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Database: PDB
Entry: 3IAR
LinkDB: 3IAR
Original site: 3IAR 
HEADER    HYDROLASE                               14-JUL-09   3IAR              
TITLE     THE CRYSTAL STRUCTURE OF HUMAN ADENOSINE DEAMINASE                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ADENOSINE DEAMINASE;                                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 5-363;                                        
COMPND   5 SYNONYM: ADENOSINE AMINOHYDROLASE;                                   
COMPND   6 EC: 3.5.4.4;                                                         
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: ADA;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3-PRARE2;                       
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PNIC-CTHF                                 
KEYWDS    DEAMINASE, ADENOSINE DEAMINASE, ADENOSINE, PURINE METABOLISM,         
KEYWDS   2 STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, DISEASE    
KEYWDS   3 MUTATION, HEREDITARY HEMOLYTIC ANEMIA, HYDROLASE, NUCLEOTIDE         
KEYWDS   4 METABOLISM, SCID                                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.UGOCHUKWU,Y.ZHANG,E.HAPKA,W.W.YUE,J.E.BRAY,J.MUNIZ,N.BURGESS-BROWN, 
AUTHOR   2 A.CHAIKUAD,F.VON DELFT,C.BOUNTRA,C.H.ARROWSMITH,J.WEIGELT,A.EDWARDS, 
AUTHOR   3 K.L.KAVANAGH,U.OPPERMANN,STRUCTURAL GENOMICS CONSORTIUM (SGC)        
REVDAT   2   13-JUL-11 3IAR    1       VERSN                                    
REVDAT   1   11-AUG-09 3IAR    0                                                
JRNL        AUTH   E.UGOCHUKWU,Y.ZHANG,E.HAPKA,W.W.YUE,J.E.BRAY,J.MUNIZ,        
JRNL        AUTH 2 N.BURGESS-BROWN,A.CHAIKUAD,K.L.KAVANAGH,U.OPPERMANN          
JRNL        TITL   THE CRYSTAL STRUCTURE OF HUMAN ADENOSINE DEAMINASE           
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.52 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.52                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.70                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 52324                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.154                           
REMARK   3   R VALUE            (WORKING SET) : 0.153                           
REMARK   3   FREE R VALUE                     : 0.185                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.630                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1901                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.7035 -  3.6613    0.99     3869   143  0.1360 0.1707        
REMARK   3     2  3.6613 -  2.9069    1.00     3756   141  0.1289 0.1513        
REMARK   3     3  2.9069 -  2.5397    1.00     3740   135  0.1360 0.1640        
REMARK   3     4  2.5397 -  2.3076    1.00     3704   140  0.1341 0.1660        
REMARK   3     5  2.3076 -  2.1422    1.00     3706   142  0.1240 0.1598        
REMARK   3     6  2.1422 -  2.0160    1.00     3678   137  0.1280 0.1743        
REMARK   3     7  2.0160 -  1.9150    1.00     3655   146  0.1299 0.1796        
REMARK   3     8  1.9150 -  1.8317    1.00     3675   133  0.1334 0.2047        
REMARK   3     9  1.8317 -  1.7612    1.00     3675   134  0.1359 0.1575        
REMARK   3    10  1.7612 -  1.7004    1.00     3628   131  0.1340 0.1726        
REMARK   3    11  1.7004 -  1.6472    0.99     3645   151  0.1373 0.1645        
REMARK   3    12  1.6472 -  1.6002    0.98     3585   129  0.1495 0.1673        
REMARK   3    13  1.6002 -  1.5580    0.92     3342   134  0.1680 0.2053        
REMARK   3    14  1.5580 -  1.5200    0.76     2765   105  0.1939 0.2191        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.32                                          
REMARK   3   B_SOL              : 32.94                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.550            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.014           3020                                  
REMARK   3   ANGLE     :  1.518           4106                                  
REMARK   3   CHIRALITY :  0.098            444                                  
REMARK   3   PLANARITY :  0.009            540                                  
REMARK   3   DIHEDRAL  : 16.224           1123                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 3:74)                               
REMARK   3    ORIGIN FOR THE GROUP (A):   9.2713   7.4552  -4.6709              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0861 T22:   0.0820                                     
REMARK   3      T33:  -0.0094 T12:  -0.0044                                     
REMARK   3      T13:   0.0036 T23:  -0.0116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1280 L22:   0.0410                                     
