GenomeNet

Database: PDB
Entry: 1U6B
LinkDB: 1U6B
Original site: 1U6B 
HEADER    STRUCTURAL PROTEIN/RNA                  29-JUL-04   1U6B              
TITLE     CRYSTAL STRUCTURE OF A SELF-SPLICING GROUP I INTRON WITH BOTH EXONS   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 197-MER;                                                   
COMPND   3 CHAIN: B;                                                            
COMPND   4 FRAGMENT: GROUP I INTRON;                                            
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: 5'-R(*AP*AP*GP*CP*CP*AP*CP*AP*CP*AP*AP*AP*CP*CP*AP*GP*AP*CP
COMPND   8 *GP *GP*CP*C)-3';                                                    
COMPND   9 CHAIN: C;                                                            
COMPND  10 FRAGMENT: GROUP I EXON;                                              
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: 5'-R(*CP*AP*(5MU))-3';                                     
COMPND  14 CHAIN: D;                                                            
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 4;                                                           
COMPND  17 MOLECULE: U1 SMALL NUCLEAR RIBONUCLEOPROTEIN A;                      
COMPND  18 CHAIN: A;                                                            
COMPND  19 SYNONYM: U1 SNRNP PROTEIN A, U1A PROTEIN, U1-A;                      
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 OTHER_DETAILS: RNA WAS IS TRANSCRIBED BY T7 RNA POLYMERASE.;         
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 SYNTHETIC: YES;                                                      
SOURCE   6 MOL_ID: 3;                                                           
SOURCE   7 SYNTHETIC: YES;                                                      
SOURCE   8 MOL_ID: 4;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: SNRPA;                                                         
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PET11                                     
KEYWDS    INTRON, EXON, RIBOZYME, GROUP I, U1A, RNA, STRUCTURAL PROTEIN-RNA     
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.L.ADAMS,M.R.STAHLEY,A.B.KOSEK,J.WANG,S.A.STROBEL                    
REVDAT   4   13-JUL-11 1U6B    1       VERSN                                    
REVDAT   3   07-JUL-09 1U6B    1       REMARK                                   
REVDAT   2   24-FEB-09 1U6B    1       VERSN                                    
REVDAT   1   10-AUG-04 1U6B    0                                                
SPRSDE     10-AUG-04 1U6B      1T42                                             
JRNL        AUTH   P.L.ADAMS,M.R.STAHLEY,A.B.KOSEK,J.WANG,S.A.STROBEL           
JRNL        TITL   CRYSTAL STRUCTURE OF A SELF-SPLICING GROUP I INTRON WITH     
JRNL        TITL 2 BOTH EXONS.                                                  
JRNL        REF    NATURE                        V. 430    45 2004              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   15175762                                                     
JRNL        DOI    10.1038/NATURE02642                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   P.L.ADAMS,M.R.STAHELY,M.L.GILL,C.BERMAN,A.B.KOSEK,J.WANG,    
REMARK   1  AUTH 2 S.A.STROBEL                                                  
REMARK   1  TITL   CRYSTAL STRUCTURE OF A GROUP I INTRON SPLICING INTERMEDIATE  
REMARK   1  REF    TO BE PUBLISHED                                              
REMARK   1  REFN                                                                
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   S.A.STROBEL,P.L.ADAMS,M.R.STAHLEY,J.WANG                     
REMARK   1  TITL   RNA KINK TURNS TO THE LEFT AND TO THE RIGHT                  
REMARK   1  REF    TO BE PUBLISHED                                              
REMARK   1  REFN                                                                
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   T.R.CECH,A.J.ZAUG,P.J.GRABOWASKI                             
REMARK   1  TITL   IN VITRO SPLICING OF THE RIBOSOMAL RNA PRECURSOR OF          
REMARK   1  TITL 2 TETRAHYMENA: INVOLVEMENT OF A GUANOSINE NUCLEOTIDE IN THE    
REMARK   1  TITL 3 EXCISION OF INTERVENING SEQUENCE                             
REMARK   1  REF    CELL(CAMBRIDGE,MASS.)         V.  27   487 1981              
REMARK   1  REFN                   ISSN 0092-8674                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   B.REINHOLD-HUREK,D.A.SHUB                                    
REMARK   1  TITL   SELF-SPLICING INTRON IN TRNA GENES OF WIDELY DIVERGENT       
REMARK   1  TITL 2 BACTERIA                                                     
REMARK   1  REF    NATURE                        V. 357   173 1992              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
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) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.22                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 23553                          
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) : 0.247                           
REMARK   3   R VALUE            (WORKING SET) : 0.246                           
REMARK   3   FREE R VALUE                     : 0.279                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1086                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.27                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2660                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3200                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 131                          
REMARK   3   BIN FREE R VALUE                    : 0.3750                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 775                                     
REMARK   3   NUCLEIC ACID ATOMS       : 4768                                    
REMARK   3   HETEROGEN ATOMS          : 18                                      
REMARK   3   SOLVENT ATOMS            : 54                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 80.42                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.60000                                              
REMARK   3    B22 (A**2) : 0.60000                                              
REMARK   3    B33 (A**2) : -1.19000                                             
