GenomeNet

Database: PDB
Entry: 3G8S
LinkDB: 3G8S
Original site: 3G8S 
HEADER    RNA BINDING PROTEIN/RNA                 12-FEB-09   3G8S              
TITLE     CRYSTAL STRUCTURE OF THE PRE-CLEAVED BACILLUS ANTHRACIS GLMS RIBOZYME 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: U1 SMALL NUCLEAR RIBONUCLEOPROTEIN A;                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: RNA BINDING DOMAIN;                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: RNA (5'-R(*AP*(A2M)P*GP*CP*GP*CP*CP*AP*GP*AP*AP*CP*U)-3'); 
COMPND   9 CHAIN: E, F, G, H;                                                   
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MUTATION: YES;                                                       
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: GLMS RIBOZYME;                                             
COMPND  14 CHAIN: P, Q, R, S;                                                   
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SNRPA;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET11;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: CHEMICALLY SYNTHESIZED;                               
SOURCE  14 MOL_ID: 3;                                                           
SOURCE  15 SYNTHETIC: YES;                                                      
SOURCE  16 OTHER_DETAILS: IN VITRO TRANSCRIBED FROM A DNA TEMPLATE              
KEYWDS    CATALYTIC RNA, RNA BINDING PROTEIN-RNA COMPLEX                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.A.STROBEL,J.C.COCHRANE,S.V.LIPCHOCK,K.D.SMITH                       
REVDAT   3   01-NOV-17 3G8S    1       REMARK                                   
REVDAT   2   13-JUL-11 3G8S    1       VERSN                                    
REVDAT   1   03-NOV-09 3G8S    0                                                
JRNL        AUTH   J.C.COCHRANE,S.V.LIPCHOCK,K.D.SMITH,S.A.STROBEL              
JRNL        TITL   STRUCTURAL AND CHEMICAL BASIS FOR GLUCOSAMINE 6-PHOSPHATE    
JRNL        TITL 2 BINDING AND ACTIVATION OF THE GLMS RIBOZYME                  
JRNL        REF    BIOCHEMISTRY                  V.  48  3239 2009              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   19228039                                                     
JRNL        DOI    10.1021/BI802069P                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0044                                      
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) : 43.77                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 37270                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.249                           
REMARK   3   R VALUE            (WORKING SET) : 0.246                           
REMARK   3   FREE R VALUE                     : 0.306                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1964                            
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) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.18                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2575                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 91.81                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3090                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 139                          
REMARK   3   BIN FREE R VALUE                    : 0.3620                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2897                                    
REMARK   3   NUCLEIC ACID ATOMS       : 13066                                   
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 79                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 62.37                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.41000                                              
REMARK   3    B22 (A**2) : 2.98000                                              
REMARK   3    B33 (A**2) : -4.41000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.74000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.638         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.490         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 27.660        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.876                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.831                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 17577 ; 0.007 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  7170 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 26700 ; 1.486 ; 2.844       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 18298 ; 0.895 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   