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Database: PDB
Entry: 3D8H
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Original site: 3D8H 
HEADER    ISOMERASE                               23-MAY-08   3D8H              
TITLE     CRYSTAL STRUCTURE OF PHOSPHOGLYCERATE MUTASE FROM CRYPTOSPORIDIUM     
TITLE    2 PARVUM, CGD7_4270                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLYCOLYTIC PHOSPHOGLYCERATE MUTASE;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CRYPTOSPORIDIUM PARVUM;                         
SOURCE   3 ORGANISM_TAXID: 353152;                                              
SOURCE   4 STRAIN: IOWA II;                                                     
SOURCE   5 GENE: CGD7_4270;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A-THROMBIN-LIC                       
KEYWDS    STRUCTURAL GENOMICS, MALARIA, CRYPTOSPORIDIUM, GLYCOLYSIS, ISOMERASE, 
KEYWDS   2 STRUCTURAL GENOMICS CONSORTIUM, SGC                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.K.WERNIMONT,J.LEW,G.WASNEY,Z.ALAM,I.KOZIERADZKI,D.COSSAR,           
AUTHOR   2 M.SCHAPIRO,A.BOCHKAREV,C.H.ARROWSMITH,C.BOUNTRA,M.WILKSTROM,         
AUTHOR   3 A.M.EDWARDS,R.HUI,J.D.ARTZ,T.HILLS,STRUCTURAL GENOMICS CONSORTIUM    
AUTHOR   4 (SGC)                                                                
REVDAT   5   07-SEP-11 3D8H    1       JRNL                                     
REVDAT   4   24-AUG-11 3D8H    1       JRNL                                     
REVDAT   3   13-JUL-11 3D8H    1       VERSN                                    
REVDAT   2   24-FEB-09 3D8H    1       VERSN                                    
REVDAT   1   15-JUL-08 3D8H    0                                                
JRNL        AUTH   T.HILLS,A.SRIVASTAVA,K.AYI,A.K.WERNIMONT,K.KAIN,A.P.WATERS,  
JRNL        AUTH 2 R.HUI,J.C.PIZARRO                                            
JRNL        TITL   CHARACTERIZATION OF A NEW PHOSPHATASE FROM PLASMODIUM.       
JRNL        REF    MOL.BIOCHEM.PARASITOL.        V. 179    69 2011              
JRNL        REFN                   ISSN 0166-6851                               
JRNL        PMID   21689687                                                     
JRNL        DOI    10.1016/J.MOLBIOPARA.2011.06.001                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.01 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.01                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.50                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 39074                          
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) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.231                           
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      : 1958                            
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) : 2.01                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.06                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2630                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.29                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2820                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 134                          
REMARK   3   BIN FREE R VALUE                    : 0.3510                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3641                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 206                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 35.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.80000                                              
REMARK   3    B22 (A**2) : -0.25000                                             
REMARK   3    B33 (A**2) : -1.55000                                             
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): 0.200         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.169         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.149         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.193        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.941                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.933                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3755 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5112 ; 1.141 ; 1.975       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   469 ; 5.920 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   152 ;33.578 ;24.474       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   652 ;14.967 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;17.109 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   582 ; 0.081 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2785 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1747 ; 0.185 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2560 ; 0.299 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   212 ; 0.129 ; 0.200       
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):    38 ; 0.140 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.127 ; 0.200       
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):  2416 ; 0.384 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3777 ; 0.647 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1582 ; 1.020 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1331 ; 1.504 ; 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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    197       A     205      3                      
REMARK   3           1     B    197       B     205      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    B    (A):     36 ; 0.030 ; 0.050           
REMARK   3   LOOSE POSITIONAL   1    B    (A):     26 ; 0.120 ; 5.000           
REMARK   3   TIGHT THERMAL      1    B (A**2):     36 ; 0.100 ; 0.500           
REMARK   3   LOOSE THERMAL      1    B (A**2):     26 ; 0.810 ;10.000           
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   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3D8H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAY-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB047724.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-APR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E+ SUPERBRIGHT           
