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Database: PDB
Entry: 2VXO
LinkDB: 2VXO
Original site: 2VXO 
HEADER    LIGASE                                  08-JUL-08   2VXO              
TITLE     HUMAN GMP SYNTHETASE IN COMPLEX WITH XMP                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GMP SYNTHASE [GLUTAMINE-HYDROLYZING];                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 20-693;                                           
COMPND   5 SYNONYM: GLUTAMINE AMIDOTRANSFERASE, GMP SYNTHETASE;                 
COMPND   6 EC: 6.3.5.2;                                                         
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: R3 PRARE;                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PNIC-BSA4                                  
KEYWDS    PROTO-ONCOGENE, PHOSPHOPROTEIN, GUANINE MONOPHOSPHATE SYNTHETASE, GMP 
KEYWDS   2 BIOSYNTHESIS, NUCLEOTIDE-BINDING, PURINE BIOSYNTHESIS, NUCLEOTIDE    
KEYWDS   3 METABOLISM, GMPS, CASP8, LIGASE, ATP-BINDING                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.WELIN,L.LEHTIO,J.ANDERSSON,C.H.ARROWSMITH,H.BERGLUND,R.COLLINS,     
AUTHOR   2 L.G.DAHLGREN,A.M.EDWARDS,S.FLODIN,A.FLORES,S.GRASLUND,M.HAMMARSTROM, 
AUTHOR   3 A.JOHANSSON,I.JOHANSSON,T.KARLBERG,T.KOTENYOVA,M.MOCHE,M.E.NILSSON,  
AUTHOR   4 T.NYMAN,K.OLESEN,C.PERSSON,J.SAGEMARK,H.SCHUELER,A.G.THORSELL,       
AUTHOR   5 L.TRESAUGUES,S.VAN DEN BERG,M.WISNIEWSKA,M.WIKSTROM,P.NORDLUND       
REVDAT   6   13-DEC-23 2VXO    1       REMARK                                   
REVDAT   5   16-OCT-19 2VXO    1       REMARK                                   
REVDAT   4   13-NOV-13 2VXO    1       JRNL                                     
REVDAT   3   10-JUL-13 2VXO    1       SOURCE KEYWDS JRNL   REMARK              
REVDAT   3 2                   1       VERSN  FORMUL                            
REVDAT   2   24-FEB-09 2VXO    1       VERSN                                    
REVDAT   1   12-AUG-08 2VXO    0                                                
JRNL        AUTH   M.WELIN,L.LEHTIO,A.JOHANSSON,S.FLODIN,T.NYMAN,L.TRESAUGUES,  
JRNL        AUTH 2 M.HAMMARSTROM,S.GRASLUND,P.NORDLUND                          
JRNL        TITL   SUBSTRATE SPECIFICITY AND OLIGOMERIZATION OF HUMAN GMP       
JRNL        TITL 2 SYNTHETASE                                                   
JRNL        REF    J.MOL.BIOL.                   V. 425  4323 2013              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   23816837                                                     
JRNL        DOI    10.1016/J.JMB.2013.06.032                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0036                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.92                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 51746                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2724                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.56                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3728                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2630                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 196                          
REMARK   3   BIN FREE R VALUE                    : 0.2800                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10019                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 78                                      
REMARK   3   SOLVENT ATOMS            : 125                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.38                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.37000                                              
REMARK   3    B22 (A**2) : 0.64000                                              
REMARK   3    B33 (A**2) : -1.01000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.504         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.290         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.202         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.944         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.904                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10313 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14002 ; 1.203 ; 1.984       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1301 ; 5.568 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   417 ;36.048 ;24.388       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1798 ;16.314 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    58 ;20.238 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1637 ; 0.077 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7608 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  6490 ; 0.863 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 10560 ; 1.679 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3823 ; 2.178 ; 4.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3438 ; 3.698 ; 6.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. U VALUES REFINED INDIVIDUALLY.                           
REMARK   4                                                                      
REMARK   4 2VXO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-JUL-08.                  
