465     ARG A   355                                                      
REMARK 465     GLN A   356                                                      
REMARK 465     LEU A   357                                                      
REMARK 465     GLY A   358                                                      
REMARK 465     ALA A   359                                                      
REMARK 465     ARG A   360                                                      
REMARK 465     VAL A   361                                                      
REMARK 465     SER A   362                                                      
REMARK 465     LYS A   363                                                      
REMARK 465     GLU A   364                                                      
REMARK 465     THR A   365                                                      
REMARK 465     PRO A   366                                                      
REMARK 465     LEU A   367                                                      
REMARK 465     MET B  1001                                                      
REMARK 465     SER B  1002                                                      
REMARK 465     SER B  1003                                                      
REMARK 465     PRO B  1004                                                      
REMARK 465     PRO B  1005                                                      
REMARK 465     PRO B  1006                                                      
REMARK 465     ALA B  1007                                                      
REMARK 465     GLY B  1034                                                      
REMARK 465     SER B  1035                                                      
REMARK 465     GLY B  1036                                                      
REMARK 465     ALA B  1037                                                      
REMARK 465     TYR B  1038                                                      
REMARK 465     GLY B  1039                                                      
REMARK 465     ASP B  1316                                                      
REMARK 465     THR B  1317                                                      
REMARK 465     GLU B  1318                                                      
REMARK 465     ASP B  1319                                                      
REMARK 465     GLU B  1320                                                      
REMARK 465     PRO B  1321                                                      
REMARK 465     PHE B  1330                                                      
REMARK 465     ASP B  1331                                                      
REMARK 465     ASP B  1332                                                      
REMARK 465     VAL B  1333                                                      
REMARK 465     ASP B  1334                                                      
REMARK 465     PRO B  1354                                                      
REMARK 465     ARG B  1355                                                      
REMARK 465     GLN B  1356                                                      
REMARK 465     LEU B  1357                                                      
REMARK 465     GLY B  1358                                                      
REMARK 465     ALA B  1359                                                      
REMARK 465     ARG B  1360                                                      
REMARK 465     VAL B  1361                                                      
REMARK 465     SER B  1362                                                      
REMARK 465     LYS B  1363                                                      
REMARK 465     GLU B  1364                                                      
REMARK 465     THR B  1365                                                      
REMARK 465     PRO B  1366                                                      
REMARK 465     LEU B  1367                                                      
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     ARG A   8    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  18    CG   CD   CE   NZ                                   
REMARK 470     ARG A  60    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  82    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 100    CG   OD1  OD2                                       
