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Database: PDB
Entry: 1O8N
LinkDB: 1O8N
Original site: 1O8N 
HEADER    MOLYBDENUM COFACTOR BIOSYNTHESIS        28-NOV-02   1O8N              
TITLE     THE ACTIVE SITE OF THE MOLYBDENUM COFACTOR BIOSYNTHETIC PROTEIN DOMAIN
TITLE    2 CNX1G                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MOLYBDOPTERIN BIOSYNTHESIS CNX1 PROTEIN;                   
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: CNX1 G-DOMAIN, RESIDUES 462-628;                           
COMPND   5 SYNONYM: MOLYBDENUM COFACTOR, BIOSYNTHESIS ENZYME CNX1;              
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ARABIDOPSIS THALIANA;                           
SOURCE   3 ORGANISM_COMMON: MOUSE-EAR CRESS;                                    
SOURCE   4 ORGANISM_TAXID: 3702;                                                
SOURCE   5 STRAIN: CV. COLUMBIA;                                                
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: RK5206;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PQE60                                      
KEYWDS    MOLYBDENUM COFACTOR BIOSYNTHESIS, CNX1G, MUTANTS                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.KUPER,J.WINKING,H.J.HECHT,G.SCHWARZ,R.R.MENDEL                      
REVDAT   3   13-DEC-23 1O8N    1       REMARK                                   
REVDAT   2   24-FEB-09 1O8N    1       VERSN                                    
REVDAT   1   27-FEB-03 1O8N    0                                                
JRNL        AUTH   J.KUPER,J.WINKING,H.J.HECHT,R.R.MENDEL,G.SCHWARZ             
JRNL        TITL   THE ACTIVE SITE OF THE MOLYBDENUM COFACTOR BIOSYNTHETIC      
JRNL        TITL 2 PROTEIN DOMAIN CNX1G                                         
JRNL        REF    ARCH.BIOCHEM.BIOPHYS.         V. 411    36 2003              
JRNL        REFN                   ISSN 0003-9861                               
JRNL        PMID   12590921                                                     
JRNL        DOI    10.1016/S0003-9861(02)00714-2                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100.00                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 15773                          
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) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 844                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1128                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2890                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 69                           
REMARK   3   BIN FREE R VALUE                    : 0.3720                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3582                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 49                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.67                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.45000                                             
REMARK   3    B22 (A**2) : -0.45000                                             
REMARK   3    B33 (A**2) : 0.89000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.945         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.317         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.221         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.964        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.939                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.905                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3633 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3516 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4923 ; 1.488 ; 1.998       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8211 ; 0.846 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   483 ; 5.001 ; 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):   597 ; 0.072 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3978 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   612 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   765 ; 0.231 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3940 ; 0.249 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2140 ; 0.087 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    93 ; 0.173 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     5 ; 0.157 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    27 ; 0.332 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.206 ; 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):  2421 ; 0.801 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3912 ; 1.575 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1212 ; 2.181 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1011 ; 4.171 ; 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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B C                           
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      4       A      28      4                      
REMARK   3           1     B      4       B      28      4                      
REMARK   3           1     C      4       C      28      4                      
REMARK   3           2     A     30       A      44      4                      
REMARK   3           2     B     30       B      44      4                      
REMARK   3           2     C     30       C      44      4                      
REMARK   3           3     A     46       A     162      4                      
REMARK   3           3     B     46       B     162      4                      
REMARK   3           3     C     46       C     162      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   2290 ;  0.17 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   2290 ;  0.17 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    C    (A):   2290 ;  0.22 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   2290 ;  0.40 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   2290 ;  0.47 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    C (A**2):   2290 ;  0.46 ;  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 : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1O8N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-NOV-02.                  