REMARK 100 THE DEPOSITION ID IS D_1290036804.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-MAY-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.2                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97968                            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54472                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 7.700                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.120                              
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 2YWC                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M NAAC,PH 5.2,1.6M AMSO4, 0.2M        
REMARK 280  NACL, VAPOR DIFFUSION, SITTING DROP                                 
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       49.26000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       63.98000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.71000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       63.98000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       49.26000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       61.71000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9960 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 50670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -128.5 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     HIS A     1                                                      
REMARK 465     HIS A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     VAL A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 465     THR A    11                                                      
REMARK 465     GLU A    12                                                      
REMARK 465     ASN A    13                                                      
REMARK 465     LEU A    14                                                      
REMARK 465     TYR A    15                                                      
REMARK 465     PHE A    16                                                      
REMARK 465     GLN A    17                                                      
REMARK 465     SER A    18                                                      
REMARK 465     MET A    19                                                      
REMARK 465     GLY A    20                                                      
REMARK 465     HIS A    21                                                      
REMARK 465     HIS A    22                                                      
REMARK 465     HIS A    23                                                      
REMARK 465     TYR A    24                                                      
REMARK 465     ALA A    35                                                      
REMARK 465     GLN A    36                                                      
REMARK 465     ASN A    79                                                      
REMARK 465     SER A    80                                                      
REMARK 465     VAL A    81                                                      
REMARK 465     TYR A    82                                                      
REMARK 465     ALA A    83                                                      
REMARK 465     GLU A    84                                                      
REMARK 465     ASP A    85                                                      
REMARK 465     LYS A   121                                                      
REMARK 465     SER A   122                                                      
REMARK 465     VAL A   123                                                      
REMARK 465     ARG A   124                                                      
REMARK 465     GLU A   125                                                      
REMARK 465     ASP A   126                                                      
REMARK 465     GLY A   127                                                      
REMARK 465     ILE A   312                                                      
REMARK 465     SER A   313                                                      
REMARK 465     ASP A   314                                                      
REMARK 465     GLU A   315                                                      
REMARK 465     ASP A   316                                                      
REMARK 465     ARG A   317                                                      
REMARK 465     THR A   318                                                      