REMARK 470     LYS A 223    CG   CD   CE   NZ                                   
REMARK 470     LYS A 227    CG   CD   CE   NZ                                   
REMARK 470     LYS A 240    CG   CD   CE   NZ                                   
REMARK 470     GLU A 269    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 271    CG   CD   CE   NZ                                   
REMARK 470     SER A 275    OG                                                  
REMARK 470     HIS A 315    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN A 322    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 324    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 335    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 337    CG   CD1  CD2                                       
REMARK 470     ARG A 342    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A 343    CG1  CG2                                            
REMARK 470     LYS A 346    CG   CD   CE   NZ                                   
REMARK 470     LYS A 352    CG   CD   CE   NZ                                   
REMARK 470     ARG B1008    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B1018    CG   CD   CE   NZ                                   
REMARK 470     ARG B1060    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B1082    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B1100    CG   OD1  OD2                                       
REMARK 470     LYS B1223    CG   CD   CE   NZ                                   
REMARK 470     LYS B1227    CG   CD   CE   NZ                                   
REMARK 470     LYS B1240    CG   CD   CE   NZ                                   
REMARK 470     GLU B1269    CG   CD   OE1  OE2                                  
REMARK 470     LYS B1271    CG   CD   CE   NZ                                   
REMARK 470     SER B1275    OG                                                  
REMARK 470     HIS B1315    CG   ND1  CD2  CE1  NE2                             
REMARK 470     GLN B1322    CG   CD   OE1  NE2                                  
REMARK 470     GLN B1324    CG   CD   OE1  NE2                                  
REMARK 470     ARG B1335    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B1337    CG   CD1  CD2                                       
REMARK 470     ARG B1342    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B1343    CG1  CG2                                            
REMARK 470     LYS B1346    CG   CD   CE   NZ                                   
REMARK 470     LYS B1352    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  13   CD  -  NE  -  CZ  ANGL. DEV. =  15.8 DEGREES          
REMARK 500    ARG A  13   NE  -  CZ  -  NH1 ANGL. DEV. =   8.6 DEGREES          
REMARK 500    ARG A  13   NE  -  CZ  -  NH2 ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    ARG A 129   CD  -  NE  -  CZ  ANGL. DEV. =  15.5 DEGREES          
REMARK 500    ARG A 129   NE  -  CZ  -  NH1 ANGL. DEV. =   9.3 DEGREES          
REMARK 500    ARG A 129   NE  -  CZ  -  NH2 ANGL. DEV. =  -9.2 DEGREES          
REMARK 500    ARG B1013   CD  -  NE  -  CZ  ANGL. DEV. =  15.8 DEGREES          
REMARK 500    ARG B1013   NE  -  CZ  -  NH1 ANGL. DEV. =   9.3 DEGREES          
REMARK 500    ARG B1013   NE  -  CZ  -  NH2 ANGL. DEV. = -10.0 DEGREES          
REMARK 500    ARG B1129   CD  -  NE  -  CZ  ANGL. DEV. =  15.3 DEGREES          
REMARK 500    ARG B1129   NE  -  CZ  -  NH1 ANGL. DEV. =   9.3 DEGREES          
REMARK 500    ARG B1129   NE  -  CZ  -  NH2 ANGL. DEV. =  -9.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A  16      -91.59    -91.97                                   
REMARK 500    THR A  17      -98.78    -96.41                                   
REMARK 500    PRO A  95       21.42    -78.57                                   
REMARK 500    PHE A 102       95.81    -64.67                                   
REMARK 500    LEU A 125      -81.22    -71.72                                   
REMARK 500    ASP A 153       33.00   -165.07                                   
REMARK 500    ASP A 171       82.62     49.88                                   
REMARK 500    VAL A 187      141.22     73.62                                   
REMARK 500    ASN A 199       53.93   -117.13                                   
REMARK 500    TRP A 200      125.67    -36.97                                   
REMARK 500    THR A 204     -168.40   -129.00                                   