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): 1.805         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.444         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.382         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 22.650        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.881                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.872                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6118 ; 0.006 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9357 ; 1.333 ; 2.883       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):    94 ; 3.257 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1000 ; 0.107 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2899 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2607 ; 0.188 ; 0.200       
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):   227 ; 0.176 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):    12 ; 0.139 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    31 ; 0.154 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     4 ; 0.131 ; 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):   476 ; 1.158 ; 3.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   771 ; 2.136 ; 4.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5642 ; 2.425 ; 5.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  8586 ; 4.280 ; 8.000       
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  : 1                                          
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     4        A    98                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.8243  86.5701  61.9647              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3316 T22:   0.1048                                     
REMARK   3      T33:   0.2601 T12:  -0.1263                                     
REMARK   3      T13:   0.2437 T23:  -0.0604                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7126 L22:  -0.0291                                     
REMARK   3      L33:   0.1295 L12:  -0.1026                                     
REMARK   3      L13:   0.1122 L23:  -0.0227                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1133 S12:   0.0084 S13:  -0.3508                       
REMARK   3      S21:  -0.0406 S22:   0.0706 S23:  -0.0343                       
REMARK   3      S31:  -0.0699 S32:   0.0939 S33:   0.0426                       
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: NULL                                      
REMARK   4                                                                      
REMARK   4 1U6B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUL-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB023299.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-JUL-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.80                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X25                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24640                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 72.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.80                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 2                         
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   -Y,X,Z+1/4                                              
REMARK 290       4555   Y,-X,Z+3/4                                              
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z+1/2                                             
REMARK 290       7555   Y,X,-Z+3/4                                              
REMARK 290       8555   -Y,-X,-Z+1/4                                            
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      124.57900            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       62.28950            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      186.86850            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      124.57900            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      186.86850            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       62.28950            
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, D, 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 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     ALA A     2                                                      
REMARK 465     VAL A     3                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480       A C  205   O2'                                                 
REMARK 480       G C  206   O2'                                                 
REMARK 480       A C    1   O2'                                                 
REMARK 480     5MU D    1   O2'                                                 
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O3'    A B    87     O2'  5MU D     1              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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      A C 205   C2'     A C 205   O2'    -0.088                       
REMARK 500      G C 206   C2'     G C 206   O2'     0.468                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
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   ATM2   ATM3                                     
REMARK 500      G B  37   C3' -  O3' -  P   ANGL. DEV. =  11.5 DEGREES          
REMARK 500      A B  81   C1' -  O4' -  C4' ANGL. DEV. =  -5.0 DEGREES          
REMARK 500      G B 107   OP1 -  P   -  OP2 ANGL. DEV. = -10.0 DEGREES          
REMARK 500      A B 106   C3' -  O3' -  P   ANGL. DEV. = -10.2 DEGREES          
REMARK 500      C B1001   OP1 -  P   -  OP2 ANGL. DEV. = -10.4 DEGREES          
REMARK 500      C B1007   C3' -  O3' -  P   ANGL. DEV. =   8.9 DEGREES          
REMARK 500      U B 126   C3' -  O3' -  P   ANGL. DEV. =   8.8 DEGREES          
REMARK 500      G B 135   O4' -  C1' -  N9  ANGL. DEV. =   5.7 DEGREES          
REMARK 500      C B 137   C3' -  O3' -  P   ANGL. DEV. =   8.7 DEGREES          
REMARK 500      C B 171   O4' -  C1' -  N1  ANGL. DEV. =   4.6 DEGREES          
REMARK 500      G B 189   O3' -  P   -  OP2 ANGL. DEV. =   8.2 DEGREES          
REMARK 500      G C 206   C1' -  C2' -  O2' ANGL. DEV. = -25.0 DEGREES          
REMARK 500      G C 206   C3' -  C2' -  O2' ANGL. DEV. = -18.3 DEGREES          
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   6     -135.17   -110.37                                   
REMARK 500    PRO A   8      135.34    -37.22                                   
REMARK 500    ARG A  36       23.67    -71.30                                   
REMARK 500    LEU A  41     -116.63    -87.31                                   
REMARK 500    MET A  82      107.48    -49.61                                   
REMARK 500    MET A  97      -31.44   -136.96                                   