REMARK 465     PRO A   319                                                      
REMARK 465     ARG A   320                                                      
REMARK 465     LYS A   321                                                      
REMARK 465     MET B    -3                                                      
REMARK 465     HIS B    -2                                                      
REMARK 465     HIS B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     HIS B     1                                                      
REMARK 465     HIS B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     GLY B     6                                                      
REMARK 465     VAL B     7                                                      
REMARK 465     ASP B     8                                                      
REMARK 465     LEU B     9                                                      
REMARK 465     GLY B    10                                                      
REMARK 465     THR B    11                                                      
REMARK 465     GLU B    12                                                      
REMARK 465     ASN B    13                                                      
REMARK 465     LEU B    14                                                      
REMARK 465     TYR B    15                                                      
REMARK 465     PHE B    16                                                      
REMARK 465     GLN B    17                                                      
REMARK 465     SER B    18                                                      
REMARK 465     MET B    19                                                      
REMARK 465     GLY B    20                                                      
REMARK 465     HIS B    21                                                      
REMARK 465     HIS B    22                                                      
REMARK 465     VAL B   123                                                      
REMARK 465     ARG B   124                                                      
REMARK 465     GLU B   125                                                      
REMARK 465     ILE B   312                                                      
REMARK 465     SER B   313                                                      
REMARK 465     ASP B   314                                                      
REMARK 465     GLU B   315                                                      
REMARK 465     ASP B   316                                                      
REMARK 465     ARG B   317                                                      
REMARK 465     THR B   318                                                      
REMARK 465     PRO B   319                                                      
REMARK 465     ARG B   320                                                      
REMARK 465     LYS B   321                                                      
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  25    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  39    CD   CE   NZ                                        
REMARK 470     ARG A  43    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A  66    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 120    CG   CD   CE   NZ                                   
REMARK 470     ARG A 278    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 281    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 289    CG   CD   CE   NZ                                   
REMARK 470     ARG A 322    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASN A 356    CG   OD1  ND2                                       
REMARK 470     LYS A 358    CD   CE   NZ                                        
REMARK 470     LYS A 569    CG   CD   CE   NZ                                   
REMARK 470     LYS A 627    CG   CD   CE   NZ                                   
REMARK 470     HIS B  23    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B  39    CG   CD   CE   NZ                                   
REMARK 470     ARG B  43    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 120    CG   CD   CE   NZ                                   
REMARK 470     LYS B 121    CG   CD   CE   NZ                                   
REMARK 470     ARG B 278    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 289    CG   CD   CE   NZ                                   