361 ; 6.742 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   133 ;35.542 ;23.534       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   567 ;18.710 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;15.032 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  3498 ; 0.060 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9477 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1975 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1824 ; 0.266 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   729 ; 0.034 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2938 ; 0.495 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 15753 ; 0.823 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 23762 ; 1.415 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 6                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      7       A      96      4                      
REMARK   3           1     D      7       D      96      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1227 ;  0.45 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1227 ;  0.17 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : B C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B      8       B      97      4                      
REMARK   3           1     C      8       C      97      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    B    (A):   1245 ;  0.41 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    B (A**2):   1245 ;  0.19 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : E H                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     E      1       E      13      4                      
REMARK   3           1     H      1       H      13      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  3    E    (A):    370 ;  0.46 ;  0.50           
REMARK   3   MEDIUM THERMAL     3    E (A**2):    370 ;  0.29 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : F G                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     F      1       F      13      4                      
REMARK   3           1     G      1       G      13      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  4    F    (A):    386 ;  0.65 ;  0.50           
REMARK   3   MEDIUM THERMAL     4    F (A**2):    386 ;  0.35 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 5                                  
REMARK   3     CHAIN NAMES                    : P S                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     P      1       P     141      4                      
REMARK   3           1     S      1       S     141      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  5    P    (A):   4122 ;  0.37 ;  0.50           
REMARK   3   MEDIUM THERMAL     5    P (A**2):   4122 ;  0.23 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 6                                  
REMARK   3     CHAIN NAMES                    : Q R                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     Q      1       Q     141      4                      
REMARK   3           1     R      1       R     141      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  6    Q    (A):   4165 ;  0.33 ;  0.50           
REMARK   3   MEDIUM THERMAL     6    Q (A**2):   4165 ;  0.38 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3G8S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-APR-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000051566.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-OCT-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
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                  : SI(111) CRYSTAL                    
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39374                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.21900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.8440                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.69300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 11% PEG 8000, 9% DMSO, 0.02M SODIUM      
REMARK 280  CACODYLATE, 0.02M MAGNESIUM CHLORIDE, 0.15M POTASSIUM CHLORIDE,     
REMARK 280  PH 6.8, VAPOR DIFFUSION, SITTING DROPS, TEMPERATURE 298K, VAPOR     
REMARK 280  DIFFUSION, SITTING DROP                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000      114.24000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E, P                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F, Q                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G, R                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, H, S                               