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 B1041        DISTANCE =  5.04 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B   2   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A B  87   OP1                                                    
REMARK 620 2   A B 127   O3' 108.4                                              
REMARK 620 3   G B 128   OP1  63.9  55.7                                        
REMARK 620 4   G B 128   O5' 108.1  46.1  46.2                                  
REMARK 620 5   G C 206   O2' 134.5 117.0 144.0 101.2                            
REMARK 620 6 HOH B1030   O    52.5  61.0  52.0  89.5 161.9                      
REMARK 620 7   A B 172   OP2 122.5 100.1 153.2 127.2  53.4 108.6                
REMARK 620 8 HOH C 101   O    80.2 168.4 135.8 139.9  55.4 122.9  68.4          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B   3  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A B 174   OP2                                                    
REMARK 620 2   U B 173   OP2  75.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B   4   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G B 152   O6                                                     
REMARK 620 2   G B 151   N7   81.4                                              
REMARK 620 3   G B 151   O6   58.7  56.3                                        
REMARK 620 4   A B 149   O3' 159.1  92.4 101.3                                  
REMARK 620 5   A B 149   O2' 112.9 100.2  67.4  48.3                            
REMARK 620 6   A B 150   OP2 154.7 119.1 144.0  43.3  79.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B1015   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B1035   O                                                      
REMARK 620 2   C B 171   OP2 107.5                                              
REMARK 620 3   U B 126   O2' 119.5 130.0                                        
REMARK 620 4   U B 126   O2   67.6 156.6  52.4                                  
REMARK 620 5   A B 127   OP2 162.8  89.7  44.0  96.4                            
REMARK 620 6   C B 171   O5' 107.1  51.5  96.7 106.7  82.7                      
REMARK 620 7   U B 124   OP1  82.9  57.5 140.1 139.5 107.9 108.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B1016   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A D   2   N6                                                     
REMARK 620 2   U B   9   O4  146.5                                              
REMARK 620 3   A C   1   N6  110.5  45.0                                        
REMARK 620 4 5MU D   1   O4   66.5 103.2  59.8                                  
REMARK 620 5 HOH B1032   O   130.9  69.4  70.2  74.1                            
REMARK 620 6   G B  10   O6   59.1  87.5  60.3  65.4 126.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B1017   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G B  24   O6                                                     
REMARK 620 2   G B  23   O6   73.4                                              
REMARK 620 3   G B  23   N7   94.4  51.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1018  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A B 172   OP2                                                    
REMARK 620 2   A C   1   OP2  87.7                                              
REMARK 620 3 5MU D   1   O3' 151.6  64.4                                        
REMARK 620 4   G B 170   OP1 134.4 123.0  65.6                                  
REMARK 620 5   A B 172   OP1  60.6 130.9 134.7  73.9                            
REMARK 620 6   C B  88   OP1 137.1 112.9  64.6  65.6 115.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1023  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U B 124   OP1                                                    
REMARK 620 2   C B 171   OP2  85.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1024  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G B  37   O2'                                                    
REMARK 620 2   G B  38   OP2  49.5                                              
REMARK 620 3   A B  39   OP2 127.8 104.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1025  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B1054   O                                                      
REMARK 620 2   A B  48   OP2  77.3                                              
REMARK 620 3   U B 133   OP2 136.4 144.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1027  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B1073   O                                                      
REMARK 620 2   G B 125   OP1  89.6                                              
REMARK 620 3 HOH B1061   O    79.1 103.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1029  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B1074   O                                                      
REMARK 620 2   U B  15   OP1  68.0                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 2                     
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 4                     
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 1015                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 1016                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 1017                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1018                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 3                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1019                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1020                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1023                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1024                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1025                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1026                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1027                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1028                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1029                 
REMARK 999                                                                      
REMARK 999 SEQUENCE NUCLEOTIDES 1001B TO 1014B BELONG TO AN ENGINEERED U1A      
REMARK 999 LOOP AND ARE INSERTED BETWEEN GUA-107B AND CYT-112B. THERE ARE NO    
REMARK 999 NUCLEOTIDES BETWEEN GUA-1B AND GUA-5B DUE TO A CLONING DESIGN. O2'   
REMARK 999 OF DEOXY MODIFICATION OF RNA NUCLEOTIDES ARE INCLUDED WITH Q=0.00    
REMARK 999 AND B=0.00. THEY ARE AT GUA-206C, CYT-1C, CYT-205C, AND THY-1D.      