REMARK 470     ARG B 322    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 360    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 361    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 569    CG   CD   CE   NZ                                   
REMARK 470     LYS B 627    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   ND2  ASN B   135     O    LEU B   143              2.13            
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    ALA A  33       57.97   -112.93                                   
REMARK 500    CYS A 104     -105.55     73.30                                   
REMARK 500    HIS A 119     -165.81   -127.11                                   
REMARK 500    ASP A 158      -91.23   -108.43                                   
REMARK 500    ARG A 278       -4.53     69.34                                   
REMARK 500    PRO A 617       40.64    -79.21                                   
REMARK 500    ASN A 655      -90.08   -111.32                                   
REMARK 500    SER A 676      -82.78    -78.02                                   
REMARK 500    ALA B  86      122.28    -37.48                                   
REMARK 500    CYS B 104      -98.65     55.18                                   
REMARK 500    ASP B 158      -85.87    -90.36                                   
REMARK 500    TYR B 208      -71.02    -97.01                                   
REMARK 500    LYS B 277      109.09    -55.22                                   
REMARK 500    GLN B 610      142.54   -172.45                                   
REMARK 500    PRO B 617       46.71    -74.68                                   
REMARK 500    GLN B 626      -17.06   -160.82                                   
REMARK 500    ASN B 655      -85.57   -123.58                                   
REMARK 500    SER B 676      -84.55    -74.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XMP A 1694                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE XMP B 1694                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1695                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1696                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1695                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1696                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1697                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1697                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VPI   RELATED DB: PDB                                   
REMARK 900 HUMAN GMP SYNTHETASE - GLUTAMINASE DOMAIN                            
DBREF  2VXO A   -3    19  PDB    2VXO     2VXO            -3     19             
DBREF  2VXO A   20   693  UNP    P49915   GUAA_HUMAN      20    693             
DBREF  2VXO B   -3    19  PDB    2VXO     2VXO            -3     19             
DBREF  2VXO B   20   693  UNP    P49915   GUAA_HUMAN      20    693             
SEQRES   1 A  697  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  697  GLY THR GLU ASN LEU TYR PHE GLN SER MET GLY HIS HIS          
SEQRES   3 A  697  HIS TYR GLU GLY ALA VAL VAL ILE LEU ASP ALA GLY ALA          
SEQRES   4 A  697  GLN TYR GLY LYS VAL ILE ASP ARG ARG VAL ARG GLU LEU          
SEQRES   5 A  697  PHE VAL GLN SER GLU ILE PHE PRO LEU GLU THR PRO ALA          
SEQRES   6 A  697  PHE ALA ILE LYS GLU GLN GLY PHE ARG ALA ILE ILE ILE          
SEQRES   7 A  697  SER GLY GLY PRO ASN SER VAL TYR ALA GLU ASP ALA PRO          
SEQRES   8 A  697  TRP PHE ASP PRO ALA ILE PHE THR ILE GLY LYS PRO VAL          
SEQRES   9 A  697  LEU GLY ILE CYS TYR GLY MET GLN MET MET ASN LYS VAL          
SEQRES  10 A  697  PHE GLY GLY THR VAL HIS LYS LYS SER VAL ARG GLU ASP          
SEQRES  11 A  697  GLY VAL PHE ASN ILE SER VAL ASP ASN THR CYS SER LEU          
SEQRES  12 A  697  PHE ARG GLY LEU GLN LYS GLU GLU VAL VAL LEU LEU THR          
SEQRES  13 A  697  HIS GLY ASP SER VAL ASP LYS VAL ALA ASP GLY PHE LYS          
SEQRES  14 A  697  VAL VAL ALA ARG SER GLY ASN ILE VAL ALA GLY ILE ALA          
SEQRES  15 A  697  ASN GLU SER LYS LYS LEU TYR GLY ALA GLN PHE HIS PRO          
SEQRES  16 A  697  GLU VAL GLY LEU THR GLU ASN GLY LYS VAL ILE LEU LYS          
SEQRES  17 A  697  ASN PHE LEU TYR ASP ILE ALA GLY CYS SER GLY THR PHE          
SEQRES  18 A  697  THR VAL GLN ASN ARG GLU LEU GLU CYS ILE ARG GLU ILE          
SEQRES  19 A  697  LYS GLU ARG VAL GLY THR SER LYS VAL LEU VAL LEU LEU          
SEQRES  20 A  697  SER GLY GLY VAL ASP SER THR VAL CYS THR ALA LEU LEU          
SEQRES  21 A  697  ASN ARG ALA LEU ASN GLN GLU GLN VAL ILE ALA VAL HIS          