REMARK   3      L33:   0.0419 L12:   0.0334                                     
REMARK   3      L13:   0.1902 L23:   0.0008                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0196 S12:   0.0749 S13:  -0.0133                       
REMARK   3      S21:  -0.0411 S22:   0.0249 S23:  -0.0058                       
REMARK   3      S31:  -0.0298 S32:   0.0284 S33:  -0.0048                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 75:196)                             
REMARK   3    ORIGIN FOR THE GROUP (A):   8.7735   2.2968   9.4301              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0792 T22:   0.0609                                     
REMARK   3      T33:  -0.0250 T12:   0.0009                                     
REMARK   3      T13:  -0.0148 T23:  -0.0007                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0787 L22:   0.1254                                     
REMARK   3      L33:   0.0111 L12:  -0.0322                                     
REMARK   3      L13:   0.0169 L23:  -0.0810                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0149 S12:   0.0012 S13:  -0.0046                       
REMARK   3      S21:   0.0749 S22:  -0.0198 S23:  -0.0149                       
REMARK   3      S31:  -0.0408 S32:   0.0024 S33:   0.0081                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 197:238)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.0428 -12.3661   9.2914              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0703 T22:   0.0368                                     
REMARK   3      T33:   0.0070 T12:  -0.0065                                     
REMARK   3      T13:  -0.0035 T23:   0.0079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0419 L22:  -0.1887                                     
REMARK   3      L33:   1.6956 L12:  -0.0177                                     
REMARK   3      L13:   0.7330 L23:   0.0441                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0299 S12:  -0.0331 S13:  -0.1269                       
REMARK   3      S21:   0.0275 S22:   0.0289 S23:   0.0074                       
REMARK   3      S31:  -0.0428 S32:  -0.0962 S33:  -0.0626                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 239:256)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -12.4473 -15.7957   3.1508              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0857 T22:   0.0875                                     
REMARK   3      T33:   0.0791 T12:  -0.0273                                     
REMARK   3      T13:   0.0139 T23:  -0.0155                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7238 L22:  -0.2019                                     
REMARK   3      L33:   0.8145 L12:   0.0304                                     
REMARK   3      L13:  -0.3652 L23:   0.0877                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0132 S12:   0.0044 S13:  -0.1347                       
REMARK   3      S21:  -0.0091 S22:  -0.0072 S23:  -0.0676                       
REMARK   3      S31:  -0.0706 S32:   0.0080 S33:  -0.0038                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 257:339)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -10.2726  -0.4035  -2.7503              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0561 T22:   0.0629                                     
REMARK   3      T33:  -0.0274 T12:   0.0013                                     
REMARK   3      T13:  -0.0066 T23:  -0.0156                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2440 L22:   0.1657                                     
REMARK   3      L33:  -0.2251 L12:  -0.0116                                     
REMARK   3      L13:  -0.0591 L23:  -0.0720                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0172 S12:   0.0314 S13:  -0.0120                       
REMARK   3      S21:  -0.0243 S22:  -0.0112 S23:   0.0108                       
REMARK   3      S31:  -0.0367 S32:   0.0140 S33:  -0.0017                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 340:362)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -21.4976   7.9565  12.5073              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0614 T22:   0.0851                                     
REMARK   3      T33:   0.0049 T12:   0.0049                                     
REMARK   3      T13:   0.0292 T23:   0.0002                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0007 L22:   0.1822                                     
REMARK   3      L33:   0.1382 L12:   0.0283                                     
REMARK   3      L13:   0.0364 L23:   0.0450                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0087 S12:  -0.0094 S13:   0.0072                       