REMARK 999 CHAINS B AND C ARE TWO PARTS OF THE ORIGINAL ONE INTRON SEQUENCE     
REMARK 999 BECAUSE OF AN EXPERIMENTAL DESIGN. THE U1A PROTEIN USED IN THIS      
REMARK 999 STUDY WAS A DOUBLE MUTANT IN WHICH TYR-31/GLN-36 WAS REPLACED WITH   
REMARK 999 HIS-31/ARG-36. THE FIRST THREE RESIDUES IN U1A PROTEIN WERE MISSING  
REMARK 999 IN THE STRUCTURE.                                                    
DBREF  1U6B A    1    98  UNP    P09012   RU1A_HUMAN       1     98             
DBREF  1U6B B    1   190  PDB    1U6B     1U6B             1    190             
DBREF  1U6B C  191     6  PDB    1U6B     1U6B           191      6             
DBREF  1U6B D    3     1  PDB    1U6B     1U6B             3      1             
SEQADV 1U6B HIS A   31  UNP  P09012    TYR    31 ENGINEERED                     
SEQADV 1U6B ARG A   36  UNP  P09012    GLN    36 ENGINEERED                     
SEQRES   1 B  197  GTP   G   C   C   G   U   G   U   G   C   C   U   U          
SEQRES   2 B  197    G   C   G   C   C   G   G   G   A   A   A   C   C          
SEQRES   3 B  197    A   C   G   C   A   A   G   G   G   A   U   G   G          
SEQRES   4 B  197    U   G   U   C   A   A   A   U   U   C   G   G   C          
SEQRES   5 B  197    G   A   A   A   C   C   U   A   A   G   C   G   C          
SEQRES   6 B  197    C   C   G   C   C   C   G   G   G   C   G   U   A          
SEQRES   7 B  197    U   G   G   C   A   A   C   G   C   C   G   A   G          
SEQRES   8 B  197    C   C   A   A   G   C   U   U   C   G   C   A   G          
SEQRES   9 B  197    C   C   A   U   U   G   C   A   C   U   C   C   G          
SEQRES  10 B  197    G   C   U   G   C   G   A   U   G   A   A   G   G          
SEQRES  11 B  197    U   G   U   A   G   A   G   A   C   U   A   G   A          
SEQRES  12 B  197    C   G   G   C   A   C   C   C   A   C   C   U   A          
SEQRES  13 B  197    A   G   G   C   A   A   A   C   G   C   U   A   U          
SEQRES  14 B  197    G   G   U   G   A   A   G   G   C   A   U   A   G          
SEQRES  15 B  197    U   C   C   A   G   G   G   A   G   U   G   G   C          
SEQRES  16 B  197    G A23                                                      
SEQRES   1 C   22    A   A   G   C   C   A   C   A   C   A   A   A   C          
SEQRES   2 C   22    C   A   G   A   C   G   G   C   C                          
SEQRES   1 D    3    C   A 5MU                                                  
SEQRES   1 A   98  MET ALA VAL PRO GLU THR ARG PRO ASN HIS THR ILE TYR          
SEQRES   2 A   98  ILE ASN ASN LEU ASN GLU LYS ILE LYS LYS ASP GLU LEU          
SEQRES   3 A   98  LYS LYS SER LEU HIS ALA ILE PHE SER ARG PHE GLY GLN          
SEQRES   4 A   98  ILE LEU ASP ILE LEU VAL SER ARG SER LEU LYS MET ARG          
SEQRES   5 A   98  GLY GLN ALA PHE VAL ILE PHE LYS GLU VAL SER SER ALA          
SEQRES   6 A   98  THR ASN ALA LEU ARG SER MET GLN GLY PHE PRO PHE TYR          
SEQRES   7 A   98  ASP LYS PRO MET ARG ILE GLN TYR ALA LYS THR ASP SER          
SEQRES   8 A   98  ASP ILE ILE ALA LYS MET LYS                                  
MODRES 1U6B GTP B    1    G  GUANOSINE-5'-TRIPHOSPHATE                          
MODRES 1U6B A23 B  190    A                                                     
MODRES 1U6B 5MU D    1    U  5-METHYLURIDINE 5'-MONOPHOSPHATE                   
HET    GTP  B   1      32                                                       
HET    A23  B 190      25                                                       
HET    5MU  D   1      21                                                       
HET      K  B   2       1                                                       
HET      K  B   4       1                                                       
HET      K  B1015       1                                                       
HET      K  B1016       1                                                       
HET      K  B1017       1                                                       