SEQRES  22 A  697  ILE ASP ASN GLY PHE MET ARG LYS ARG GLU SER GLN SER          
SEQRES  23 A  697  VAL GLU GLU ALA LEU LYS LYS LEU GLY ILE GLN VAL LYS          
SEQRES  24 A  697  VAL ILE ASN ALA ALA HIS SER PHE TYR ASN GLY THR THR          
SEQRES  25 A  697  THR LEU PRO ILE SER ASP GLU ASP ARG THR PRO ARG LYS          
SEQRES  26 A  697  ARG ILE SER LYS THR LEU ASN MET THR THR SER PRO GLU          
SEQRES  27 A  697  GLU LYS ARG LYS ILE ILE GLY ASP THR PHE VAL LYS ILE          
SEQRES  28 A  697  ALA ASN GLU VAL ILE GLY GLU MET ASN LEU LYS PRO GLU          
SEQRES  29 A  697  GLU VAL PHE LEU ALA GLN GLY THR LEU ARG PRO ASP LEU          
SEQRES  30 A  697  ILE GLU SER ALA SER LEU VAL ALA SER GLY LYS ALA GLU          
SEQRES  31 A  697  LEU ILE LYS THR HIS HIS ASN ASP THR GLU LEU ILE ARG          
SEQRES  32 A  697  LYS LEU ARG GLU GLU GLY LYS VAL ILE GLU PRO LEU LYS          
SEQRES  33 A  697  ASP PHE HIS LYS ASP GLU VAL ARG ILE LEU GLY ARG GLU          
SEQRES  34 A  697  LEU GLY LEU PRO GLU GLU LEU VAL SER ARG HIS PRO PHE          
SEQRES  35 A  697  PRO GLY PRO GLY LEU ALA ILE ARG VAL ILE CYS ALA GLU          
SEQRES  36 A  697  GLU PRO TYR ILE CYS LYS ASP PHE PRO GLU THR ASN ASN          
SEQRES  37 A  697  ILE LEU LYS ILE VAL ALA ASP PHE SER ALA SER VAL LYS          
SEQRES  38 A  697  LYS PRO HIS THR LEU LEU GLN ARG VAL LYS ALA CYS THR          
SEQRES  39 A  697  THR GLU GLU ASP GLN GLU LYS LEU MET GLN ILE THR SER          
SEQRES  40 A  697  LEU HIS SER LEU ASN ALA PHE LEU LEU PRO ILE LYS THR          
SEQRES  41 A  697  VAL GLY VAL GLN GLY ASP CYS ARG SER TYR SER TYR VAL          
SEQRES  42 A  697  CYS GLY ILE SER SER LYS ASP GLU PRO ASP TRP GLU SER          
SEQRES  43 A  697  LEU ILE PHE LEU ALA ARG LEU ILE PRO ARG MET CYS HIS          
SEQRES  44 A  697  ASN VAL ASN ARG VAL VAL TYR ILE PHE GLY PRO PRO VAL          
SEQRES  45 A  697  LYS GLU PRO PRO THR ASP VAL THR PRO THR PHE LEU THR          
SEQRES  46 A  697  THR GLY VAL LEU SER THR LEU ARG GLN ALA ASP PHE GLU          
SEQRES  47 A  697  ALA HIS ASN ILE LEU ARG GLU SER GLY TYR ALA GLY LYS          
SEQRES  48 A  697  ILE SER GLN MET PRO VAL ILE LEU THR PRO LEU HIS PHE          
SEQRES  49 A  697  ASP ARG ASP PRO LEU GLN LYS GLN PRO SER CYS GLN ARG          
SEQRES  50 A  697  SER VAL VAL ILE ARG THR PHE ILE THR SER ASP PHE MET          
SEQRES  51 A  697  THR GLY ILE PRO ALA THR PRO GLY ASN GLU ILE PRO VAL          
SEQRES  52 A  697  GLU VAL VAL LEU LYS MET VAL THR GLU ILE LYS LYS ILE          
SEQRES  53 A  697  PRO GLY ILE SER ARG ILE MET TYR ASP LEU THR SER LYS          
SEQRES  54 A  697  PRO PRO GLY THR THR GLU TRP GLU                              
SEQRES   1 B  697  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  697  GLY THR GLU ASN LEU TYR PHE GLN SER MET GLY HIS HIS          
SEQRES   3 B  697  HIS TYR GLU GLY ALA VAL VAL ILE LEU ASP ALA GLY ALA          
SEQRES   4 B  697  GLN TYR GLY LYS VAL ILE ASP ARG ARG VAL ARG GLU LEU          
SEQRES   5 B  697  PHE VAL GLN SER GLU ILE PHE PRO LEU GLU THR PRO ALA          
SEQRES   6 B  697  PHE ALA ILE LYS GLU GLN GLY PHE ARG ALA ILE ILE ILE          
SEQRES   7 B  697  SER GLY GLY PRO ASN SER VAL TYR ALA GLU ASP ALA PRO          
SEQRES   8 B  697  TRP PHE ASP PRO ALA ILE PHE THR ILE GLY LYS PRO VAL          
SEQRES   9 B  697  LEU GLY ILE CYS TYR GLY MET GLN MET MET ASN LYS VAL          
SEQRES  10 B  697  PHE GLY GLY THR VAL HIS LYS LYS SER VAL ARG GLU ASP          
SEQRES  11 B  697  GLY VAL PHE ASN ILE SER VAL ASP ASN THR CYS SER LEU          
SEQRES  12 B  697  PHE ARG GLY LEU GLN LYS GLU GLU VAL VAL LEU LEU THR          
SEQRES  13 B  697  HIS GLY ASP SER VAL ASP LYS VAL ALA ASP GLY PHE LYS          
SEQRES  14 B  697  VAL VAL ALA ARG SER GLY ASN ILE VAL ALA GLY ILE ALA          
SEQRES  15 B  697  ASN GLU SER LYS LYS LEU TYR GLY ALA GLN PHE HIS PRO          
SEQRES  16 B  697  GLU VAL GLY LEU THR GLU ASN GLY LYS VAL ILE LEU LYS          
SEQRES  17 B  697  ASN PHE LEU TYR ASP ILE ALA GLY CYS SER GLY THR PHE          
SEQRES  18 B  697  THR VAL GLN ASN ARG GLU LEU GLU CYS ILE ARG GLU ILE          
SEQRES  19 B  697  LYS GLU ARG VAL GLY THR SER LYS VAL LEU VAL LEU LEU          
SEQRES  20 B  697  SER GLY GLY VAL ASP SER THR VAL CYS THR ALA LEU LEU          
SEQRES  21 B  697  ASN ARG ALA LEU ASN GLN GLU GLN VAL ILE ALA VAL HIS          
SEQRES  22 B  697  ILE ASP ASN GLY PHE MET ARG LYS ARG GLU SER GLN SER          
SEQRES  23 B  697  VAL GLU GLU ALA LEU LYS LYS LEU GLY ILE GLN VAL LYS          
SEQRES  24 B  697  VAL ILE ASN ALA ALA HIS SER PHE TYR ASN GLY THR THR          