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 465     PRO A     4                                                      
REMARK 465     GLU A     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     MET A    97                                                      
REMARK 465     LYS A    98                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     VAL B     3                                                      
REMARK 465     PRO B     4                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C     2                                                      
REMARK 465     VAL C     3                                                      
REMARK 465     PRO C     4                                                      
REMARK 465     GLU C     5                                                      
REMARK 465     THR C     6                                                      
REMARK 465     MET C    97                                                      
REMARK 465     LYS C    98                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D     2                                                      
REMARK 465     VAL D     3                                                      
REMARK 465     PRO D     4                                                      
REMARK 465     GLU D     5                                                      
REMARK 465     THR D     6                                                      
REMARK 465     MET D    97                                                      
REMARK 465     LYS D    98                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A   7    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     LYS A  20    CD   CE   NZ                                        
REMARK 470     LYS A  88    CG   CD   CE   NZ                                   
REMARK 470     LYS A  96    CG   CD   CE   NZ                                   
REMARK 470       A E  -1    O5'  C5'                                            
REMARK 470       A E   6    N9   C8   N7   C5   C6   N6   N1                    
REMARK 470       A E   6    C2   N3   C4                                        
REMARK 470       U P  17I   N1   C2   O2   N3   C4   O4   C5                    
REMARK 470       U P  17I   C6                                                  
REMARK 470       C P  17J   N1   C2   O2   N3   C4   N4   C5                    
REMARK 470       C P  17J   C6                                                  
REMARK 470       C P  85    N1   C2   O2   N3   C4   N4   C5                    
REMARK 470       C P  85    C6                                                  
REMARK 470       U P  91    N1   C2   O2   N3   C4   O4   C5                    
REMARK 470       U P  91    C6                                                  
REMARK 470       U P 134    N1   C2   O2   N3   C4   O4   C5                    
REMARK 470       U P 134    C6                                                  
REMARK 470     GLU B   5    CG   CD   OE1  OE2                                  
REMARK 470     ARG B   7    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  96    CG   CD   CE   NZ                                   
REMARK 470     LYS B  98    CG   CD   CE   NZ                                   
REMARK 470       U Q  49    N1   C2   O2   N3   C4   O4   C5                    
REMARK 470       U Q  49    C6                                                  
REMARK 470       C Q  85    N1   C2   O2   N3   C4   N4   C5                    
REMARK 470       C Q  85    C6                                                  
REMARK 470     ARG C   7    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     LYS C  20    CD   CE   NZ                                        
REMARK 470     LYS C  88    CG   CD   CE   NZ                                   
REMARK 470     LYS C  96    CG   CD   CE   NZ                                   
REMARK 470       U R  49    N1   C2   O2   N3   C4   O4   C5                    
REMARK 470       U R  49    C6                                                  
REMARK 470       C R  85    N1   C2   O2   N3   C4   N4   C5                    
REMARK 470       C R  85    C6                                                  
REMARK 470     ARG D   7    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     LYS D  20    CD   CE   NZ                                        
REMARK 470     LYS D  88    CG   CD   CE   NZ                                   
REMARK 470     LYS D  96    CG   CD   CE   NZ                                   
REMARK 470       A H   6    N9   C8   N7   C5   C6   N6   N1                    
REMARK 470       A H   6    C2   N3   C4                                        