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39125                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.010                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : 0.07500                            
REMARK 200  R SYM                      (I) : 0.04600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.79600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.79600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.320                              
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 1XQ9                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 0.2 M NH4OAC, 0.1 M        
REMARK 280  HEPES PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 273K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.12450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       70.12450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       26.12400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       79.18250            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       26.12400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       79.18250            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       70.12450            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       26.12400            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       79.18250            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       70.12450            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       26.12400            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       79.18250            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20420 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.7 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     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     HIS A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     HIS A     8                                                      
REMARK 465     HIS A     9                                                      
REMARK 465     HIS A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     SER A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     LEU A    14                                                      
REMARK 465     VAL A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     ARG A    17                                                      
REMARK 465     GLY A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     SER A   249                                                      
REMARK 465     GLU A   250                                                      
REMARK 465     GLU A   251                                                      
REMARK 465     GLU A   252                                                      
REMARK 465     LEU A   253                                                      
REMARK 465     LYS A   254                                                      
REMARK 465     ALA A   255                                                      
REMARK 465     LYS A   256                                                      
REMARK 465     MET A   257                                                      
REMARK 465     GLU A   258                                                      
REMARK 465     ALA A   259                                                      
REMARK 465     VAL A   260                                                      
REMARK 465     ALA A   261                                                      
REMARK 465     ASN A   262                                                      
REMARK 465     GLN A   263                                                      
REMARK 465     GLY A   264                                                      
REMARK 465     LYS A   265                                                      
REMARK 465     ALA A   266                                                      
REMARK 465     LYS A   267                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     HIS B     5                                                      
REMARK 465     HIS B     6                                                      
REMARK 465     HIS B     7                                                      
REMARK 465     HIS B     8                                                      
REMARK 465     HIS B     9                                                      
REMARK 465     HIS B    10                                                      
REMARK 465     SER B    11                                                      
REMARK 465     SER B    12                                                      
REMARK 465     GLY B    13                                                      
REMARK 465     LEU B    14                                                      
REMARK 465     VAL B    15                                                      
REMARK 465     SER B   249                                                      
REMARK 465     GLU B   252                                                      
REMARK 465     LEU B   253                                                      
REMARK 465     LYS B   254                                                      
REMARK 465     ALA B   255                                                      
REMARK 465     LYS B   256                                                      
REMARK 465     MET B   257                                                      
REMARK 465     GLU B   258                                                      
REMARK 465     ALA B   259                                                      
REMARK 465     VAL B   260                                                      
REMARK 465     ALA B   261                                                      
REMARK 465     ASN B   262                                                      
REMARK 465     GLN B   263                                                      
REMARK 465     GLY B   264                                                      