SEQRES  25 B  697  THR LEU PRO ILE SER ASP GLU ASP ARG THR PRO ARG LYS          
SEQRES  26 B  697  ARG ILE SER LYS THR LEU ASN MET THR THR SER PRO GLU          
SEQRES  27 B  697  GLU LYS ARG LYS ILE ILE GLY ASP THR PHE VAL LYS ILE          
SEQRES  28 B  697  ALA ASN GLU VAL ILE GLY GLU MET ASN LEU LYS PRO GLU          
SEQRES  29 B  697  GLU VAL PHE LEU ALA GLN GLY THR LEU ARG PRO ASP LEU          
SEQRES  30 B  697  ILE GLU SER ALA SER LEU VAL ALA SER GLY LYS ALA GLU          
SEQRES  31 B  697  LEU ILE LYS THR HIS HIS ASN ASP THR GLU LEU ILE ARG          
SEQRES  32 B  697  LYS LEU ARG GLU GLU GLY LYS VAL ILE GLU PRO LEU LYS          
SEQRES  33 B  697  ASP PHE HIS LYS ASP GLU VAL ARG ILE LEU GLY ARG GLU          
SEQRES  34 B  697  LEU GLY LEU PRO GLU GLU LEU VAL SER ARG HIS PRO PHE          
SEQRES  35 B  697  PRO GLY PRO GLY LEU ALA ILE ARG VAL ILE CYS ALA GLU          
SEQRES  36 B  697  GLU PRO TYR ILE CYS LYS ASP PHE PRO GLU THR ASN ASN          
SEQRES  37 B  697  ILE LEU LYS ILE VAL ALA ASP PHE SER ALA SER VAL LYS          
SEQRES  38 B  697  LYS PRO HIS THR LEU LEU GLN ARG VAL LYS ALA CYS THR          
SEQRES  39 B  697  THR GLU GLU ASP GLN GLU LYS LEU MET GLN ILE THR SER          
SEQRES  40 B  697  LEU HIS SER LEU ASN ALA PHE LEU LEU PRO ILE LYS THR          
SEQRES  41 B  697  VAL GLY VAL GLN GLY ASP CYS ARG SER TYR SER TYR VAL          
SEQRES  42 B  697  CYS GLY ILE SER SER LYS ASP GLU PRO ASP TRP GLU SER          
SEQRES  43 B  697  LEU ILE PHE LEU ALA ARG LEU ILE PRO ARG MET CYS HIS          
SEQRES  44 B  697  ASN VAL ASN ARG VAL VAL TYR ILE PHE GLY PRO PRO VAL          
SEQRES  45 B  697  LYS GLU PRO PRO THR ASP VAL THR PRO THR PHE LEU THR          
SEQRES  46 B  697  THR GLY VAL LEU SER THR LEU ARG GLN ALA ASP PHE GLU          
SEQRES  47 B  697  ALA HIS ASN ILE LEU ARG GLU SER GLY TYR ALA GLY LYS          
SEQRES  48 B  697  ILE SER GLN MET PRO VAL ILE LEU THR PRO LEU HIS PHE          
SEQRES  49 B  697  ASP ARG ASP PRO LEU GLN LYS GLN PRO SER CYS GLN ARG          
SEQRES  50 B  697  SER VAL VAL ILE ARG THR PHE ILE THR SER ASP PHE MET          
SEQRES  51 B  697  THR GLY ILE PRO ALA THR PRO GLY ASN GLU ILE PRO VAL          
SEQRES  52 B  697  GLU VAL VAL LEU LYS MET VAL THR GLU ILE LYS LYS ILE          
SEQRES  53 B  697  PRO GLY ILE SER ARG ILE MET TYR ASP LEU THR SER LYS          
SEQRES  54 B  697  PRO PRO GLY THR THR GLU TRP GLU                              
HET    XMP  A1694      24                                                       
HET    SO4  A1695       5                                                       
HET    SO4  A1696       5                                                       
HET    SO4  A1697       5                                                       
HET    XMP  B1694      24                                                       
HET    SO4  B1695       5                                                       
HET    SO4  B1696       5                                                       
HET    SO4  B1697       5                                                       
HETNAM     XMP XANTHOSINE-5'-MONOPHOSPHATE                                      
HETNAM     SO4 SULFATE ION                                                      
HETSYN     XMP 5-MONOPHOSPHATE-9-BETA-D-RIBOFURANOSYL XANTHINE                  
FORMUL   3  XMP    2(C10 H14 N4 O9 P 1+)                                        
FORMUL   4  SO4    6(O4 S 2-)                                                   
FORMUL  11  HOH   *125(H2 O)                                                    
HELIX    1   1 TYR A   37  LEU A   48  1                                  12    
HELIX    2   2 PRO A   60  GLY A   68  1                                   9    
HELIX    3   3 ASP A   90  PHE A   94  5                                   5    
HELIX    4   4 CYS A  104  PHE A  114  1                                  11    
HELIX    5   5 CYS A  137  ARG A  141  5                                   5    
HELIX    6   6 ASN A  198  TYR A  208  1                                  11    
HELIX    7   7 THR A  218  GLY A  235  1                                  18    
HELIX    8   8 GLY A  246  LEU A  260  1                                  15    
HELIX    9   9 ASN A  261  GLU A  263  5                                   3    
HELIX   10  10 SER A  280  LEU A  290  1                                  11    
HELIX   11  11 ALA A  299  ASN A  305  1                                   7    
HELIX   12  12 THR A  326  THR A  330  5                                   5    