REMARK 500    PRO A 266     -178.39    -63.73                                   
REMARK 500    VAL B1016      -91.68    -91.62                                   
REMARK 500    THR B1017      -97.65    -96.36                                   
REMARK 500    PRO B1095       21.26    -77.88                                   
REMARK 500    PHE B1102       95.72    -64.31                                   
REMARK 500    LEU B1125      -80.44    -71.98                                   
REMARK 500    ASP B1153       33.13   -163.07                                   
REMARK 500    ASP B1171       81.99     50.51                                   
REMARK 500    VAL B1187      141.25     73.12                                   
REMARK 500    ASN B1199       54.35   -117.35                                   
REMARK 500    TRP B1200      124.43    -37.10                                   
REMARK 500    THR B1204     -168.67   -128.73                                   
REMARK 500    PRO B1266     -177.81    -63.35                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B2082        DISTANCE =  6.08 ANGSTROMS                       
REMARK 525    HOH A2120        DISTANCE =  5.34 ANGSTROMS                       
REMARK 525    HOH B2084        DISTANCE =  5.46 ANGSTROMS                       
REMARK 525    HOH A2142        DISTANCE =  7.01 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 401  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 158   OD1                                                    
REMARK 620 2 HOH A2039   O   121.3                                              
REMARK 620 3 ANP A 400   O2A  86.5 149.8                                        
REMARK 620 4 ASP A 171   OD2  67.7 136.4  61.7                                  
REMARK 620 5 ANP A 400   O2G  93.6  71.7 122.0  65.0                            
REMARK 620 6 ANP A 400   N3B 132.1  94.4  71.1  64.4  66.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 171   OD1                                                    
REMARK 620 2 HOH A2152   O    83.4                                              
REMARK 620 3 HOH A2153   O    76.1 147.3                                        
REMARK 620 4 ANP A 400   O2B  95.4  67.5 138.8                                  
REMARK 620 5 ANP A 400   O3G 114.6 130.0  82.2  64.7                            
REMARK 620 6 ASP A 171   OD2  49.0 114.0  70.1  74.2  65.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1401  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP B1400   N3B                                                    
REMARK 620 2 ASN B1158   OD1 129.0                                              
REMARK 620 3 ASP B1171   OD2  62.3  66.8                                        
REMARK 620 4 ANP B1400   O2A  69.7  83.9  60.4                                  
REMARK 620 5 ANP B1400   O2G  65.1  93.8  62.6 118.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ANP B1400   O2B                                                    
REMARK 620 2 ASP B1171   OD1  95.1                                              
REMARK 620 3 ASP B1171   OD2  74.6  50.3                                        
REMARK 620 4 HOH B2118   O   148.8  80.3  79.1                                  
REMARK 620 5 ANP B1400   O3G  65.5 115.1  64.9  88.4                            
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 401                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 402                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1401                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1402                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP A 400                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP B 1400                
DBREF  1CM8 A    1   367  UNP    P53778   MK12_HUMAN       1    367             
DBREF  1CM8 B 1001  1367  UNP    P53778   MK12_HUMAN       1    367             
SEQADV 1CM8 TPO A  183  UNP  P53778    THR   183 MODIFIED RESIDUE               
SEQADV 1CM8 TPO B 1183  UNP  P53778    THR   183 MODIFIED RESIDUE               
SEQADV 1CM8 PTR A  185  UNP  P53778    TYR   185 MODIFIED RESIDUE               
SEQADV 1CM8 PTR B 1185  UNP  P53778    TYR   185 MODIFIED RESIDUE               
SEQRES   1 A  367  MET SER SER PRO PRO PRO ALA ARG SER GLY PHE TYR ARG          
SEQRES   2 A  367  GLN GLU VAL THR LYS THR ALA TRP GLU VAL ARG ALA VAL          
SEQRES   3 A  367  TYR ARG ASP LEU GLN PRO VAL GLY SER GLY ALA TYR GLY          
SEQRES   4 A  367  ALA VAL CYS SER ALA VAL ASP GLY ARG THR GLY ALA LYS          
