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Database: PDB
Entry: 3GFP
LinkDB: 3GFP
Original site: 3GFP 
HEADER    HYDROLASE                               27-FEB-09   3GFP              
TITLE     STRUCTURE OF THE C-TERMINAL DOMAIN OF THE DEAD-BOX PROTEIN DBP5       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DEAD BOX PROTEIN 5;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: HELICASE C-TERMINAL DOMAIN;                                
COMPND   5 SYNONYM: ATP-DEPENDENT RNA HELICASE DBP5, HELICASE CA5/6, RIBONUCLEIC
COMPND   6 ACID-TRAFFICKING PROTEIN 8;                                          
COMPND   7 EC: 3.6.1.-;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: YEAST;                                              
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 GENE: DBP5, RAT8, YOR046C;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 DE3 RIL;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET                                        
KEYWDS    MRNA EXPORT, ATPASE, RECA-FOLD, ATP-BINDING, HELICASE, HYDROLASE,     
KEYWDS   2 MEMBRANE, MRNA TRANSPORT, NUCLEAR PORE COMPLEX, NUCLEOTIDE-BINDING,  
KEYWDS   3 NUCLEUS, PHOSPHOPROTEIN, PROTEIN TRANSPORT, RNA-BINDING,             
KEYWDS   4 TRANSLOCATION, TRANSPORT                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.P.ERZBERGER,Z.Y.DOSSANI,C.S.WEIRICH,K.WEIS,J.M.BERGER               
REVDAT   3   13-JUL-11 3GFP    1       VERSN                                    
REVDAT   2   13-OCT-09 3GFP    1       JRNL                                     
REVDAT   1   01-SEP-09 3GFP    0                                                
JRNL        AUTH   Z.Y.DOSSANI,C.S.WEIRICH,J.P.ERZBERGER,J.M.BERGER,K.WEIS      
JRNL        TITL   STRUCTURE OF THE C-TERMINUS OF THE MRNA EXPORT FACTOR DBP5   
JRNL        TITL 2 REVEALS THE INTERACTION SURFACE FOR THE ATPASE ACTIVATOR     
JRNL        TITL 3 GLE1                                                         
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 106 16251 2009              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   19805289                                                     
JRNL        DOI    10.1073/PNAS.0902251106                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 19340                          
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) : 0.193                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1016                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1404                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.73                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2300                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 80                           
REMARK   3   BIN FREE R VALUE                    : 0.2860                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1422                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 153                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 25.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.96                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.82000                                             
REMARK   3    B22 (A**2) : -0.82000                                             
REMARK   3    B33 (A**2) : 1.23000                                              
REMARK   3    B12 (A**2) : -0.41000                                             
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): 0.123         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.121         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.076         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.320         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.938                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1451 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1959 ; 0.956 ; 1.959       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   180 ; 5.219 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    66 ;30.504 ;24.242       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   268 ;14.028 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    10 ;18.491 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   228 ; 0.073 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1069 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   738 ; 0.207 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1022 ; 0.305 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   119 ; 0.146 ; 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):    57 ; 0.156 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    22 ; 0.149 ; 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):   919 ; 0.851 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1454 ; 1.251 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   588 ; 2.011 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   505 ; 2.965 ; 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   300        A   479                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.9794 -19.9272  -8.4130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0285 T22:  -0.0326                                     
REMARK   3      T33:  -0.0399 T12:  -0.0184                                     
REMARK   3      T13:  -0.0466 T23:   0.0337                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0484 L22:   1.3285                                     
REMARK   3      L33:   0.7842 L12:  -0.2151                                     
REMARK   3      L13:   0.1901 L23:  -0.0990                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1296 S12:   0.0642 S13:   0.1011                       
REMARK   3      S21:   0.0240 S22:   0.0543 S23:  -0.0772                       
REMARK   3      S31:  -0.0900 S32:   0.0649 S33:   0.0753                       
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 :   A     1        A   153                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.7709 -20.7604  -9.6589              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0344 T22:  -0.0096                                     
REMARK   3      T33:  -0.0479 T12:  -0.0090                                     
REMARK   3      T13:  -0.0237 T23:   0.0351                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4479 L22:   1.0719                                     
REMARK   3      L33:   0.4110 L12:  -0.2593                                     
REMARK   3      L13:   0.1624 L23:  -0.1058                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1049 S12:   0.0778 S13:   0.0472                       
REMARK   3      S21:   0.0156 S22:   0.0276 S23:  -0.0478                       
REMARK   3      S31:  -0.0411 S32:   0.0162 S33:   0.0773                       
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   : 1.20                                          
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 3GFP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-MAR-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB051801.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-NOV-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795,1.0332,1.11588              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24212                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 56.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.04000                            
REMARK 200  R SYM                      (I) : NULL                               
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: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M NA/K HPO4, 100MM NA CACODYLATE PH     
REMARK 280  6.5, 8% GLYCEROL, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+2/3                                            
REMARK 290       6555   X-Y,X,Z+1/3                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.71867            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       18.85933            
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  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       37.71867            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       18.85933            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A   2  LIES ON A SPECIAL POSITION.                          
