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Database: PDB
Entry: 4EE0
LinkDB: 4EE0
Original site: 4EE0 
HEADER    ISOMERASE/ISOMERASE INHIBITOR           28-MAR-12   4EE0              
TITLE     CRYSTAL STRUCTURE OF HH-PGDS WITH WATER DISPLACING INHIBITOR          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEMATOPOIETIC PROSTAGLANDIN D SYNTHASE;                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: H-PGDS, GST CLASS-SIGMA, GLUTATHIONE S-TRANSFERASE,         
COMPND   5 GLUTATHIONE-DEPENDENT PGD SYNTHASE, GLUTATHIONE-REQUIRING            
COMPND   6 PROSTAGLANDIN D SYNTHASE, PROSTAGLANDIN-H2 D-ISOMERASE;              
COMPND   7 EC: 5.3.99.2, 2.5.1.18;                                              
COMPND   8 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: GSTS, HPGDS, PGDS, PTGDS2;                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    INHIBITOR, SOLVENT REPLACEMENT, ISOMERASE-ISOMERASE INHIBITOR COMPLEX 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.E.DAY,A.THORARENSEN,J.I.TRUJILLO                                    
REVDAT   1   18-JUL-12 4EE0    0                                                
JRNL        AUTH   J.I.TRUJILLO,J.R.KIEFER,W.HUANG,J.E.DAY,J.MOON,G.M.JEROME,   
JRNL        AUTH 2 C.P.BONO,C.M.KORNMEIER,M.L.WILLIAMS,C.KUHN,G.R.RENNIE,       
JRNL        AUTH 3 T.A.WYNN,C.P.CARRON,A.THORARENSEN                            
JRNL        TITL   INVESTIGATION OF THE BINDING POCKET OF HUMAN HEMATOPOIETIC   
JRNL        TITL 2 PROSTAGLANDIN (PG) D2 SYNTHASE (HH-PGDS): A TALE OF TWO      
JRNL        TITL 3 WATERS.                                                      
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  22  3795 2012              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   22546671                                                     
JRNL        DOI    10.1016/J.BMCL.2012.04.004                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.73                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 37441                          
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) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1929                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.74                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.78                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2171                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.71                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2940                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 121                          
REMARK   3   BIN FREE R VALUE                    : 0.3590                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3209                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 99                                      
REMARK   3   SOLVENT ATOMS            : 307                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.71                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.05000                                              
REMARK   3    B22 (A**2) : -0.08000                                             
REMARK   3    B33 (A**2) : 0.01000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.58000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.139         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.124         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.085         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.541         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3413 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2304 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4632 ; 1.062 ; 1.989       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5605 ; 0.828 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   384 ; 4.865 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   161 ;34.267 ;24.099       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   568 ;12.334 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;13.069 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   504 ; 0.059 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3694 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   693 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1948 ; 0.408 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   773 ; 0.091 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3165 ; 0.764 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1465 ; 1.271 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1467 ; 2.036 ; 4.500       
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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   199                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.4239  -0.1560  21.4692              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0158 T22:   0.0162                                     
REMARK   3      T33:   0.0168 T12:  -0.0047                                     
REMARK   3      T13:   0.0136 T23:  -0.0134                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2878 L22:   1.7809                                     
REMARK   3      L33:   1.8519 L12:   0.0235                                     
REMARK   3      L13:   0.3220 L23:   0.1750                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0060 S12:  -0.0117 S13:   0.0210                       
REMARK   3      S21:   0.0147 S22:   0.0176 S23:  -0.0450                       
REMARK   3      S31:   0.0415 S32:   0.0753 S33:  -0.0236                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   199                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.9707 -19.6920   6.8058              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0142 T22:   0.0067                                     
REMARK   3      T33:   0.0070 T12:  -0.0027                                     
REMARK   3      T13:   0.0095 T23:  -0.0030                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8847 L22:   1.3264                                     
REMARK   3      L33:   1.1513 L12:  -0.5905                                     
REMARK   3      L13:   0.4528 L23:   0.0090                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0321 S12:   0.0993 S13:   0.0202                       
REMARK   3      S21:  -0.0736 S22:  -0.0294 S23:   0.0022                       
REMARK   3      S31:  -0.0079 S32:   0.0356 S33:  -0.0027                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4EE0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB071498.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
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 MICROMAX-007                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : OSMIC MIRRORS                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39455                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION                          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       38.93800            
REMARK 290   SMTRY3   2  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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.                         