REMARK   3      S21:   0.1216 S22:   0.0230 S23:   0.0384                       
REMARK   3      S31:  -0.0673 S32:  -0.1546 S33:  -0.0303                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3IAR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB054178.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JUL-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E SUPERBRIGHT            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54180                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52538                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.520                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.698                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.04800                            
REMARK 200  R SYM                      (I) : 0.04800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.52                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.25100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1KRM                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.20M NANO3, VAPOR         
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K                           
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       30.53500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.33000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.75500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       38.33000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.53500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.75500            
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     4                                                      
REMARK 465     GLU A   365                                                      
REMARK 465     ASN A   366                                                      
REMARK 465     LEU A   367                                                      
REMARK 465     TYR A   368                                                      
REMARK 465     PHE A   369                                                      
REMARK 465     GLN A   370                                                      
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  44    CD   OE1  OE2                                       
REMARK 470     GLN A 138    CD   OE1  NE2                                       
REMARK 470     GLU A 320    CD   OE1  OE2                                       
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   O    HOH A   696     O    HOH A   989              1.98            
REMARK 500   O    HOH A   458     O    HOH A   697              2.04            
REMARK 500   O    HOH A   482     O    HOH A   965              2.12            
REMARK 500   O    HOH A   792     O    HOH A  1033              2.15            
REMARK 500   O    HOH A   433     O    HOH A   946              2.16            
REMARK 500   O    HOH A   529     O    HOH A  1044              2.17            
REMARK 500   O    HOH A   394     O    HOH A   985              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A   8       45.54    -87.45                                   
REMARK 500    LEU A  56     -119.16   -118.30                                   
REMARK 500    THR A 176      -14.78     90.49                                   
REMARK 500    HIS A 238      -86.13     75.15                                   
REMARK 500    ASP A 295      -77.42     70.35                                   
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 A 424        DISTANCE =  5.38 ANGSTROMS                       
REMARK 525    HOH A 445        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH A 452        DISTANCE =  5.70 ANGSTROMS                       
REMARK 525    HOH A 466        DISTANCE =  5.49 ANGSTROMS                       
REMARK 525    HOH A 474        DISTANCE =  5.26 ANGSTROMS                       
REMARK 525    HOH A 487        DISTANCE =  6.76 ANGSTROMS                       
REMARK 525    HOH A 498        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH A 550        DISTANCE =  5.54 ANGSTROMS                       
REMARK 525    HOH A 552        DISTANCE =  6.76 ANGSTROMS                       
REMARK 525    HOH A 582        DISTANCE =  6.56 ANGSTROMS                       
REMARK 525    HOH A 617        DISTANCE =  5.11 ANGSTROMS                       
REMARK 525    HOH A 624        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH A 667        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH A 688        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH A 996        DISTANCE =  5.33 ANGSTROMS                       
REMARK 525    HOH A1029        DISTANCE =  5.51 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                              NI A   1  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  15   NE2                                                    