HET     MG  B1018       1                                                       
HET     MG  B   3       1                                                       
HET     MG  B1019       1                                                       
HET     MG  B1020       1                                                       
HET     MG  B1021       1                                                       
HET     MG  B1022       1                                                       
HET     MG  B1023       1                                                       
HET     MG  B1024       1                                                       
HET     MG  B1025       1                                                       
HET     MG  B1026       1                                                       
HET     MG  B1027       1                                                       
HET     MG  B1028       1                                                       
HET     MG  B1029       1                                                       
HETNAM     GTP GUANOSINE-5'-TRIPHOSPHATE                                        
HETNAM     A23 ADENOSINE-5'-PHOSPHATE-2',3'-CYCLIC PHOSPHATE                    
HETNAM     5MU 5-METHYLURIDINE 5'-MONOPHOSPHATE                                 
HETNAM       K POTASSIUM ION                                                    
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   1  GTP    C10 H16 N5 O14 P3                                            
FORMUL   1  A23    C10 H13 N5 O9 P2                                             
FORMUL   3  5MU    C10 H15 N2 O9 P                                              
FORMUL   5    K    5(K 1+)                                                      
FORMUL  10   MG    13(MG 2+)                                                    
FORMUL  23  HOH   *54(H2 O)                                                     
HELIX    1   1 LYS A   22  ALA A   32  1                                  11    
HELIX    2   2 GLU A   61  MET A   72  1                                  12    
HELIX    3   3 SER A   91  LYS A   96  1                                   6    
SHEET    1   A 4 ILE A  40  VAL A  45  0                                        
SHEET    2   A 4 ALA A  55  PHE A  59 -1  O  ILE A  58   N  LEU A  41           
SHEET    3   A 4 THR A  11  ASN A  15 -1  N  ILE A  14   O  ALA A  55           
SHEET    4   A 4 ARG A  83  TYR A  86 -1  O  ARG A  83   N  ASN A  15           
SHEET    1   B 2 PRO A  76  PHE A  77  0                                        
SHEET    2   B 2 LYS A  80  PRO A  81 -1  O  LYS A  80   N  PHE A  77           
LINK         O3'   A D   2                 P   5MU D   1     1555   1555  1.59  
LINK         O3'   C D   3                 P     A D   2     1555   1555  1.61  
LINK         O3' GTP B   1                 P     G B   5     1555   1555  1.59  
LINK         K     K B   2                 OP1   A B  87     1555   1555  2.72  
LINK         K     K B   2                 O3'   A B 127     1555   1555  2.73  
LINK         K     K B   2                 OP1   G B 128     1555   1555  2.61  
LINK         K     K B   2                 O5'   G B 128     1555   1555  3.48  
LINK         K     K B   2                 O2'   G C 206     1555   1555  2.72  
LINK         K     K B   2                 O   HOH B1030     1555   1555  2.96  
LINK         K     K B   2                 OP2   A B 172     1555   1555  3.12  
LINK         K     K B   2                 O   HOH C 101     1555   1555  2.68  
LINK        MG    MG B   3                 OP2   A B 174     1555   1555  2.11  
LINK        MG    MG B   3                 OP2   U B 173     1555   1555  2.30  
LINK         K     K B   4                 O6    G B 152     1555   1555  3.01  
LINK         K     K B   4                 N7    G B 151     1555   1555  2.93  
LINK         K     K B   4                 O6    G B 151     1555   1555  3.40  