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: 4090 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     HIS A     1                                                      
REMARK 465     GLN A    36                                                      
REMARK 465     ALA A    37                                                      
REMARK 465     ASP A    38                                                      
REMARK 465     TRP A    39                                                      
REMARK 465     GLU B    35                                                      
REMARK 465     GLN B    36                                                      
REMARK 465     LYS B   107                                                      
REMARK 465     LYS B   108                                                      
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     HIS B   1    CG   ND1  CD2  CE1  NE2                             
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    GLN A  63      107.96     74.09                                   
REMARK 500    GLN B  63      106.86     75.29                                   
REMARK 500    ASP B 110      -68.65     73.25                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 201  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 323   O                                                      
REMARK 620 2 HOH A 318   O    90.9                                              
REMARK 620 3 HOH B 356   O    99.1 170.0                                        
REMARK 620 4 HOH B 349   O   173.7  83.2  86.8                                  
REMARK 620 5 HOH B 317   O    87.5  92.3  87.5  90.5                            
REMARK 620 6 HOH A 334   O    92.1  94.9  85.5  90.6 172.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0O4 A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSF A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0O4 B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSF B 202                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4EDZ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4EDY   RELATED DB: PDB                                   
DBREF  4EE0 A    2   199  UNP    O60760   HPGDS_HUMAN      2    199             
DBREF  4EE0 B    2   199  UNP    O60760   HPGDS_HUMAN      2    199             
SEQADV 4EE0 HIS A    1  UNP  O60760              EXPRESSION TAG                 
SEQADV 4EE0 HIS B    1  UNP  O60760              EXPRESSION TAG                 
SEQRES   1 A  199  HIS PRO ASN TYR LYS LEU THR TYR PHE ASN MET ARG GLY          
SEQRES   2 A  199  ARG ALA GLU ILE ILE ARG TYR ILE PHE ALA TYR LEU ASP          
SEQRES   3 A  199  ILE GLN TYR GLU ASP HIS ARG ILE GLU GLN ALA ASP TRP          
SEQRES   4 A  199  PRO GLU ILE LYS SER THR LEU PRO PHE GLY LYS ILE PRO          
SEQRES   5 A  199  ILE LEU GLU VAL ASP GLY LEU THR LEU HIS GLN SER LEU          
SEQRES   6 A  199  ALA ILE ALA ARG TYR LEU THR LYS ASN THR ASP LEU ALA          
SEQRES   7 A  199  GLY ASN THR GLU MET GLU GLN CYS HIS VAL ASP ALA ILE          
SEQRES   8 A  199  VAL ASP THR LEU ASP ASP PHE MET SER CYS PHE PRO TRP          
SEQRES   9 A  199  ALA GLU LYS LYS GLN ASP VAL LYS GLU GLN MET PHE ASN          
SEQRES  10 A  199  GLU LEU LEU THR TYR ASN ALA PRO HIS LEU MET GLN ASP          
SEQRES  11 A  199  LEU ASP THR TYR LEU GLY GLY ARG GLU TRP LEU ILE GLY          
SEQRES  12 A  199  ASN SER VAL THR TRP ALA ASP PHE TYR TRP GLU ILE CYS          
SEQRES  13 A  199  SER THR THR LEU LEU VAL PHE LYS PRO ASP LEU LEU ASP          
SEQRES  14 A  199  ASN HIS PRO ARG LEU VAL THR LEU ARG LYS LYS VAL GLN          
