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Database: PDB
Entry: 3NRF
LinkDB: 3NRF
Original site: 3NRF 
HEADER    STRUCTURAL GENOMICS, UNKNOWN FUNCTION   30-JUN-10   3NRF              
TITLE     CRYSTAL STRUCTURE OF AN APAG PROTEIN (PA1934) FROM PSEUDOMONAS        
TITLE    2 AERUGINOSA PAO1 AT 1.50 A RESOLUTION                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: APAG PROTEIN;                                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 287;                                                 
SOURCE   4 GENE: PA1934;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: HK100;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: SPEEDET                                   
KEYWDS    STRUCTURAL GENOMICS, JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG,      
KEYWDS   2 PROTEIN STRUCTURE INITIATIVE, PSI-2, UNKNOWN FUNCTION                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)                           
REVDAT   5   17-JUL-19 3NRF    1       REMARK LINK                              
REVDAT   4   08-NOV-17 3NRF    1       REMARK                                   
REVDAT   3   16-NOV-11 3NRF    1       TITLE                                    
REVDAT   2   20-JUL-11 3NRF    1       HEADER                                   
REVDAT   1   28-JUL-10 3NRF    0                                                
JRNL        AUTH   JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)                  
JRNL        TITL   CRYSTAL STRUCTURE OF AN APAG PROTEIN (PA1934) FROM           
JRNL        TITL 2 PSEUDOMONAS AERUGINOSA AT 1.50 A RESOLUTION                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0110                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.18                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 32812                          
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) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1666                            
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) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2229                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.65                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2740                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 108                          
REMARK   3   BIN FREE R VALUE                    : 0.3100                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1508                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 212                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.85                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.29                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.21000                                              
REMARK   3    B22 (A**2) : -0.52000                                             
REMARK   3    B33 (A**2) : -0.68000                                             
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.084         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.062         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.387         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.946                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1706 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1155 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2341 ; 1.697 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2837 ; 0.895 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   250 ; 4.317 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    80 ;31.772 ;24.250       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   297 ; 9.911 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;11.653 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   274 ; 0.107 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1988 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   352 ; 0.002 ; 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):  1091 ; 3.608 ;35.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   445 ; 2.687 ;35.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1761 ; 4.366 ; 8.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   615 ; 3.637 ;11.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   558 ; 4.053 ; 4.500       
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  : 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    25        A   126                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.4095  13.1912  27.0536              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0394 T22:   0.0594                                     
REMARK   3      T33:   0.0592 T12:   0.0081                                     
REMARK   3      T13:  -0.0203 T23:   0.0018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8374 L22:   1.1659                                     
REMARK   3      L33:   0.5640 L12:   0.5720                                     
REMARK   3      L13:  -0.2835 L23:  -0.1165                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0537 S12:   0.0926 S13:  -0.0781                       
REMARK   3      S21:  -0.0764 S22:  -0.0348 S23:   0.0551                       
REMARK   3      S31:  -0.0278 S32:  -0.0539 S33:  -0.0189                       
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    23        B   125                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.9751  13.3357  51.5627              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0726 T22:   0.0472                                     
REMARK   3      T33:   0.0647 T12:   0.0119                                     
REMARK   3      T13:  -0.0175 T23:  -0.0028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6488 L22:   1.0837                                     
REMARK   3      L33:   1.7229 L12:   0.1956                                     
REMARK   3      L13:  -0.2165 L23:   0.2822                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1137 S12:  -0.0855 S13:  -0.0644                       
REMARK   3      S21:   0.1987 S22:  -0.0088 S23:   0.1332                       
REMARK   3      S31:   0.1206 S32:  -0.0389 S33:  -0.1049                       
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: 1. HYDROGENS HAVE BEEN ADDED IN THE       
REMARK   3  RIDING POSITIONS. 2. ATOM RECORD CONTAINS SUM OF TLS AND            
REMARK   3  RESIDUAL B FACTORS. 3. ANISOU RECORD CONTAINS SUM OF TLS AND        
REMARK   3  RESIDUAL U FACTORS. 4. A MET-INHIBITION PROTOCOL WAS USED FOR       
REMARK   3  SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE       
REMARK   3  OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO        
REMARK   3  0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET          
REMARK   3  INCORPORATION. 5.(4R)-2-METHYL- 2,4-PENTANEDIOL (MRD),AND           
REMARK   3  CACODYLATE (CAC) FROM THE CRYSTALLIZATION WERE MODELED INTO THE     
REMARK   3  STRUCTURE. THE MODELING OF CACODYLATE IS SUPPORTED BY ANOMALOUS     
REMARK   3  DIFFERENCE MAPS. 5. SOLVENT MOLECULES WERE EXCLUDED FROM THE        
REMARK   3  ASSIGNMENT OF THE TLS GROUPS.                                       
REMARK   4                                                                      
REMARK   4 3NRF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUL-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000060186.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-MAY-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91837,0.97936,0.97922            
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : FLAT COLLIMATING MIRROR, TOROID    
REMARK 200                                   FOCUSING MIRROR                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.15                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32823                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.178                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.79800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHELX, AUTOSHARP                                      
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 40.000000000% MPD, 5.000000000% PEG      
REMARK 280  -8000, 0.1M CACODYLATE PH 6.5, NANODROP, VAPOR DIFFUSION,           
REMARK 280  SITTING DROP, TEMPERATURE 277K                                      
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       30.89400            
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       30.89400            
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       34.67150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       48.24550            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       34.67150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       48.24550            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       30.89400            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       34.67150            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       48.24550            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       30.89400            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       34.67150            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       48.24550            
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 300 REMARK: CRYSTAL PACKING ANALYSIS SUGGESTS THE ASSIGNMENT OF A        
REMARK 300 TETRAMER AS A SIGNIFICANT OLIGOMERIZATION STATE.                     