REMARK 470       U S  17I   N1   C2   O2   N3   C4   O4   C5                    
REMARK 470       U S  17I   C6                                                  
REMARK 470       U S  49    N1   C2   O2   N3   C4   O4   C5                    
REMARK 470       U S  49    C6                                                  
REMARK 470       C S  85    N1   C2   O2   N3   C4   N4   C5                    
REMARK 470       C S  85    C6                                                  
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    ASN B  18       95.35    -65.21                                   
REMARK 500    ASP B  42      150.84    179.46                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG P   2  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C E   2   OP2                                                    
REMARK 620 2   C P  29   OP2 138.8                                              
REMARK 620 3   G P  30   OP2 110.4  94.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG Q   3  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C F   2   OP2                                                    
REMARK 620 2   C Q  29   OP2 153.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG R   7  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C G   2   OP2                                                    
REMARK 620 2   C R  29   OP2 104.9                                              
REMARK 620 3   G R  30   OP2  74.4  67.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG S   9  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C H   2   OP2                                                    
REMARK 620 2   C S  29   OP2 143.2                                              
REMARK 620 3   G S  30   OP2  79.2  69.7                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 12                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG P 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Q 3                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Q 4                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Q 5                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG R 6                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG R 7                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 12                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG S 9                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG P 10                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3G8T   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3G95   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3G96   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3G9C   RELATED DB: PDB                                   
DBREF  3G8S A    1    98  UNP    P09012   SNRPA_HUMAN      1     98             
DBREF  3G8S B    1    98  UNP    P09012   SNRPA_HUMAN      1     98             
DBREF  3G8S C    1    98  UNP    P09012   SNRPA_HUMAN      1     98             
DBREF  3G8S D    1    98  UNP    P09012   SNRPA_HUMAN      1     98             
DBREF  3G8S E   -1    11  PDB    3G8S     3G8S            -1     11             
DBREF  3G8S F   -1    11  PDB    3G8S     3G8S            -1     11             
DBREF  3G8S G   -1    11  PDB    3G8S     3G8S            -1     11             
DBREF  3G8S H   -1    11  PDB    3G8S     3G8S            -1     11             
DBREF  3G8S P   12   141  PDB    3G8S     3G8S            12    141             
DBREF  3G8S Q   12   141  PDB    3G8S     3G8S            12    141             
DBREF  3G8S R   12   141  PDB    3G8S     3G8S            12    141             
DBREF  3G8S S   12   141  PDB    3G8S     3G8S            12    141             
SEQADV 3G8S HIS A   31  UNP  P09012    TYR    31 ENGINEERED                     
SEQADV 3G8S ARG A   36  UNP  P09012    GLN    36 ENGINEERED                     
SEQADV 3G8S HIS B   31  UNP  P09012    TYR    31 ENGINEERED                     
SEQADV 3G8S ARG B   36  UNP  P09012    GLN    36 ENGINEERED                     
SEQADV 3G8S HIS C   31  UNP  P09012    TYR    31 ENGINEERED                     
SEQADV 3G8S ARG C   36  UNP  P09012    GLN    36 ENGINEERED                     
SEQADV 3G8S HIS D   31  UNP  P09012    TYR    31 ENGINEERED                     
SEQADV 3G8S ARG D   36  UNP  P09012    GLN    36 ENGINEERED                     
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                                  
SEQRES   1 E   13    A A2M   G   C   G   C   C   A   G   A   A   C   U          
SEQRES   1 P  141  GTP   G   C   A   C   C   A   U   U   G   C   A   C          