SEQRES  15 A  199  ALA ILE PRO ALA VAL ALA ASN TRP ILE LYS ARG ARG PRO          
SEQRES  16 A  199  GLN THR LYS LEU                                              
SEQRES   1 B  199  HIS PRO ASN TYR LYS LEU THR TYR PHE ASN MET ARG GLY          
SEQRES   2 B  199  ARG ALA GLU ILE ILE ARG TYR ILE PHE ALA TYR LEU ASP          
SEQRES   3 B  199  ILE GLN TYR GLU ASP HIS ARG ILE GLU GLN ALA ASP TRP          
SEQRES   4 B  199  PRO GLU ILE LYS SER THR LEU PRO PHE GLY LYS ILE PRO          
SEQRES   5 B  199  ILE LEU GLU VAL ASP GLY LEU THR LEU HIS GLN SER LEU          
SEQRES   6 B  199  ALA ILE ALA ARG TYR LEU THR LYS ASN THR ASP LEU ALA          
SEQRES   7 B  199  GLY ASN THR GLU MET GLU GLN CYS HIS VAL ASP ALA ILE          
SEQRES   8 B  199  VAL ASP THR LEU ASP ASP PHE MET SER CYS PHE PRO TRP          
SEQRES   9 B  199  ALA GLU LYS LYS GLN ASP VAL LYS GLU GLN MET PHE ASN          
SEQRES  10 B  199  GLU LEU LEU THR TYR ASN ALA PRO HIS LEU MET GLN ASP          
SEQRES  11 B  199  LEU ASP THR TYR LEU GLY GLY ARG GLU TRP LEU ILE GLY          
SEQRES  12 B  199  ASN SER VAL THR TRP ALA ASP PHE TYR TRP GLU ILE CYS          
SEQRES  13 B  199  SER THR THR LEU LEU VAL PHE LYS PRO ASP LEU LEU ASP          
SEQRES  14 B  199  ASN HIS PRO ARG LEU VAL THR LEU ARG LYS LYS VAL GLN          
SEQRES  15 B  199  ALA ILE PRO ALA VAL ALA ASN TRP ILE LYS ARG ARG PRO          
SEQRES  16 B  199  GLN THR LYS LEU                                              
HET     MG  A 201       1                                                       
HET    0O4  A 202      27                                                       
HET    GSF  A 203      44                                                       
HET    0O4  B 201      27                                                       
HET    GSF  B 202      22                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     0O4 4-(ISOQUINOLIN-1-YL)-N-[2-(MORPHOLIN-4-YL)                       
HETNAM   2 0O4  ETHYL]BENZAMIDE                                                 
HETNAM     GSF L-GAMMA-GLUTAMYL-3-SULFINO-L-ALANYLGLYCINE                       
HETSYN     GSF GLUTATHIONE SULFINATE                                            
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  0O4    2(C22 H23 N3 O2)                                             
FORMUL   5  GSF    2(C10 H17 N3 O8 S)                                           
FORMUL   8  HOH   *307(H2 O)                                                    
HELIX    1   1 ALA A   15  LEU A   25  1                                  11    
HELIX    2   2 GLU A   41  LEU A   46  5                                   6    
HELIX    3   3 GLN A   63  LYS A   73  1                                  11    
HELIX    4   4 THR A   81  CYS A  101  1                                  21    
HELIX    5   5 LYS A  108  TYR A  122  1                                  15    
HELIX    6   6 TYR A  122  GLY A  136  1                                  15    
HELIX    7   7 THR A  147  LYS A  164  1                                  18    
HELIX    8   8 HIS A  171  ILE A  184  1                                  14    
HELIX    9   9 ILE A  184  ARG A  194  1                                  11    
HELIX   10  10 ARG B   12  ARG B   14  5                                   3    
HELIX   11  11 ALA B   15  ASP B   26  1                                  12    
HELIX   12  12 ASP B   38  SER B   44  1                                   7    
HELIX   13  13 GLN B   63  LYS B   73  1                                  11    
HELIX   14  14 THR B   81  PHE B  102  1                                  22    