REMARK 620 2 HIS A  17   NE2 110.4                                              
REMARK 620 3 HIS A 214   NE2  88.9  94.5                                        
REMARK 620 4 ASP A 295   OD1  87.7  92.8 172.7                                  
REMARK 620 5 3D1 A 501   N6  128.1 121.4  90.6  86.4                            
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 3D1 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 371                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 A 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 372                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1KRM   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF BOVINE ADENOSINE DEAMINASE COMPLEXED            
REMARK 900 WITH 6-HYDROXYL-1,6-DIHYDROPURINE RIBOSIDE                           
DBREF  3IAR A    5   363  UNP    P00813   ADA_HUMAN        5    363             
SEQADV 3IAR MET A    4  UNP  P00813              INITIATING METHIONINE          
SEQADV 3IAR ALA A  364  UNP  P00813              EXPRESSION TAG                 
SEQADV 3IAR GLU A  365  UNP  P00813              EXPRESSION TAG                 
SEQADV 3IAR ASN A  366  UNP  P00813              EXPRESSION TAG                 
SEQADV 3IAR LEU A  367  UNP  P00813              EXPRESSION TAG                 
SEQADV 3IAR TYR A  368  UNP  P00813              EXPRESSION TAG                 
SEQADV 3IAR PHE A  369  UNP  P00813              EXPRESSION TAG                 
SEQADV 3IAR GLN A  370  UNP  P00813              EXPRESSION TAG                 
SEQRES   1 A  367  MET PRO ALA PHE ASP LYS PRO LYS VAL GLU LEU HIS VAL          
SEQRES   2 A  367  HIS LEU ASP GLY SER ILE LYS PRO GLU THR ILE LEU TYR          
SEQRES   3 A  367  TYR GLY ARG ARG ARG GLY ILE ALA LEU PRO ALA ASN THR          
SEQRES   4 A  367  ALA GLU GLY LEU LEU ASN VAL ILE GLY MET ASP LYS PRO          
SEQRES   5 A  367  LEU THR LEU PRO ASP PHE LEU ALA LYS PHE ASP TYR TYR          
SEQRES   6 A  367  MET PRO ALA ILE ALA GLY CYS ARG GLU ALA ILE LYS ARG          
SEQRES   7 A  367  ILE ALA TYR GLU PHE VAL GLU MET LYS ALA LYS GLU GLY          
SEQRES   8 A  367  VAL VAL TYR VAL GLU VAL ARG TYR SER PRO HIS LEU LEU          
SEQRES   9 A  367  ALA ASN SER LYS VAL GLU PRO ILE PRO TRP ASN GLN ALA          
SEQRES  10 A  367  GLU GLY ASP LEU THR PRO ASP GLU VAL VAL ALA LEU VAL          
SEQRES  11 A  367  GLY GLN GLY LEU GLN GLU GLY GLU ARG ASP PHE GLY VAL          
SEQRES  12 A  367  LYS ALA ARG SER ILE LEU CYS CYS MET ARG HIS GLN PRO          
SEQRES  13 A  367  ASN TRP SER PRO LYS VAL VAL GLU LEU CYS LYS LYS TYR          
SEQRES  14 A  367  GLN GLN GLN THR VAL VAL ALA ILE ASP LEU ALA GLY ASP          
SEQRES  15 A  367  GLU THR ILE PRO GLY SER SER LEU LEU PRO GLY HIS VAL          
SEQRES  16 A  367  GLN ALA TYR GLN GLU ALA VAL LYS SER GLY ILE HIS ARG          
SEQRES  17 A  367  THR VAL HIS ALA GLY GLU VAL GLY SER ALA GLU VAL VAL          
SEQRES  18 A  367  LYS GLU ALA VAL ASP ILE LEU LYS THR GLU ARG LEU GLY          
SEQRES  19 A  367  HIS GLY TYR HIS THR LEU GLU ASP GLN ALA LEU TYR ASN          
SEQRES  20 A  367  ARG LEU ARG GLN GLU ASN MET HIS PHE GLU ILE CYS PRO          
SEQRES  21 A  367  TRP SER SER TYR LEU THR GLY ALA TRP LYS PRO ASP THR          
SEQRES  22 A  367  GLU HIS ALA VAL ILE ARG LEU LYS ASN ASP GLN ALA ASN          
SEQRES  23 A  367  TYR SER LEU ASN THR ASP ASP PRO LEU ILE PHE LYS SER          
SEQRES  24 A  367  THR LEU ASP THR ASP TYR GLN MET THR LYS ARG ASP MET          
SEQRES  25 A  367  GLY PHE THR GLU GLU GLU PHE LYS ARG LEU ASN ILE ASN          
SEQRES  26 A  367  ALA ALA LYS SER SER PHE LEU PRO GLU ASP GLU LYS ARG          
SEQRES  27 A  367  GLU LEU LEU ASP LEU LEU TYR LYS ALA TYR GLY MET PRO          
SEQRES  28 A  367  PRO SER ALA SER ALA GLY GLN ASN LEU ALA GLU ASN LEU          
SEQRES  29 A  367  TYR PHE GLN                                                  
HET    3D1  A 501      18                                                       
HET     NI  A   1       1                                                       
HET    NO3  A 371       4                                                       
HET    NO3  A   2       4                                                       
HET    GOL  A 372       6                                                       
HETNAM     3D1 (2R,3S,5R)-5-(6-AMINO-9H-PURIN-9-YL)-TETRAHYDRO-2-               
HETNAM   2 3D1  (HYDROXYMETHYL)FURAN-3-OL                                       
HETNAM      NI NICKEL (II) ION                                                  
HETNAM     NO3 NITRATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     3D1 2'-DEOXYADENOSINE                                                
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  3D1    C10 H13 N5 O3                                                