LINK         K     K B   4                 O3'   A B 149     1555   1555  3.61  
LINK         K     K B   4                 O2'   A B 149     1555   1555  2.68  
LINK         K     K B   4                 OP2   A B 150     1555   1555  2.54  
LINK         O3'   G B 189                 P   A23 B 190     1555   1555  1.61  
LINK         K     K B1015                 O   HOH B1035     1555   1555  3.61  
LINK         K     K B1015                 OP2   C B 171     1555   1555  2.77  
LINK         K     K B1015                 O2'   U B 126     1555   1555  3.01  
LINK         K     K B1015                 O2    U B 126     1555   1555  3.66  
LINK         K     K B1015                 OP2   A B 127     1555   1555  3.39  
LINK         K     K B1015                 O5'   C B 171     1555   1555  2.89  
LINK         K     K B1015                 OP1   U B 124     1555   1555  3.32  
LINK         K     K B1016                 N6    A D   2     1555   1555  2.98  
LINK         K     K B1016                 O4    U B   9     1555   1555  2.78  
LINK         K     K B1016                 N6    A C   1     1555   1555  3.65  
LINK         K     K B1016                 O4  5MU D   1     1555   1555  3.03  
LINK         K     K B1016                 O   HOH B1032     1555   1555  3.13  
LINK         K     K B1016                 O6    G B  10     1555   1555  3.16  
LINK         K     K B1017                 O6    G B  24     1555   1555  3.01  
LINK         K     K B1017                 O6    G B  23     1555   1555  3.42  
LINK         K     K B1017                 N7    G B  23     1555   1555  3.63  
LINK        MG    MG B1018                 OP2   A B 172     1555   1555  2.82  
LINK        MG    MG B1018                 OP2   A C   1     1555   1555  2.30  
LINK        MG    MG B1018                 O3' 5MU D   1     1555   1555  2.44  
LINK        MG    MG B1018                 OP1   G B 170     1555   1555  2.51  
LINK        MG    MG B1018                 OP1   A B 172     1555   1555  2.13  
LINK        MG    MG B1018                 OP1   C B  88     1555   1555  2.26  
LINK        MG    MG B1019                 OP1   U B 126     1555   1555  1.82  
LINK        MG    MG B1020                 O   HOH B1071     1555   1555  1.98  
LINK        MG    MG B1023                 OP1   U B 124     1555   1555  2.09  
LINK        MG    MG B1023                 OP2   C B 171     1555   1555  2.28  
LINK        MG    MG B1024                 O2'   G B  37     1555   1555  2.93  
LINK        MG    MG B1024                 OP2   G B  38     1555   1555  1.84  
LINK        MG    MG B1024                 OP2   A B  39     1555   1555  2.38  
LINK        MG    MG B1025                 O   HOH B1054     1555   1555  2.97  
LINK        MG    MG B1025                 OP2   A B  48     1555   1555  2.59  
LINK        MG    MG B1025                 OP2   U B 133     1555   1555  2.75  
LINK        MG    MG B1026                 OP2   C B  74     1555   1555  2.34  
LINK        MG    MG B1027                 O   HOH B1073     1555   1555  1.76  
LINK        MG    MG B1027                 OP1   G B 125     1555   1555  2.73  
LINK        MG    MG B1027                 O   HOH B1061     1555   1555  2.59  
LINK        MG    MG B1028                 OP1   G B 181     1555   1555  2.57  
LINK        MG    MG B1029                 O   HOH B1074     1555   1555  2.69  
LINK        MG    MG B1029                 OP1   U B  15     1555   1555  2.24  
SITE     1 AC1  6   A B  87    A B 127    G B 128    A B 172                    
SITE     2 AC1  6 HOH B1030  HOH C 101                                          
SITE     1 AC2  4   A B 149    A B 150    G B 151    G B 152                    
SITE     1 AC3  4   U B 124    U B 126    A B 127    C B 171                    
SITE     1 AC4  5   U B   9    G B  10    A C   1  5MU D   1                    
SITE     2 AC4  5   A D   2                                                     