SEQRES   2 P  141    U   C   C   G   G   U   G   C   C   A   G   U   U          
SEQRES   3 P  141    G   A   C   G   A   G   G   U   G   G   G   G   U          
SEQRES   4 P  141    U   U   A   U   C   G   A   G   A   U   U   U   C          
SEQRES   5 P  141    G   G   C   G   G   A   U   G   A   C   U   C   C          
SEQRES   6 P  141    C   G   G   U   U   G   U   U   C   A   U   C   A          
SEQRES   7 P  141    C   A   A   C   C   G   C   A   A   G   C   U   U          
SEQRES   8 P  141    U   U   A   C   U   U   A   A   A   U   C   A   U          
SEQRES   9 P  141    U   A   A   G   G   U   G   A   C   U   U   A   G          
SEQRES  10 P  141    U   G   G   A   C   A   A   A   G   G   U   G   A          
SEQRES  11 P  141    A   A   G   U   G   U   G   A   U   G   A                  
SEQRES   1 B   98  MET ALA VAL PRO GLU THR ARG PRO ASN HIS THR ILE TYR          
SEQRES   2 B   98  ILE ASN ASN LEU ASN GLU LYS ILE LYS LYS ASP GLU LEU          
SEQRES   3 B   98  LYS LYS SER LEU HIS ALA ILE PHE SER ARG PHE GLY GLN          
SEQRES   4 B   98  ILE LEU ASP ILE LEU VAL SER ARG SER LEU LYS MET ARG          
SEQRES   5 B   98  GLY GLN ALA PHE VAL ILE PHE LYS GLU VAL SER SER ALA          
SEQRES   6 B   98  THR ASN ALA LEU ARG SER MET GLN GLY PHE PRO PHE TYR          
SEQRES   7 B   98  ASP LYS PRO MET ARG ILE GLN TYR ALA LYS THR ASP SER          
SEQRES   8 B   98  ASP ILE ILE ALA LYS MET LYS                                  
SEQRES   1 F   13    A A2M   G   C   G   C   C   A   G   A   A   C   U          
SEQRES   1 Q  141  GTP   G   C   A   C   C   A   U   U   G   C   A   C          
SEQRES   2 Q  141    U   C   C   G   G   U   G   C   C   A   G   U   U          
SEQRES   3 Q  141    G   A   C   G   A   G   G   U   G   G   G   G   U          
SEQRES   4 Q  141    U   U   A   U   C   G   A   G   A   U   U   U   C          
SEQRES   5 Q  141    G   G   C   G   G   A   U   G   A   C   U   C   C          
SEQRES   6 Q  141    C   G   G   U   U   G   U   U   C   A   U   C   A          
SEQRES   7 Q  141    C   A   A   C   C   G   C   A   A   G   C   U   U          
SEQRES   8 Q  141    U   U   A   C   U   U   A   A   A   U   C   A   U          
SEQRES   9 Q  141    U   A   A   G   G   U   G   A   C   U   U   A   G          
SEQRES  10 Q  141    U   G   G   A   C   A   A   A   G   G   U   G   A          
SEQRES  11 Q  141    A   A   G   U   G   U   G   A   U   G   A                  
SEQRES   1 C   98  MET ALA VAL PRO GLU THR ARG PRO ASN HIS THR ILE TYR          
SEQRES   2 C   98  ILE ASN ASN LEU ASN GLU LYS ILE LYS LYS ASP GLU LEU          
SEQRES   3 C   98  LYS LYS SER LEU HIS ALA ILE PHE SER ARG PHE GLY GLN          
SEQRES   4 C   98  ILE LEU ASP ILE LEU VAL SER ARG SER LEU LYS MET ARG          
SEQRES   5 C   98  GLY GLN ALA PHE VAL ILE PHE LYS GLU VAL SER SER ALA          
SEQRES   6 C   98  THR ASN ALA LEU ARG SER MET GLN GLY PHE PRO PHE TYR          
SEQRES   7 C   98  ASP LYS PRO MET ARG ILE GLN TYR ALA LYS THR ASP SER          
SEQRES   8 C   98  ASP ILE ILE ALA LYS MET LYS                                  
SEQRES   1 G   13    A A2M   G   C   G   C   C   A   G   A   A   C   U          
SEQRES   1 R  141  GTP   G   C   A   C   C   A   U   U   G   C   A   C          
SEQRES   2 R  141    U   C   C   G   G   U   G   C   C   A   G   U   U          
SEQRES   3 R  141    G   A   C   G   A   G   G   U   G   G   G   G   U          
SEQRES   4 R  141    U   U   A   U   C   G   A   G   A   U   U   U   C          
SEQRES   5 R  141    G   G   C   G   G   A   U   G   A   C   U   C   C          
SEQRES   6 R  141    C   G   G   U   U   G   U   U   C   A   U   C   A          
SEQRES   7 R  141    C   A   A   C   C   G   C   A   A   G   C   U   U          
SEQRES   8 R  141    U   U   A   C   U   U   A   A   A   U   C   A   U          
SEQRES   9 R  141    U   A   A   G   G   U   G   A   C   U   U   A   G          
SEQRES  10 R  141    U   G   G   A   C   A   A   A   G   G   U   G   A          
SEQRES  11 R  141    A   A   G   U   G   U   G   A   U   G   A                  
SEQRES   1 D   98  MET ALA VAL PRO GLU THR ARG PRO ASN HIS THR ILE TYR          
SEQRES   2 D   98  ILE ASN ASN LEU ASN GLU LYS ILE LYS LYS ASP GLU LEU          
SEQRES   3 D   98  LYS LYS SER LEU HIS ALA ILE PHE SER ARG PHE GLY GLN          
SEQRES   4 D   98  ILE LEU ASP ILE LEU VAL SER ARG SER LEU LYS MET ARG          
SEQRES   5 D   98  GLY GLN ALA PHE VAL ILE PHE LYS GLU VAL SER SER ALA          
SEQRES   6 D   98  THR ASN ALA LEU ARG SER MET GLN GLY PHE PRO PHE TYR          
SEQRES   7 D   98  ASP LYS PRO MET ARG ILE GLN TYR ALA LYS THR ASP SER          
SEQRES   8 D   98  ASP ILE ILE ALA LYS MET LYS                                  