FORMUL   3   NI    NI 2+                                                        
FORMUL   4  NO3    2(N O3 1-)                                                   
FORMUL   6  GOL    C3 H8 O3                                                     
FORMUL   7  HOH   *691(H2 O)                                                    
HELIX    1   1 HIS A   17  SER A   21  5                                   5    
HELIX    2   2 LYS A   23  GLY A   35  1                                  13    
HELIX    3   3 THR A   42  GLY A   51  1                                  10    
HELIX    4   4 THR A   57  ALA A   63  1                                   7    
HELIX    5   5 LYS A   64  TYR A   67  5                                   4    
HELIX    6   6 TYR A   68  ALA A   73  1                                   6    
HELIX    7   7 CYS A   75  LYS A   92  1                                  18    
HELIX    8   8 SER A  103  ALA A  108  5                                   6    
HELIX    9   9 ILE A  115  GLN A  119  5                                   5    
HELIX   10  10 THR A  125  GLY A  145  1                                  21    
HELIX   11  11 GLN A  158  ASN A  160  5                                   3    
HELIX   12  12 TRP A  161  TYR A  172  1                                  12    
HELIX   13  13 GLY A  190  LEU A  193  5                                   4    
HELIX   14  14 LEU A  194  GLY A  208  1                                  15    
HELIX   15  15 SER A  220  ILE A  230  1                                  11    
HELIX   16  16 TYR A  240  GLU A  244  5                                   5    
HELIX   17  17 ASP A  245  GLU A  255  1                                  11    
HELIX   18  18 CYS A  262  THR A  269  1                                   8    
HELIX   19  19 HIS A  278  ASP A  286  1                                   9    
HELIX   20  20 ASP A  296  LYS A  301  1                                   6    
HELIX   21  21 THR A  303  GLY A  316  1                                  14    
HELIX   22  22 THR A  318  SER A  332  1                                  15    
HELIX   23  23 PRO A  336  GLY A  352  1                                  17    
HELIX   24  24 PRO A  354  LEU A  363  1                                  10    
SHEET    1   A 8 LYS A  11  GLU A  13  0                                        
SHEET    2   A 8 VAL A  95  TYR A 102  1  O  VAL A  96   N  LYS A  11           
SHEET    3   A 8 LYS A 147  MET A 155  1  O  CYS A 153   N  TYR A 102           
SHEET    4   A 8 VAL A 177  ALA A 183  1  O  ASP A 181   N  CYS A 154           
SHEET    5   A 8 HIS A 210  ALA A 215  1  O  HIS A 214   N  LEU A 182           
SHEET    6   A 8 ARG A 235  HIS A 238  1  O  GLY A 237   N  VAL A 213           
SHEET    7   A 8 HIS A 258  ILE A 261  1  O  GLU A 260   N  LEU A 236           
SHEET    8   A 8 TYR A 290  LEU A 292  1  O  SER A 291   N  PHE A 259           
LINK         NE2 HIS A  15                NI    NI A   1     1555   1555  2.10  
LINK         NE2 HIS A  17                NI    NI A   1     1555   1555  2.04  
LINK         NE2 HIS A 214                NI    NI A   1     1555   1555  2.21  
LINK         OD1 ASP A 295                NI    NI A   1     1555   1555  2.12  
LINK         N6  3D1 A 501                NI    NI A   1     1555   1555  2.15  
CISPEP   1 GLU A  113    PRO A  114          0        -4.56                     
SITE     1 AC1 14  NI A   1  HIS A  17  ASP A  19  LEU A  62                    
SITE     2 AC1 14 PHE A  65  LEU A 106  GLY A 184  HIS A 214                    
SITE     3 AC1 14 GLU A 217  HIS A 238  ASP A 295  ASP A 296                    
SITE     4 AC1 14 HOH A 781  HOH A 814                                          
SITE     1 AC2  5 HIS A  15  HIS A  17  HIS A 214  ASP A 295                    
SITE     2 AC2  5 3D1 A 501                                                     
SITE     1 AC3  7 LYS A 111  THR A 125  PRO A 126  ASP A 127                    
SITE     2 AC3  7 LYS A 164  HOH A 727  HOH A1058                               
SITE     1 AC4 10 PRO A   5  PHE A   7  ASP A   8  LYS A  11                    
SITE     2 AC4 10 TYR A  29  ARG A  33  GLU A  93  ASP A 305                    
SITE     3 AC4 10 HOH A 702  HOH A 827                                          
SITE     1 AC5  8 PRO A 116  TRP A 117  HIS A 157  HOH A 397                    
SITE     2 AC5  8 HOH A 485  HOH A 613  HOH A 795  HOH A 797                    
CRYST1   61.070   73.510   76.660  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016375  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013604  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013045        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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