SITE     1 AC5  2   G B  23    G B  24                                          
SITE     1 AC6  5   C B  88    G B 170    A B 172    A C   1                    
SITE     2 AC6  5 5MU D   1                                                     
SITE     1 AC7  3   A B 172    U B 173    A B 174                               
SITE     1 AC8  2   G B 125    U B 126                                          
SITE     1 AC9  1 HOH B1071                                                     
SITE     1 BC1  2   U B 124    C B 171                                          
SITE     1 BC2  3   G B  37    G B  38    A B  39                               
SITE     1 BC3  3   A B  48    U B 133  HOH B1054                               
SITE     1 BC4  2   C B  73    C B  74                                          
SITE     1 BC5  4   U B  51    G B 125  HOH B1061  HOH B1073                    
SITE     1 BC6  2   G B 181    G B 182                                          
SITE     1 BC7  3   U B  15    C B  29  HOH B1074                               
CRYST1  108.541  108.541  249.158  90.00  90.00  90.00 P 41 2 2      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009213  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009213  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004014        0.00000                         
HETATM    1  PG  GTP B   1      67.536  74.584  50.449  1.00144.97           P  
HETATM    2  O1G GTP B   1      67.219  73.111  50.385  1.00142.79           O  
HETATM    3  O2G GTP B   1      66.648  75.502  49.666  1.00143.28           O  
HETATM    4  O3G GTP B   1      68.985  74.856  50.255  1.00142.20           O  
HETATM    5  O3B GTP B   1      67.204  75.078  51.983  1.00140.60           O  
HETATM    6  PB  GTP B   1      67.956  74.679  53.391  1.00137.13           P  
HETATM    7  O1B GTP B   1      69.391  75.079  53.342  1.00132.50           O  
HETATM    8  O2B GTP B   1      67.140  75.232  54.528  1.00135.77           O  
HETATM    9  O3A GTP B   1      67.774  73.047  53.579  1.00129.55           O  
HETATM   10  PA  GTP B   1      68.782  72.131  52.927  1.00125.34           P  
HETATM   11  O1A GTP B   1      68.060  71.123  52.108  1.00125.01           O  
HETATM   12  O2A GTP B   1      69.705  72.887  52.044  1.00125.40           O  
HETATM   13  O5' GTP B   1      69.573  71.427  53.963  1.00114.36           O  
HETATM   14  C5' GTP B   1      70.371  72.348  54.688  1.00 95.81           C  
HETATM   15  C4' GTP B   1      71.814  71.951  54.841  1.00 91.57           C  
HETATM   16  O4' GTP B   1      72.491  71.998  53.560  1.00 86.92           O  
HETATM   17  C3' GTP B   1      72.604  72.919  55.683  1.00 89.43           C  
HETATM   18  O3' GTP B   1      72.369  72.673  57.043  1.00 94.59           O  
HETATM   19  C2' GTP B   1      74.037  72.682  55.231  1.00 83.50           C  
HETATM   20  O2' GTP B   1      74.626  71.526  55.795  1.00 76.18           O  
HETATM   21  C1' GTP B   1      73.824  72.469  53.735  1.00 79.48           C  
HETATM   22  N9  GTP B   1      73.964  73.707  52.975  1.00 69.48           N  
HETATM   23  C8  GTP B   1      72.969  74.374  52.303  1.00 66.30           C  
HETATM   24  N7  GTP B   1      73.396  75.432  51.675  1.00 59.63           N  
HETATM   25  C5  GTP B   1      74.749  75.474  51.957  1.00 55.20           C  
HETATM   26  C6  GTP B   1      75.715  76.387  51.541  1.00 52.37           C  
HETATM   27  O6  GTP B   1      75.559  77.360  50.818  1.00 57.34           O  
HETATM   28  N1  GTP B   1      76.971  76.081  52.044  1.00 46.19           N  
HETATM   29  C2  GTP B   1      77.252  75.006  52.858  1.00 53.14           C  
HETATM   30  N2  GTP B   1      78.539  74.866  53.245  1.00 50.26           N  
HETATM   31  N3  GTP B   1      76.339  74.129  53.263  1.00 53.78           N  
HETATM   32  C4  GTP B   1      75.116  74.425  52.769  1.00 60.83           C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system