REMARK 465     LYS B   265                                                      
REMARK 465     ALA B   266                                                      
REMARK 465     LYS B   267                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  38    CZ   NH1  NH2                                       
REMARK 470     LYS A 123    CG   CD   CE   NZ                                   
REMARK 470     ARG A 133    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 134    CZ   NH1  NH2                                       
REMARK 470     LYS A 145    CE   NZ                                             
REMARK 470     GLU A 222    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 224    CG   OD1  ND2                                       
REMARK 470     LYS A 240    CD   CE   NZ                                        
REMARK 470     ILE A 248    CG1  CG2  CD1                                       
REMARK 470     ARG B  17    NE   CZ   NH1  NH2                                  
REMARK 470     LYS B 123    CG   CD   CE   NZ                                   
REMARK 470     ASP B 127    CG   OD1  OD2                                       
REMARK 470     VAL B 129    CG1  CG2                                            
REMARK 470     ARG B 133    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 134    CZ   NH1  NH2                                       
REMARK 470     GLU B 144    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 145    CG   CD   CE   NZ                                   
REMARK 470     GLU B 218    CD   OE1  OE2                                       
REMARK 470     GLU B 222    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 224    CG   OD1  ND2                                       
REMARK 470     ILE B 225    CD1                                                 
REMARK 470     LYS B 240    CE   NZ                                             
REMARK 470     ILE B 248    CG1  CG2  CD1                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLN A 219   CD    GLN A 219   OE1     0.234                       
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    THR A  40      -65.17   -101.40                                   
REMARK 500    ASN A  93       33.58   -143.53                                   
REMARK 500    VAL A 185      -58.34   -120.95                                   
REMARK 500    ALA A 200     -138.54   -145.83                                   
REMARK 500    ASN B 116     -169.29    -71.72                                   
REMARK 500    PHE B 124     -163.63   -122.49                                   
REMARK 500    VAL B 185      -57.61   -120.04                                   
REMARK 500    ALA B 200     -133.64   -149.99                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3D8H A   20   267  UNP    Q5CXZ9   Q5CXZ9_CRYPV     2    249             
DBREF  3D8H B   20   266  UNP    Q5CXZ9   Q5CXZ9_CRYPV     2    249             
SEQADV 3D8H MET A    1  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H GLY A    2  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H SER A    3  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H SER A    4  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H HIS A    5  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H HIS A    6  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H HIS A    7  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H HIS A    8  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H HIS A    9  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H HIS A   10  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H SER A   11  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H SER A   12  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H GLY A   13  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H LEU A   14  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H VAL A   15  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H PRO A   16  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H ARG A   17  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H GLY A   18  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H SER A   19  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H MET B    1  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H GLY B    2  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H SER B    3  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H SER B    4  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H HIS B    5  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H HIS B    6  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H HIS B    7  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H HIS B    8  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H HIS B    9  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H HIS B   10  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H SER B   11  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H SER B   12  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H GLY B   13  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H LEU B   14  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H VAL B   15  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H PRO B   16  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H ARG B   17  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H GLY B   18  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQADV 3D8H SER B   19  UNP  Q5CXZ9              EXPRESSION TAG                 
SEQRES   1 A  267  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  267  LEU VAL PRO ARG GLY SER THR TYR LYS LEU THR LEU ILE          
SEQRES   3 A  267  ARG HIS GLY GLU SER GLU TRP ASN LYS GLU ASN ARG PHE          
SEQRES   4 A  267  THR GLY TRP THR ASP VAL SER LEU SER GLU GLN GLY VAL          
SEQRES   5 A  267  SER GLU ALA ILE GLU ALA GLY ARG MET LEU LEU GLU LYS          
SEQRES   6 A  267  GLY PHE LYS PHE ASP VAL VAL TYR THR SER VAL LEU LYS          
SEQRES   7 A  267  ARG ALA ILE MET THR THR TRP THR VAL LEU LYS GLU LEU          
SEQRES   8 A  267  GLY ASN ILE ASN CYS PRO ILE ILE ASN HIS TRP ARG LEU          