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   294                                                      
REMARK 465     ALA A   295                                                      
REMARK 465     THR A   296                                                      
REMARK 465     ASN A   297                                                      
REMARK 465     GLU A   298                                                      
REMARK 465     VAL A   299                                                      
REMARK 465     LEU A   480                                                      
REMARK 465     LYS A   481                                                      
REMARK 465     ASP A   482                                                      
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    LYS A 478      -71.08    -59.01                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 114        DISTANCE =  5.78 ANGSTROMS                       
DBREF  3GFP A  296   482  UNP    P20449   DBP5_YEAST     296    482             
SEQADV 3GFP GLY A  294  UNP  P20449              EXPRESSION TAG                 
SEQADV 3GFP ALA A  295  UNP  P20449              EXPRESSION TAG                 
SEQRES   1 A  189  GLY ALA THR ASN GLU VAL ASN VAL ASP ALA ILE LYS GLN          
SEQRES   2 A  189  LEU TYR MSE ASP CYS LYS ASN GLU ALA ASP LYS PHE ASP          
SEQRES   3 A  189  VAL LEU THR GLU LEU TYR GLY LEU MSE THR ILE GLY SER          
SEQRES   4 A  189  SER ILE ILE PHE VAL ALA THR LYS LYS THR ALA ASN VAL          
SEQRES   5 A  189  LEU TYR GLY LYS LEU LYS SER GLU GLY HIS GLU VAL SER          
SEQRES   6 A  189  ILE LEU HIS GLY ASP LEU GLN THR GLN GLU ARG ASP ARG          
SEQRES   7 A  189  LEU ILE ASP ASP PHE ARG GLU GLY ARG SER LYS VAL LEU          
SEQRES   8 A  189  ILE THR THR ASN VAL LEU ALA ARG GLY ILE ASP ILE PRO          
SEQRES   9 A  189  THR VAL SER MSE VAL VAL ASN TYR ASP LEU PRO THR LEU          
SEQRES  10 A  189  ALA ASN GLY GLN ALA ASP PRO ALA THR TYR ILE HIS ARG          
SEQRES  11 A  189  ILE GLY ARG THR GLY ARG PHE GLY ARG LYS GLY VAL ALA          
SEQRES  12 A  189  ILE SER PHE VAL HIS ASP LYS ASN SER PHE ASN ILE LEU          
SEQRES  13 A  189  SER ALA ILE GLN LYS TYR PHE GLY ASP ILE GLU MSE THR          
SEQRES  14 A  189  ARG VAL PRO THR ASP ASP TRP ASP GLU VAL GLU LYS ILE          
SEQRES  15 A  189  VAL LYS LYS VAL LEU LYS ASP                                  
MODRES 3GFP MSE A  309  MET  SELENOMETHIONINE                                   
MODRES 3GFP MSE A  328  MET  SELENOMETHIONINE                                   
MODRES 3GFP MSE A  401  MET  SELENOMETHIONINE                                   
MODRES 3GFP MSE A  461  MET  SELENOMETHIONINE                                   
HET    MSE  A 309       8                                                       
HET    MSE  A 328       8                                                       
HET    MSE  A 401       8                                                       
HET    MSE  A 461       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    4(C5 H11 N O2 SE)                                            
FORMUL   2  HOH   *153(H2 O)                                                    
HELIX    1   1 ALA A  315  MSE A  328  1                                  14    
HELIX    2   2 THR A  339  GLU A  353  1                                  15    
HELIX    3   3 GLN A  365  GLY A  379  1                                  15    
HELIX    4   4 ASP A  416  GLY A  425  1                                  10    
HELIX    5   5 ASP A  442  PHE A  456  1                                  15    
HELIX    6   6 ASP A  468  VAL A  479  1                                  12    
SHEET    1   A 7 VAL A 357  LEU A 360  0                                        
SHEET    2   A 7 VAL A 383  THR A 387  1  O  ILE A 385   N  LEU A 360           
SHEET    3   A 7 SER A 333  VAL A 337  1  N  ILE A 335   O  LEU A 384           
SHEET    4   A 7 MSE A 401  ASN A 404  1  O  VAL A 403   N  ILE A 334           
SHEET    5   A 7 VAL A 435  VAL A 440  1  O  ILE A 437   N  VAL A 402           
SHEET    6   A 7 LYS A 305  ASP A 310  1  N  MSE A 309   O  SER A 438           
SHEET    7   A 7 THR A 462  PRO A 465  1  O  VAL A 464   N  TYR A 308           
LINK         C   TYR A 308                 N   MSE A 309     1555   1555  1.33  
LINK         C   MSE A 309                 N   ASP A 310     1555   1555  1.33  
LINK         C   LEU A 327                 N   MSE A 328     1555   1555  1.33  
LINK         C   MSE A 328                 N   THR A 329     1555   1555  1.33  
LINK         C   SER A 400                 N   MSE A 401     1555   1555  1.33  
LINK         C   MSE A 401                 N   VAL A 402     1555   1555  1.33  
LINK         C   GLU A 460                 N   MSE A 461     1555   1555  1.33  
LINK         C   MSE A 461                 N   THR A 462     1555   1555  1.33  
CRYST1   82.423   82.423   56.578  90.00  90.00 120.00 P 62          6          
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      0.012133  0.007005  0.000000        0.00000                         
SCALE2      0.000000  0.014009  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017675        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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