SEQRES   5 A  367  VAL ALA ILE LYS LYS LEU TYR ARG PRO PHE GLN SER GLU          
SEQRES   6 A  367  LEU PHE ALA LYS ARG ALA TYR ARG GLU LEU ARG LEU LEU          
SEQRES   7 A  367  LYS HIS MET ARG HIS GLU ASN VAL ILE GLY LEU LEU ASP          
SEQRES   8 A  367  VAL PHE THR PRO ASP GLU THR LEU ASP ASP PHE THR ASP          
SEQRES   9 A  367  PHE TYR LEU VAL MET PRO PHE MET GLY THR ASP LEU GLY          
SEQRES  10 A  367  LYS LEU MET LYS HIS GLU LYS LEU GLY GLU ASP ARG ILE          
SEQRES  11 A  367  GLN PHE LEU VAL TYR GLN MET LEU LYS GLY LEU ARG TYR          
SEQRES  12 A  367  ILE HIS ALA ALA GLY ILE ILE HIS ARG ASP LEU LYS PRO          
SEQRES  13 A  367  GLY ASN LEU ALA VAL ASN GLU ASP CYS GLU LEU LYS ILE          
SEQRES  14 A  367  LEU ASP PHE GLY LEU ALA ARG GLN ALA ASP SER GLU MET          
SEQRES  15 A  367  TPO GLY PTR VAL VAL THR ARG TRP TYR ARG ALA PRO GLU          
SEQRES  16 A  367  VAL ILE LEU ASN TRP MET ARG TYR THR GLN THR VAL ASP          
SEQRES  17 A  367  ILE TRP SER VAL GLY CYS ILE MET ALA GLU MET ILE THR          
SEQRES  18 A  367  GLY LYS THR LEU PHE LYS GLY SER ASP HIS LEU ASP GLN          
SEQRES  19 A  367  LEU LYS GLU ILE MET LYS VAL THR GLY THR PRO PRO ALA          
SEQRES  20 A  367  GLU PHE VAL GLN ARG LEU GLN SER ASP GLU ALA LYS ASN          
SEQRES  21 A  367  TYR MET LYS GLY LEU PRO GLU LEU GLU LYS LYS ASP PHE          
SEQRES  22 A  367  ALA SER ILE LEU THR ASN ALA SER PRO LEU ALA VAL ASN          
SEQRES  23 A  367  LEU LEU GLU LYS MET LEU VAL LEU ASP ALA GLU GLN ARG          
SEQRES  24 A  367  VAL THR ALA GLY GLU ALA LEU ALA HIS PRO TYR PHE GLU          
SEQRES  25 A  367  SER LEU HIS ASP THR GLU ASP GLU PRO GLN VAL GLN LYS          
SEQRES  26 A  367  TYR ASP ASP SER PHE ASP ASP VAL ASP ARG THR LEU ASP          
SEQRES  27 A  367  GLU TRP LYS ARG VAL THR TYR LYS GLU VAL LEU SER PHE          
SEQRES  28 A  367  LYS PRO PRO ARG GLN LEU GLY ALA ARG VAL SER LYS GLU          
SEQRES  29 A  367  THR PRO LEU                                                  
SEQRES   1 B  367  MET SER SER PRO PRO PRO ALA ARG SER GLY PHE TYR ARG          
SEQRES   2 B  367  GLN GLU VAL THR LYS THR ALA TRP GLU VAL ARG ALA VAL          
SEQRES   3 B  367  TYR ARG ASP LEU GLN PRO VAL GLY SER GLY ALA TYR GLY          
SEQRES   4 B  367  ALA VAL CYS SER ALA VAL ASP GLY ARG THR GLY ALA LYS          
SEQRES   5 B  367  VAL ALA ILE LYS LYS LEU TYR ARG PRO PHE GLN SER GLU          
SEQRES   6 B  367  LEU PHE ALA LYS ARG ALA TYR ARG GLU LEU ARG LEU LEU          
SEQRES   7 B  367  LYS HIS MET ARG HIS GLU ASN VAL ILE GLY LEU LEU ASP          
SEQRES   8 B  367  VAL PHE THR PRO ASP GLU THR LEU ASP ASP PHE THR ASP          
SEQRES   9 B  367  PHE TYR LEU VAL MET PRO PHE MET GLY THR ASP LEU GLY          
SEQRES  10 B  367  LYS LEU MET LYS HIS GLU LYS LEU GLY GLU ASP ARG ILE          
SEQRES  11 B  367  GLN PHE LEU VAL TYR GLN MET LEU LYS GLY LEU ARG TYR          
SEQRES  12 B  367  ILE HIS ALA ALA GLY ILE ILE HIS ARG ASP LEU LYS PRO          
SEQRES  13 B  367  GLY ASN LEU ALA VAL ASN GLU ASP CYS GLU LEU LYS ILE          
SEQRES  14 B  367  LEU ASP PHE GLY LEU ALA ARG GLN ALA ASP SER GLU MET          
SEQRES  15 B  367  TPO GLY PTR VAL VAL THR ARG TRP TYR ARG ALA PRO GLU          
SEQRES  16 B  367  VAL ILE LEU ASN TRP MET ARG TYR THR GLN THR VAL ASP          
SEQRES  17 B  367  ILE TRP SER VAL GLY CYS ILE MET ALA GLU MET ILE THR          
SEQRES  18 B  367  GLY LYS THR LEU PHE LYS GLY SER ASP HIS LEU ASP GLN          
SEQRES  19 B  367  LEU LYS GLU ILE MET LYS VAL THR GLY THR PRO PRO ALA          
SEQRES  20 B  367  GLU PHE VAL GLN ARG LEU GLN SER ASP GLU ALA LYS ASN          
SEQRES  21 B  367  TYR MET LYS GLY LEU PRO GLU LEU GLU LYS LYS ASP PHE          
SEQRES  22 B  367  ALA SER ILE LEU THR ASN ALA SER PRO LEU ALA VAL ASN          
SEQRES  23 B  367  LEU LEU GLU LYS MET LEU VAL LEU ASP ALA GLU GLN ARG          
SEQRES  24 B  367  VAL THR ALA GLY GLU ALA LEU ALA HIS PRO TYR PHE GLU          
SEQRES  25 B  367  SER LEU HIS ASP THR GLU ASP GLU PRO GLN VAL GLN LYS          
SEQRES  26 B  367  TYR ASP ASP SER PHE ASP ASP VAL ASP ARG THR LEU ASP          
SEQRES  27 B  367  GLU TRP LYS ARG VAL THR TYR LYS GLU VAL LEU SER PHE          
SEQRES  28 B  367  LYS PRO PRO ARG GLN LEU GLY ALA ARG VAL SER LYS GLU          
SEQRES  29 B  367  THR PRO LEU                                                  
MODRES 1CM8 TPO A  183  THR  PHOSPHOTHREONINE                                   