SEQRES   9 A  267  ASN GLU ARG HIS TYR GLY ALA LEU GLN GLY LEU ASN LYS          
SEQRES  10 A  267  SER GLU THR ALA SER LYS PHE GLY GLU ASP GLN VAL LYS          
SEQRES  11 A  267  ILE TRP ARG ARG SER PHE ASP VAL PRO PRO PRO VAL LEU          
SEQRES  12 A  267  GLU LYS SER ASP PRO ARG TRP PRO GLY ASN GLU LEU ILE          
SEQRES  13 A  267  TYR LYS GLY ILE CYS PRO SER CYS LEU PRO THR THR GLU          
SEQRES  14 A  267  CYS LEU LYS ASP THR VAL GLU ARG VAL LYS PRO TYR PHE          
SEQRES  15 A  267  GLU ASP VAL ILE ALA PRO SER ILE MET SER GLY LYS SER          
SEQRES  16 A  267  VAL LEU VAL SER ALA HIS GLY ASN SER LEU ARG ALA LEU          
SEQRES  17 A  267  LEU TYR LEU LEU GLU GLY MET THR PRO GLU GLN ILE LEU          
SEQRES  18 A  267  GLU VAL ASN ILE PRO THR ALA CYS PRO LEU VAL LEU GLU          
SEQRES  19 A  267  LEU ASP ASP TYR LEU LYS VAL THR LYS LYS TYR TYR LEU          
SEQRES  20 A  267  ILE SER GLU GLU GLU LEU LYS ALA LYS MET GLU ALA VAL          
SEQRES  21 A  267  ALA ASN GLN GLY LYS ALA LYS                                  
SEQRES   1 B  267  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  267  LEU VAL PRO ARG GLY SER THR TYR LYS LEU THR LEU ILE          
SEQRES   3 B  267  ARG HIS GLY GLU SER GLU TRP ASN LYS GLU ASN ARG PHE          
SEQRES   4 B  267  THR GLY TRP THR ASP VAL SER LEU SER GLU GLN GLY VAL          
SEQRES   5 B  267  SER GLU ALA ILE GLU ALA GLY ARG MET LEU LEU GLU LYS          
SEQRES   6 B  267  GLY PHE LYS PHE ASP VAL VAL TYR THR SER VAL LEU LYS          
SEQRES   7 B  267  ARG ALA ILE MET THR THR TRP THR VAL LEU LYS GLU LEU          
SEQRES   8 B  267  GLY ASN ILE ASN CYS PRO ILE ILE ASN HIS TRP ARG LEU          
SEQRES   9 B  267  ASN GLU ARG HIS TYR GLY ALA LEU GLN GLY LEU ASN LYS          
SEQRES  10 B  267  SER GLU THR ALA SER LYS PHE GLY GLU ASP GLN VAL LYS          
SEQRES  11 B  267  ILE TRP ARG ARG SER PHE ASP VAL PRO PRO PRO VAL LEU          
SEQRES  12 B  267  GLU LYS SER ASP PRO ARG TRP PRO GLY ASN GLU LEU ILE          
SEQRES  13 B  267  TYR LYS GLY ILE CYS PRO SER CYS LEU PRO THR THR GLU          
SEQRES  14 B  267  CYS LEU LYS ASP THR VAL GLU ARG VAL LYS PRO TYR PHE          
SEQRES  15 B  267  GLU ASP VAL ILE ALA PRO SER ILE MET SER GLY LYS SER          
SEQRES  16 B  267  VAL LEU VAL SER ALA HIS GLY ASN SER LEU ARG ALA LEU          
SEQRES  17 B  267  LEU TYR LEU LEU GLU GLY MET THR PRO GLU GLN ILE LEU          
SEQRES  18 B  267  GLU VAL ASN ILE PRO THR ALA CYS PRO LEU VAL LEU GLU          
SEQRES  19 B  267  LEU ASP ASP TYR LEU LYS VAL THR LYS LYS TYR TYR LEU          
SEQRES  20 B  267  ILE SER GLU GLU GLU LEU LYS ALA LYS MET GLU ALA VAL          
SEQRES  21 B  267  ALA ASN GLN GLY LYS ALA LYS                                  
FORMUL   3  HOH   *206(H2 O)                                                    
HELIX    1   1 SER A   48  LYS A   65  1                                  18    
HELIX    2   2 LEU A   77  GLY A   92  1                                  16    
HELIX    3   3 TRP A  102  ASN A  105  5                                   4    
HELIX    4   4 TYR A  109  GLN A  113  5                                   5    
HELIX    5   5 ASN A  116  PHE A  124  1                                   9    
HELIX    6   6 GLY A  125  SER A  135  1                                  11    
HELIX    7   7 TRP A  150  LYS A  158  5                                   9    
HELIX    8   8 CYS A  161  LEU A  165  5                                   5    
HELIX    9   9 CYS A  170  VAL A  185  1                                  16    
HELIX   10  10 VAL A  185  SER A  192  1                                   8    
HELIX   11  11 HIS A  201  GLY A  214  1                                  14    
HELIX   12  12 THR A  216  LEU A  221  1                                   6    
HELIX   13  13 SER B   31  GLU B   36  1                                   6    
HELIX   14  14 SER B   48  LYS B   65  1                                  18    
HELIX   15  15 LEU B   77  LEU B   91  1                                  15    
HELIX   16  16 TRP B  102  ASN B  105  5                                   4    
HELIX   17  17 TYR B  109  GLN B  113  5                                   5    
HELIX   18  18 SER B  118  PHE B  124  1                                   7    
HELIX   19  19 GLY B  125  SER B  135  1                                  11    
HELIX   20  20 TRP B  150  LYS B  158  5                                   9    
HELIX   21  21 CYS B  161  LEU B  165  5                                   5    
HELIX   22  22 CYS B  170  VAL B  185  1                                  16    
HELIX   23  23 VAL B  185  SER B  192  1                                   8    
HELIX   24  24 HIS B  201  GLY B  214  1                                  14    
HELIX   25  25 THR B  216  GLU B  222  1                                   7    
SHEET    1   A 6 ILE A  98  ASN A 100  0                                        
SHEET    2   A 6 VAL A  71  THR A  74  1  N  VAL A  72   O  ILE A  99           
SHEET    3   A 6 VAL A 196  ALA A 200  1  O  SER A 199   N  TYR A  73           
SHEET    4   A 6 TYR A  21  ARG A  27  1  N  THR A  24   O  VAL A 198           
SHEET    5   A 6 LEU A 231  LEU A 235 -1  O  LEU A 233   N  LEU A  23           
SHEET    6   A 6 VAL A 241  TYR A 246 -1  O  TYR A 245   N  VAL A 232           
SHEET    1   B 6 ILE B  98  ASN B 100  0                                        
SHEET    2   B 6 VAL B  71  THR B  74  1  N  VAL B  72   O  ILE B  99           
SHEET    3   B 6 VAL B 196  ALA B 200  1  O  SER B 199   N  TYR B  73           
SHEET    4   B 6 TYR B  21  ARG B  27  1  N  THR B  24   O  VAL B 198           
SHEET    5   B 6 LEU B 231  LEU B 235 -1  O  LEU B 233   N  LEU B  23           
SHEET    6   B 6 VAL B 241  TYR B 246 -1  O  LYS B 243   N  GLU B 234           
CRYST1   52.248  158.365  140.249  90.00  90.00  90.00 C 2 2 21     16          
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      0.019139  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006315  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007130        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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