HELIX   13  13 SER A  332  MET A  355  1                                  24    
HELIX   14  14 SER A  376  GLY A  383  1                                   8    
HELIX   15  15 GLU A  386  THR A  390  5                                   5    
HELIX   16  16 THR A  395  GLU A  404  1                                  10    
HELIX   17  17 GLU A  409  PHE A  414  5                                   6    
HELIX   18  18 HIS A  415  LEU A  426  1                                  12    
HELIX   19  19 PRO A  429  SER A  434  1                                   6    
HELIX   20  20 PRO A  441  ARG A  446  5                                   6    
HELIX   21  21 ASP A  458  ASP A  471  1                                  14    
HELIX   22  22 ASP A  471  VAL A  476  1                                   6    
HELIX   23  23 HIS A  480  THR A  490  1                                  11    
HELIX   24  24 THR A  491  HIS A  505  1                                  15    
HELIX   25  25 ASP A  539  CYS A  554  1                                  16    
HELIX   26  26 THR A  581  SER A  602  1                                  22    
HELIX   27  27 TYR A  604  ILE A  608  5                                   5    
HELIX   28  28 ASP A  623  LYS A  627  5                                   5    
HELIX   29  29 PRO A  658  ILE A  672  1                                  15    
HELIX   30  30 GLN B   36  LEU B   48  1                                  13    
HELIX   31  31 PRO B   60  GLY B   68  1                                   9    
HELIX   32  32 ASP B   90  THR B   95  5                                   6    
HELIX   33  33 CYS B  104  PHE B  114  1                                  11    
HELIX   34  34 CYS B  137  ARG B  141  5                                   5    
HELIX   35  35 ASN B  198  TYR B  208  1                                  11    
HELIX   36  36 THR B  218  GLY B  235  1                                  18    
HELIX   37  37 GLY B  246  LEU B  260  1                                  15    
HELIX   38  38 GLN B  281  LEU B  290  1                                  10    
HELIX   39  39 ALA B  299  ASN B  305  1                                   7    
HELIX   40  40 THR B  326  THR B  330  5                                   5    
HELIX   41  41 SER B  332  MET B  355  1                                  24    
HELIX   42  42 LYS B  358  GLU B  360  5                                   3    
HELIX   43  43 SER B  376  GLY B  383  1                                   8    
HELIX   44  44 GLU B  386  THR B  390  5                                   5    
HELIX   45  45 THR B  395  GLU B  404  1                                  10    
HELIX   46  46 GLU B  409  PHE B  414  5                                   6    
HELIX   47  47 HIS B  415  LEU B  426  1                                  12    
HELIX   48  48 PRO B  429  SER B  434  1                                   6    
HELIX   49  49 PRO B  441  ARG B  446  5                                   6    
HELIX   50  50 ASP B  458  ASP B  471  1                                  14    
HELIX   51  51 ASP B  471  LYS B  478  1                                   8    
HELIX   52  52 HIS B  480  THR B  490  1                                  11    
HELIX   53  53 THR B  491  HIS B  505  1                                  15    
HELIX   54  54 ASP B  539  CYS B  554  1                                  16    
HELIX   55  55 THR B  581  SER B  602  1                                  22    
HELIX   56  56 TYR B  604  ILE B  608  5                                   5    
HELIX   57  57 PRO B  658  LYS B  671  1                                  14    
SHEET    1  AA 9 SER A  52  PRO A  56  0                                        
SHEET    2  AA 9 VAL A  28  ALA A  33  1  O  VAL A  28   N  GLU A  53           
SHEET    3  AA 9 ALA A  71  GLY A  76  1  O  ALA A  71   N  VAL A  29           
SHEET    4  AA 9 VAL A 100  ILE A 103  1  O  LEU A 101   N  ILE A  74           
SHEET    5  AA 9 LEU A 184  ALA A 187  1  O  TYR A 185   N  GLY A 102           
SHEET    6  AA 9 ILE A 173  ASN A 179 -1  O  ILE A 177   N  GLY A 186           
SHEET    7  AA 9 LYS A 165  SER A 170 -1  O  LYS A 165   N  ALA A 178           
SHEET    8  AA 9 PHE A 129  VAL A 133 -1  O  SER A 132   N  ARG A 169           
SHEET    9  AA 9 GLU A 146  VAL A 149 -1  O  GLU A 147   N  ILE A 131           
SHEET    1  AB 5 VAL A 294  ASN A 298  0                                        
SHEET    2  AB 5 VAL A 265  ASP A 271  1  O  ALA A 267   N  LYS A 295           
SHEET    3  AB 5 LYS A 238  LEU A 242  1  O  VAL A 239   N  ILE A 266           