HELIX   15  15 ASP B  110  ASN B  123  1                                  14    
HELIX   16  16 ASN B  123  GLY B  136  1                                  14    
HELIX   17  17 THR B  147  LYS B  164  1                                  18    
HELIX   18  18 HIS B  171  ILE B  184  1                                  14    
HELIX   19  19 ILE B  184  ARG B  194  1                                  11    
SHEET    1   A 4 GLU A  30  ILE A  34  0                                        
SHEET    2   A 4 TYR A   4  PHE A   9  1  N  LEU A   6   O  GLU A  30           
SHEET    3   A 4 ILE A  53  VAL A  56 -1  O  GLU A  55   N  LYS A   5           
SHEET    4   A 4 LEU A  59  HIS A  62 -1  O  LEU A  59   N  VAL A  56           
SHEET    1   B 4 GLU B  30  ILE B  34  0                                        
SHEET    2   B 4 TYR B   4  PHE B   9  1  N  TYR B   4   O  GLU B  30           
SHEET    3   B 4 ILE B  53  VAL B  56 -1  O  GLU B  55   N  LYS B   5           
SHEET    4   B 4 LEU B  59  HIS B  62 -1  O  LEU B  61   N  LEU B  54           
LINK        MG    MG A 201                 O   HOH A 323     1555   1555  2.00  
LINK        MG    MG A 201                 O   HOH A 318     1555   1555  2.01  
LINK        MG    MG A 201                 O   HOH B 356     1555   1555  2.06  
LINK        MG    MG A 201                 O   HOH B 349     1555   1555  2.08  
LINK        MG    MG A 201                 O   HOH B 317     1555   1555  2.10  
LINK        MG    MG A 201                 O   HOH A 334     1555   1555  2.14  
CISPEP   1 ILE A   34    GLU A   35          0         4.98                     
CISPEP   2 ILE A   51    PRO A   52          0         7.17                     
CISPEP   3 ILE B   51    PRO B   52          0         9.87                     
SITE     1 AC1  6 HOH A 318  HOH A 323  HOH A 334  HOH B 317                    
SITE     2 AC1  6 HOH B 349  HOH B 356                                          
SITE     1 AC2 10 MET A  11  GLY A  13  ARG A  14  ASP A  96                    
SITE     2 AC2 10 MET A  99  TRP A 104  TYR A 152  LEU A 199                    
SITE     3 AC2 10 GSF A 203  HOH A 320                                          
SITE     1 AC3 17 TYR A   8  PHE A   9  ARG A  14  LYS A  43                    
SITE     2 AC3 17 GLY A  49  LYS A  50  ILE A  51  PRO A  52                    
SITE     3 AC3 17 GLN A  63  SER A  64  0O4 A 202  HOH A 326                    
SITE     4 AC3 17 HOH A 327  HOH A 355  HOH A 357  HOH A 398                    
SITE     5 AC3 17 ASP B  97                                                     
SITE     1 AC4 13 PHE B   9  MET B  11  GLY B  13  ARG B  14                    
SITE     2 AC4 13 ASP B  96  MET B  99  SER B 100  TRP B 104                    
SITE     3 AC4 13 TYR B 152  GSF B 202  HOH B 344  HOH B 430                    
SITE     4 AC4 13 HOH B 453                                                     
SITE     1 AC5 16 ASP A  97  TYR B   8  PHE B   9  ARG B  14                    
SITE     2 AC5 16 TRP B  39  LYS B  43  LYS B  50  ILE B  51                    
SITE     3 AC5 16 GLN B  63  SER B  64  0O4 B 201  HOH B 318                    
SITE     4 AC5 16 HOH B 321  HOH B 322  HOH B 325  HOH B 427                    
CRYST1   48.612   77.876   52.560  90.00  91.39  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020571  0.000000  0.000499        0.00000                         
SCALE2      0.000000  0.012841  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019031        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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