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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 350   BIOMT1   2 -1.000000  0.000000  0.000000       69.34300            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       92.68200            
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     GLY A     0                                                      
REMARK 465     ALA A    22                                                      
REMARK 465     ALA A    23                                                      
REMARK 465     PRO A    24                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     ALA B    22                                                      
REMARK 465     LYS B   126                                                      
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     ASP A  25    CG   OD1  OD2                                       
REMARK 470     LYS A  60    CG   CD   CE   NZ                                   
REMARK 470     LYS A 126    CG   CD   CE   NZ                                   
REMARK 470     ARG B  32    CZ   NH1  NH2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP B  25       48.30    -82.37                                   
REMARK 500    ASP B 110     -157.64   -100.12                                   
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 MRD A 128                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD B 127                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MRD B 129                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAC B 130                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 416839   RELATED DB: TARGETDB                            
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THIS CONSTRUCT (RESIDUES 22-126) WAS EXPRESSED WITH A PURIFICATION   
REMARK 999 TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE       
REMARK 999 LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE           
DBREF  3NRF A   22   126  UNP    Q9I2H0   Q9I2H0_PSEAE    22    126             
DBREF  3NRF B   22   126  UNP    Q9I2H0   Q9I2H0_PSEAE    22    126             
SEQADV 3NRF GLY A    0  UNP  Q9I2H0              LEADER SEQUENCE                
SEQADV 3NRF GLY B    0  UNP  Q9I2H0              LEADER SEQUENCE                
SEQRES   1 A  106  GLY ALA ALA PRO ASP ALA VAL MSE VAL PHE ALA ARG GLN          
SEQRES   2 A  106  GLY ASP LYS GLY SER VAL SER VAL GLY ASP LYS HIS PHE          
SEQRES   3 A  106  ARG THR GLN ALA PHE LYS VAL ARG LEU VAL ASN ALA ALA          
SEQRES   4 A  106  LYS SER GLU ILE SER LEU LYS ASN SER CYS LEU VAL ALA          
SEQRES   5 A  106  GLN SER ALA ALA GLY GLN SER PHE ARG LEU ASP THR VAL          
SEQRES   6 A  106  ASP GLU GLU LEU THR ALA ASP THR LEU LYS PRO GLY ALA          
SEQRES   7 A  106  SER VAL GLU GLY ASP ALA ILE PHE ALA SER GLU ASP ASP          
SEQRES   8 A  106  ALA VAL TYR GLY ALA SER LEU VAL ARG LEU SER ASP ARG          
SEQRES   9 A  106  CYS LYS                                                      
SEQRES   1 B  106  GLY ALA ALA PRO ASP ALA VAL MSE VAL PHE ALA ARG GLN          
SEQRES   2 B  106  GLY ASP LYS GLY SER VAL SER VAL GLY ASP LYS HIS PHE          
SEQRES   3 B  106  ARG THR GLN ALA PHE LYS VAL ARG LEU VAL ASN ALA ALA          
SEQRES   4 B  106  LYS SER GLU ILE SER LEU LYS ASN SER CYS LEU VAL ALA          
SEQRES   5 B  106  GLN SER ALA ALA GLY GLN SER PHE ARG LEU ASP THR VAL          
SEQRES   6 B  106  ASP GLU GLU LEU THR ALA ASP THR LEU LYS PRO GLY ALA          
SEQRES   7 B  106  SER VAL GLU GLY ASP ALA ILE PHE ALA SER GLU ASP ASP          
SEQRES   8 B  106  ALA VAL TYR GLY ALA SER LEU VAL ARG LEU SER ASP ARG          
SEQRES   9 B  106  CYS LYS                                                      
MODRES 3NRF MSE A   28  MET  SELENOMETHIONINE                                   
MODRES 3NRF MSE B   28  MET  SELENOMETHIONINE                                   