SHEET    4  AB 5 VAL A 362  ALA A 365  1  O  PHE A 363   N  LEU A 240           
SHEET    5  AB 5 VAL A 407  ILE A 408  1  N  ILE A 408   O  LEU A 364           
SHEET    1  AC 6 LEU A 507  GLN A 520  0                                        
SHEET    2  AC 6 CYS A 523  SER A 534 -1  O  CYS A 523   N  GLN A 520           
SHEET    3  AC 6 VAL A 557  ILE A 563  1  N  ASN A 558   O  TYR A 528           
SHEET    4  AC 6 ILE A 675  ASP A 681 -1  O  TYR A 680   N  TYR A 562           
SHEET    5  AC 6 ARG A 633  ILE A 637  1  O  ARG A 633   N  SER A 676           
SHEET    6  AC 6 VAL A 613  THR A 616 -1  O  ILE A 614   N  VAL A 636           
SHEET    1  BA 9 SER B  52  PRO B  56  0                                        
SHEET    2  BA 9 VAL B  28  ASP B  32  1  O  VAL B  28   N  GLU B  53           
SHEET    3  BA 9 ALA B  71  SER B  75  1  O  ALA B  71   N  VAL B  29           
SHEET    4  BA 9 VAL B 100  ILE B 103  1  O  LEU B 101   N  ILE B  74           
SHEET    5  BA 9 LEU B 184  ALA B 187  1  O  TYR B 185   N  GLY B 102           
SHEET    6  BA 9 ILE B 173  ASN B 179 -1  O  ILE B 177   N  GLY B 186           
SHEET    7  BA 9 LYS B 165  SER B 170 -1  O  LYS B 165   N  ALA B 178           
SHEET    8  BA 9 VAL B 128  VAL B 133 -1  O  SER B 132   N  ARG B 169           
SHEET    9  BA 9 GLU B 146  LEU B 150 -1  O  GLU B 147   N  ILE B 131           
SHEET    1  BB 5 VAL B 294  ASN B 298  0                                        
SHEET    2  BB 5 VAL B 265  ASP B 271  1  O  ALA B 267   N  LYS B 295           
SHEET    3  BB 5 LYS B 238  LEU B 242  1  O  VAL B 239   N  ILE B 266           
SHEET    4  BB 5 VAL B 362  ALA B 365  1  O  PHE B 363   N  LEU B 240           
SHEET    5  BB 5 VAL B 407  ILE B 408  1  N  ILE B 408   O  LEU B 364           
SHEET    1  BC 6 LEU B 507  GLN B 520  0                                        
SHEET    2  BC 6 CYS B 523  SER B 534 -1  O  CYS B 523   N  GLN B 520           
SHEET    3  BC 6 VAL B 557  ILE B 563  1  N  ASN B 558   O  TYR B 528           
SHEET    4  BC 6 ILE B 675  ASP B 681 -1  O  TYR B 680   N  TYR B 562           
SHEET    5  BC 6 ARG B 633  ILE B 637  1  O  ARG B 633   N  SER B 676           
SHEET    6  BC 6 VAL B 613  THR B 616 -1  O  ILE B 614   N  VAL B 636           
CISPEP   1 LYS A  685    PRO A  686          0        -6.34                     
CISPEP   2 PRO A  686    PRO A  687          0        -4.03                     
CISPEP   3 LYS B  685    PRO B  686          0        -6.20                     
CISPEP   4 PRO B  686    PRO B  687          0         2.86                     
SITE     1 AC1 15 ARG A 337  GLY A 383  LYS A 384  PRO A 439                    
SITE     2 AC1 15 GLY A 440  PRO A 441  GLN A 610  PHE A 645                    
SITE     3 AC1 15 LYS A 685  THR A 689  THR A 690  GLU A 691                    
SITE     4 AC1 15 HOH A2066  HOH A2067  ASP B 522                               
SITE     1 AC2 16 ASP A 522  ARG B 337  GLY B 383  LYS B 384                    
SITE     2 AC2 16 PRO B 439  GLY B 440  PRO B 441  ARG B 524                    
SITE     3 AC2 16 GLN B 610  PHE B 645  LYS B 685  THR B 689                    
SITE     4 AC2 16 THR B 690  GLU B 691  HOH B2029  HOH B2057                    
SITE     1 AC3  6 ARG A 276  GLU A 279  ARG A 435  HIS A 436                    
SITE     2 AC3  6 HIS A 596  ARG A 600                                          
SITE     1 AC4  3 THR A 581  GLY A 583  VAL A 584                               
SITE     1 AC5  3 THR B 581  GLY B 583  VAL B 584                               
SITE     1 AC6  5 ARG B 276  ARG B 435  HIS B 436  HIS B 596                    
SITE     2 AC6  5 ARG B 600                                                     
SITE     1 AC7  5 SER A 244  GLY A 246  VAL A 247  ASP A 248                    
SITE     2 AC7  5 SER A 249                                                     
SITE     1 AC8  4 SER B 244  GLY B 246  ASP B 248  SER B 249                    
CRYST1   98.520  123.420  127.960  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      0.010150  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008102  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007815        0.00000                         
MTRIX1   1 -1.000000 -0.009850 -0.001055       24.64000    1                    
MTRIX2   1 -0.000966  0.202900 -0.979200      -24.04000    1                    
MTRIX3   1  0.009859 -0.979100 -0.202900      -29.46000    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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