MODRES 1CM8 PTR A  185  TYR  O-PHOSPHOTYROSINE                                  
MODRES 1CM8 TPO B 1183  THR  PHOSPHOTHREONINE                                   
MODRES 1CM8 PTR B 1185  TYR  O-PHOSPHOTYROSINE                                  
HET    TPO  A 183      11                                                       
HET    PTR  A 185      16                                                       
HET    TPO  B1183      11                                                       
HET    PTR  B1185      16                                                       
HET     MG  A 401       1                                                       
HET     MG  A 402       1                                                       
HET     MG  B1401       1                                                       
HET     MG  B1402       1                                                       
HET    ANP  A 400      31                                                       
HET    ANP  B1400      31                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     PTR PHOSPHONOTYROSINE                                                
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   1  PTR    2(C9 H12 N O6 P)                                             
FORMUL   3   MG    4(MG 2+)                                                     
FORMUL   7  ANP    2(C10 H17 N6 O12 P3)                                         
FORMUL   9  HOH   *186(H2 O)                                                    
HELIX    1   1 GLU A   65  HIS A   80  1                                  16    
HELIX    2   2 LEU A  116  HIS A  122  1                                   7    
HELIX    3   3 GLU A  127  ALA A  146  1                                  20    
HELIX    4   4 PRO A  156  ASN A  158  5                                   3    
HELIX    5   5 ARG A  189  TYR A  191  5                                   3    
HELIX    6   6 PRO A  194  LEU A  198  5                                   5    
HELIX    7   7 GLN A  205  THR A  221  5                                  17    
HELIX    8   8 HIS A  231  THR A  242  1                                  12    
HELIX    9   9 ALA A  247  ARG A  252  1                                   6    
HELIX   10  10 ASP A  256  GLY A  264  1                                   9    
HELIX   11  11 PHE A  273  SER A  275  5                                   3    
HELIX   12  12 PRO A  282  MET A  291  1                                  10    
HELIX   13  13 ALA A  302  ALA A  307  1                                   6    
HELIX   14  14 PRO A  309  PHE A  311  5                                   3    
HELIX   15  15 LEU A  337  LEU A  349  1                                  13    
HELIX   16  16 GLU B 1065  HIS B 1080  1                                  16    
HELIX   17  17 LEU B 1116  HIS B 1122  1                                   7    
HELIX   18  18 GLU B 1127  ALA B 1146  1                                  20    
HELIX   19  19 PRO B 1156  ASN B 1158  5                                   3    
HELIX   20  20 ARG B 1189  TYR B 1191  5                                   3    
HELIX   21  21 PRO B 1194  LEU B 1198  5                                   5    
HELIX   22  22 GLN B 1205  THR B 1221  5                                  17    
HELIX   23  23 HIS B 1231  THR B 1242  1                                  12    
HELIX   24  24 ALA B 1247  ARG B 1252  1                                   6    
HELIX   25  25 ASP B 1256  GLY B 1264  1                                   9    
HELIX   26  26 PHE B 1273  SER B 1275  5                                   3    
HELIX   27  27 PRO B 1282  MET B 1291  1                                  10    
HELIX   28  28 ALA B 1302  ALA B 1307  1                                   6    
HELIX   29  29 PRO B 1309  PHE B 1311  5                                   3    
HELIX   30  30 LEU B 1337  LEU B 1349  1                                  13    
SHEET    1   A 4 ALA A  40  VAL A  45  0                                        
SHEET    2   A 4 LYS A  52  LYS A  57 -1  N  LYS A  57   O  ALA A  40           
SHEET    3   A 4 TYR A 106  PRO A 110 -1  N  MET A 109   O  ALA A  54           
SHEET    4   A 4 LEU A  89  PHE A  93 -1  N  PHE A  93   O  TYR A 106           
SHEET    1   B 2 LEU A 159  VAL A 161  0                                        
SHEET    2   B 2 LEU A 167  ILE A 169 -1  N  LYS A 168   O  ALA A 160           
SHEET    1   C 4 ALA B1040  VAL B1045  0                                        
SHEET    2   C 4 LYS B1052  LYS B1057 -1  N  LYS B1057   O  ALA B1040           