SEQRES   1 H   13    A A2M   G   C   G   C   C   A   G   A   A   C   U          
SEQRES   1 S  141  GTP   G   C   A   C   C   A   U   U   G   C   A   C          
SEQRES   2 S  141    U   C   C   G   G   U   G   C   C   A   G   U   U          
SEQRES   3 S  141    G   A   C   G   A   G   G   U   G   G   G   G   U          
SEQRES   4 S  141    U   U   A   U   C   G   A   G   A   U   U   U   C          
SEQRES   5 S  141    G   G   C   G   G   A   U   G   A   C   U   C   C          
SEQRES   6 S  141    C   G   G   U   U   G   U   U   C   A   U   C   A          
SEQRES   7 S  141    C   A   A   C   C   G   C   A   A   G   C   U   U          
SEQRES   8 S  141    U   U   A   C   U   U   A   A   A   U   C   A   U          
SEQRES   9 S  141    U   A   A   G   G   U   G   A   C   U   U   A   G          
SEQRES  10 S  141    U   G   G   A   C   A   A   A   G   G   U   G   A          
SEQRES  11 S  141    A   A   G   U   G   U   G   A   U   G   A                  
MODRES 3G8S A2M E    0    A  2'-O-METHYL-ADENOSINE-5'-MONOPHOSPHATE             
MODRES 3G8S GTP P   12    G  GUANOSINE-5'-TRIPHOSPHATE                          
MODRES 3G8S A2M F    0    A  2'-O-METHYL-ADENOSINE-5'-MONOPHOSPHATE             
MODRES 3G8S GTP Q   12    G  GUANOSINE-5'-TRIPHOSPHATE                          
MODRES 3G8S A2M G    0    A  2'-O-METHYL-ADENOSINE-5'-MONOPHOSPHATE             
MODRES 3G8S GTP R   12    G  GUANOSINE-5'-TRIPHOSPHATE                          
MODRES 3G8S A2M H    0    A  2'-O-METHYL-ADENOSINE-5'-MONOPHOSPHATE             
MODRES 3G8S GTP S   12    G  GUANOSINE-5'-TRIPHOSPHATE                          
HET    A2M  E   0      23                                                       
HET    GTP  P  12      32                                                       
HET    A2M  F   0      23                                                       
HET    GTP  Q  12      32                                                       
HET    A2M  G   0      23                                                       
HET    GTP  R  12      32                                                       
HET    A2M  H   0      23                                                       
HET    GTP  S  12      32                                                       
HET     MG  E  12       1                                                       
HET     MG  P   2       1                                                       
HET     MG  P  10       1                                                       
HET     MG  Q   3       1                                                       
HET     MG  Q   4       1                                                       
HET     MG  Q   5       1                                                       
HET     MG  R   6       1                                                       
HET     MG  R   7       1                                                       
HET     MG  H  12       1                                                       
HET     MG  S   9       1                                                       
HETNAM     A2M 2'-O-METHYLADENOSINE 5'-(DIHYDROGEN PHOSPHATE)                   
HETNAM     GTP GUANOSINE-5'-TRIPHOSPHATE                                        
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   2  A2M    4(C11 H16 N5 O7 P)                                           
FORMUL   3  GTP    4(C10 H16 N5 O14 P3)                                         
FORMUL  13   MG    10(MG 2+)                                                    
FORMUL  23  HOH   *79(H2 O)                                                     
HELIX    1   1 LYS A   22  SER A   35  1                                  14    
HELIX    2   2 GLU A   61  GLN A   73  1                                  13    
HELIX    3   3 SER A   91  LYS A   96  1                                   6    
HELIX    4   4 LYS B   22  SER B   35  1                                  14    
HELIX    5   5 ARG B   36  GLY B   38  5                                   3    
HELIX    6   6 GLU B   61  GLN B   73  1                                  13    
HELIX    7   7 SER B   91  LYS B   98  1                                   8    
HELIX    8   8 LYS C   22  PHE C   34  1                                  13    
HELIX    9   9 GLU C   61  GLN C   73  1                                  13    
HELIX   10  10 SER C   91  LYS C   96  1                                   6    
HELIX   11  11 LYS D   22  SER D   35  1                                  14    
HELIX   12  12 GLU D   61  GLN D   73  1                                  13    
HELIX   13  13 SER D   91  LYS D   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  GLN A  85   N  TYR A  13           