HET    MSE  A  28       8                                                       
HET    MSE  B  28       8                                                       
HET    MRD  A 128       8                                                       
HET    MRD  B 127       8                                                       
HET    MRD  B 129       8                                                       
HET    CAC  B 130       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     MRD (4R)-2-METHYLPENTANE-2,4-DIOL                                    
HETNAM     CAC CACODYLATE ION                                                   
HETSYN     CAC DIMETHYLARSINATE                                                 
FORMUL   1  MSE    2(C5 H11 N O2 SE)                                            
FORMUL   3  MRD    3(C6 H14 O2)                                                 
FORMUL   6  CAC    C2 H6 AS O2 1-                                               
FORMUL   7  HOH   *212(H2 O)                                                    
HELIX    1   1 GLU A   87  ALA A   91  5                                   5    
HELIX    2   2 ASP A  111  TYR A  114  5                                   4    
HELIX    3   3 GLU B   87  ALA B   91  5                                   5    
HELIX    4   4 ASP B  111  ALA B  116  5                                   6    
SHEET    1   A12 ALA A 116  SER A 122  0                                        
SHEET    2   A12 CYS A  69  SER A  74 -1  N  CYS A  69   O  SER A 122           
SHEET    3   A12 SER A  79  VAL A  85 -1  O  PHE A  80   N  ALA A  72           
SHEET    4   A12 SER A  99  SER A 108 -1  O  ILE A 105   N  ASP A  83           
SHEET    5   A12 LYS A  44  VAL A  56 -1  N  ARG A  47   O  SER A 108           
SHEET    6   A12 MSE A  28  VAL A  41 -1  N  VAL A  41   O  LYS A  44           
SHEET    7   A12 VAL B  27  VAL B  41 -1  O  SER B  40   N  VAL A  29           
SHEET    8   A12 LYS B  44  ASN B  57 -1  O  ALA B  50   N  GLY B  34           
SHEET    9   A12 SER B  99  SER B 108 -1  O  SER B 108   N  ARG B  47           
SHEET   10   A12 SER B  79  VAL B  85 -1  N  THR B  84   O  ILE B 105           
SHEET   11   A12 CYS B  69  GLN B  73 -1  N  ALA B  72   O  PHE B  80           
SHEET   12   A12 LEU B 118  SER B 122 -1  O  ARG B 120   N  VAL B  71           
SHEET    1   B 2 ILE A  63  SER A  64  0                                        
SHEET    2   B 2 THR A  93  LEU A  94 -1  O  LEU A  94   N  ILE A  63           
SHEET    1   C 2 ILE B  63  SER B  64  0                                        
SHEET    2   C 2 THR B  93  LEU B  94 -1  O  LEU B  94   N  ILE B  63           
SSBOND   1 CYS A   69    CYS A  125                          1555   1555  2.08  
SSBOND   2 CYS B   69    CYS B  125                          1555   1555  2.04  
LINK         C   VAL A  27                 N   MSE A  28     1555   1555  1.33  
LINK         C   MSE A  28                 N   VAL A  29     1555   1555  1.32  
LINK         C   VAL B  27                 N   MSE B  28     1555   1555  1.32  
LINK         C   MSE B  28                 N   VAL B  29     1555   1555  1.32  
SITE     1 AC1  4 PHE A  30  ARG A  32  LYS A  52  GLU A 101                    
SITE     1 AC2  2 LYS B  52  GLU B 101                                          
SITE     1 AC3  3 THR B  84  VAL B  85  ASP B  86                               
SITE     1 AC4  9 ARG A 120  SER A 122  ARG A 124  HOH A 311                    
SITE     2 AC4  9 GLN B  73  SER B  79  ARG B 120  SER B 122                    
SITE     3 AC4  9 HOH B 310                                                     
CRYST1   69.343   96.491   61.788  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      0.014421  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010364  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016184        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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