SHEET    3   C 4 TYR B1106  PRO B1110 -1  N  MET B1109   O  ALA B1054           
SHEET    4   C 4 LEU B1089  PHE B1093 -1  N  PHE B1093   O  TYR B1106           
SHEET    1   D 2 LEU B1159  VAL B1161  0                                        
SHEET    2   D 2 LEU B1167  ILE B1169 -1  N  LYS B1168   O  ALA B1160           
LINK         C   MET A 182                 N   TPO A 183     1555   1555  1.33  
LINK         C   TPO A 183                 N   GLY A 184     1555   1555  1.33  
LINK         C   GLY A 184                 N   PTR A 185     1555   1555  1.33  
LINK         C   PTR A 185                 N   VAL A 186     1555   1555  1.33  
LINK        MG    MG A 401                 OD1 ASN A 158     1555   1555  2.11  
LINK        MG    MG A 401                 O   HOH A2039     1555   1555  2.91  
LINK        MG    MG A 401                 O2A ANP A 400     1555   1555  2.28  
LINK        MG    MG A 401                 OD2 ASP A 171     1555   1555  2.95  
LINK        MG    MG A 401                 O2G ANP A 400     1555   1555  2.11  
LINK        MG    MG A 401                 N3B ANP A 400     1555   1555  2.54  
LINK        MG    MG A 402                 OD1 ASP A 171     1555   1555  2.34  
LINK        MG    MG A 402                 O   HOH A2152     1555   1555  2.74  
LINK        MG    MG A 402                 O   HOH A2153     1555   1555  2.68  
LINK        MG    MG A 402                 O2B ANP A 400     1555   1555  2.60  
LINK        MG    MG A 402                 O3G ANP A 400     1555   1555  2.51  
LINK        MG    MG A 402                 OD2 ASP A 171     1555   1555  2.84  
LINK         C   MET B1182                 N   TPO B1183     1555   1555  1.33  
LINK         C   TPO B1183                 N   GLY B1184     1555   1555  1.33  
LINK         C   GLY B1184                 N   PTR B1185     1555   1555  1.33  
LINK         C   PTR B1185                 N   VAL B1186     1555   1555  1.34  
LINK        MG    MG B1401                 N3B ANP B1400     1555   1555  2.58  
LINK        MG    MG B1401                 OD1 ASN B1158     1555   1555  2.14  
LINK        MG    MG B1401                 OD2 ASP B1171     1555   1555  3.01  
LINK        MG    MG B1401                 O2A ANP B1400     1555   1555  2.34  
LINK        MG    MG B1401                 O2G ANP B1400     1555   1555  2.10  
LINK        MG    MG B1402                 O2B ANP B1400     1555   1555  2.65  
LINK        MG    MG B1402                 OD1 ASP B1171     1555   1555  2.32  
LINK        MG    MG B1402                 OD2 ASP B1171     1555   1555  2.81  
LINK        MG    MG B1402                 O   HOH B2118     1555   1555  2.62  
LINK        MG    MG B1402                 O3G ANP B1400     1555   1555  2.47  
SITE     1 AC1  4 ASN A 158  ASP A 171  ANP A 400  HOH A2039                    
SITE     1 AC2  4 ASP A 171  ANP A 400  HOH A2152  HOH A2153                    
SITE     1 AC3  3 ASN B1158  ASP B1171  ANP B1400                               
SITE     1 AC4  3 ASP B1171  ANP B1400  HOH B2118                               
SITE     1 AC5 18 VAL A  41  ALA A  54  LYS A  56  ILE A  87                    
SITE     2 AC5 18 MET A 109  PRO A 110  MET A 112  ASP A 115                    
SITE     3 AC5 18 LYS A 155  GLY A 157  ASN A 158  LEU A 170                    
SITE     4 AC5 18 ASP A 171   MG A 401   MG A 402  HOH A2039                    
SITE     5 AC5 18 HOH A2111  HOH A2152                                          
SITE     1 AC6 20 VAL B1041  ALA B1054  LYS B1056  ILE B1087                    
SITE     2 AC6 20 MET B1109  PRO B1110  MET B1112  ASP B1115                    
SITE     3 AC6 20 LYS B1155  GLY B1157  ASN B1158  LEU B1170                    
SITE     4 AC6 20 ASP B1171   MG B1401   MG B1402  HOH B2002                    
SITE     5 AC6 20 HOH B2037  HOH B2053  HOH B2185  HOH B2186                    
CRYST1   63.500   66.820  206.020  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      0.015748  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014965  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004854        0.00000                         
MTRIX1   1 -0.010500 -0.998900 -0.045400       83.90470    1                    
MTRIX2   1 -0.999900  0.010800 -0.007300       79.17460    1                    
MTRIX3   1  0.007700  0.045400 -0.998900       47.92390    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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