SHEET    1   B 4 ILE B  40  LEU B  44  0                                        
SHEET    2   B 4 ALA B  55  PHE B  59 -1  O  PHE B  56   N  LEU B  44           
SHEET    3   B 4 THR B  11  ASN B  15 -1  N  ILE B  12   O  VAL B  57           
SHEET    4   B 4 ARG B  83  TYR B  86 -1  O  GLN B  85   N  TYR B  13           
SHEET    1   C 2 PRO B  76  PHE B  77  0                                        
SHEET    2   C 2 LYS B  80  PRO B  81 -1  O  LYS B  80   N  PHE B  77           
SHEET    1   D 4 ILE C  40  VAL C  45  0                                        
SHEET    2   D 4 ALA C  55  PHE C  59 -1  O  ILE C  58   N  LEU C  41           
SHEET    3   D 4 THR C  11  ASN C  15 -1  N  ILE C  14   O  ALA C  55           
SHEET    4   D 4 ARG C  83  TYR C  86 -1  O  ARG C  83   N  ASN C  15           
SHEET    1   E 4 ILE D  40  LEU D  44  0                                        
SHEET    2   E 4 GLN D  54  PHE D  59 -1  O  ILE D  58   N  LEU D  41           
SHEET    3   E 4 THR D  11  ASN D  15 -1  N  ILE D  14   O  ALA D  55           
SHEET    4   E 4 ARG D  83  TYR D  86 -1  O  ARG D  83   N  ASN D  15           
LINK         O3'   A E  -1                 P   A2M E   0     1555   1555  1.60  
LINK         O3' A2M E   0                 P     G E   1     1555   1555  1.60  
LINK         O3' GTP P  12                 P     G P  13     1555   1555  1.60  
LINK         O3'   A F  -1                 P   A2M F   0     1555   1555  1.60  
LINK         O3' A2M F   0                 P     G F   1     1555   1555  1.60  
LINK         O3' GTP Q  12                 P     G Q  13     1555   1555  1.60  
LINK         O3'   A G  -1                 P   A2M G   0     1555   1555  1.60  
LINK         O3' A2M G   0                 P     G G   1     1555   1555  1.60  
LINK         O3' GTP R  12                 P     G R  13     1555   1555  1.60  
LINK         O3'   A H  -1                 P   A2M H   0     1555   1555  1.60  
LINK         O3' A2M H   0                 P     G H   1     1555   1555  1.60  
LINK         O3' GTP S  12                 P     G S  13     1555   1555  1.60  
LINK         OP2   C E   2                MG    MG P   2     1555   1555  2.16  
LINK         OP2   C P  29                MG    MG P   2     1555   1555  1.99  
LINK         OP2   G P  30                MG    MG P   2     1555   1555  2.11  
LINK         OP2   A P  31                MG    MG E  12     1555   1555  2.38  
LINK         OP2   C F   2                MG    MG Q   3     1555   1555  2.44  
LINK         OP2   C Q  29                MG    MG Q   3     1555   1555  2.10  
LINK         OP1   U Q  40                MG    MG Q   5     1555   1555  2.50  
LINK         OP2   C G   2                MG    MG R   7     1555   1555  2.49  
LINK         OP2   C R  29                MG    MG R   7     1555   1555  2.18  
LINK         OP2   G R  30                MG    MG R   7     1555   1555  2.34  
LINK         OP1   U R  40                MG    MG Q   4     1555   1555  2.50  
LINK         OP2   A R  46                MG    MG R   6     1555   1555  2.15  
LINK         OP2   C H   2                MG    MG S   9     1555   1555  2.20  
LINK         OP2   C S  29                MG    MG S   9     1555   1555  2.34  
LINK         OP2   G S  30                MG    MG S   9     1555   1555  2.47  
LINK         OP2   A S  31                MG    MG H  12     1555   1555  2.50  
SITE     1 AC1  2   C E   2    A P  31                                          
SITE     1 AC2  3   C E   2    C P  29    G P  30                               
SITE     1 AC3  5   G F   1    C F   2    A Q  28    C Q  29                    
SITE     2 AC3  5   G Q  30                                                     
SITE     1 AC4  3   U Q  19    U R  40    U R  93                               
SITE     1 AC5  3   U Q  40    U Q  93    U R  19                               
SITE     1 AC6  1   A R  46                                                     
SITE     1 AC7  3   C G   2    C R  29    G R  30                               
SITE     1 AC8  2   C H   2    A S  31                                          
SITE     1 AC9  4   C H   2    A S  28    C S  29    G S  30                    
SITE     1 BC1  2   A P  48    A S  46                                          
CRYST1   47.364  228.480  103.915  90.00  90.58  90.00 P 1 21 1      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      0.021113  0.000000  0.000214        0.00000                         
SCALE2      0.000000  0.004377  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009624        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system