REMARK 100 THE DEPOSITION ID IS D_1290011743.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-JUL-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : MIRROR                             
REMARK 200  OPTICS                         : OSMIX MIRROR                       
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU IMAGE PLATE                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15774                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 87.710                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : 0.07400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.15700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1EAV                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4 M SODIUM ACETATE 0.1 M SODIUM        
REMARK 280  CACODYLATE, PH 6.5, PH 6.50                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 41 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       3555   -Y,X+1/2,Z+1/4                                          
REMARK 290       4555   Y+1/2,-X,Z+3/4                                          
REMARK 290       5555   -X+1/2,Y,-Z+3/4                                         
REMARK 290       6555   X,-Y+1/2,-Z+1/4                                         
REMARK 290       7555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X,-Y,Z                                                 
REMARK 290      11555   -Y+1/2,X,Z+3/4                                          
REMARK 290      12555   Y,-X+1/2,Z+1/4                                          
REMARK 290      13555   -X,Y+1/2,-Z+1/4                                         
REMARK 290      14555   X+1/2,-Y,-Z+3/4                                         
REMARK 290      15555   Y,X,-Z                                                  
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
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       61.24300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000       61.24300            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       87.18000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       61.24300            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       43.59000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       61.24300            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      130.77000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       61.24300            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      130.77000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       61.24300            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       43.59000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000       61.24300            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       61.24300            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       87.18000            
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        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       61.24300            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       61.24300            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       87.18000            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       61.24300            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000      130.77000            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       61.24300            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       43.59000            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       61.24300            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       43.59000            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       61.24300            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      130.77000            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       61.24300            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       61.24300            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       87.18000            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED MUTATION IN CHAIN A, THR 542 ALA                          
REMARK 400 ENGINEERED MUTATION IN CHAIN B, THR 542 ALA                          
REMARK 400 ENGINEERED MUTATION IN CHAIN C, THR 542 ALA                          
REMARK 400                                                                      
REMARK 400  THE MOLECULE CNX1G IS INVOLVED IN MOLYBDENUM COFACTOR               
REMARK 400   BIOSYNTHESIS                                                       
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     VAL A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     LYS A   166                                                      
REMARK 465     ARG A   167                                                      
REMARK 465     VAL B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     LYS B   166                                                      
REMARK 465     ARG B   167                                                      
REMARK 465     VAL C     1                                                      
REMARK 465     PRO C     2                                                      
REMARK 465     LYS C   166                                                      
REMARK 465     ARG C   167                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP A 165    CA   C    O    CB   CG   OD1  OD2                   
REMARK 470     ASP B 165    CA   C    O    CB   CG   OD1  OD2                   
REMARK 470     ASP C 165    CA   C    O    CB   CG   OD1  OD2                   
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    ASP A  87   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP B  70   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP C  24   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP C  70   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP C  73   CB  -  CG  -  OD2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP C  87   CB  -  CG  -  OD2 ANGL. DEV. =   6.4 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    SER A  14      115.94   -174.30                                   
REMARK 500    SER B  14      113.15   -177.31                                   
REMARK 500    ASP B  87       97.92    -65.35                                   
REMARK 500    PRO C   4      142.04    -39.51                                   
REMARK 500    SER C  14      107.71    175.98                                   
REMARK 500    ASP C  87      102.23    -56.73                                   
REMARK 500    THR C 116      143.72   -172.74                                   
REMARK 500    SER C 124      134.45    -35.16                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1EAV   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURES OF HUMAN GEPHYRIN AND PLANT CNX1 G DOMAINS -      
REMARK 900 COMPARATIVE ANALYSIS AND FUNCTIONAL IMPLICATIONS                     
REMARK 900 RELATED ID: 1O8O   RELATED DB: PDB                                   
REMARK 900 THE ACTIVE SITE OF THE MOLYBDENUM COFACTOR BIOSENTHETIC PROTEIN      
REMARK 900 DOMAIN CNX1G                                                         
REMARK 900 RELATED ID: 1O8Q   RELATED DB: PDB                                   
REMARK 900 THE ACTIVE SITE OF THE MOLYBDENUM COFACTOR BIOSENTHETIC PROTEIN      
REMARK 900 DOMAIN CNX1G                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 DOMAIN DEFINITION MODIFIED FROM SWALL:CNX1_ARATH_2                   
REMARK 999  N-TERMINAL EXTENSION VPGP,                                          
REMARK 999  C-TERMINAL EXTENSION KQIKGDK                                        
DBREF  1O8N A    1   167  UNP    Q39054   CNX1_ARATH     462    628             
DBREF  1O8N B    1   167  UNP    Q39054   CNX1_ARATH     462    628             
DBREF  1O8N C    1   167  UNP    Q39054   CNX1_ARATH     462    628             
SEQADV 1O8N ALA A   81  UNP  Q39054    THR   542 ENGINEERED MUTATION            
SEQADV 1O8N ALA B   81  UNP  Q39054    THR   542 ENGINEERED MUTATION            
SEQADV 1O8N ALA C   81  UNP  Q39054    THR   542 ENGINEERED MUTATION            
SEQRES   1 A  167  VAL PRO GLY PRO GLU TYR LYS VAL ALA ILE LEU THR VAL          
SEQRES   2 A  167  SER ASP THR VAL SER ALA GLY ALA GLY PRO ASP ARG SER          
SEQRES   3 A  167  GLY PRO ARG ALA VAL SER VAL VAL ASP SER SER SER GLU          
SEQRES   4 A  167  LYS LEU GLY GLY ALA LYS VAL VAL ALA THR ALA VAL VAL          
SEQRES   5 A  167  PRO ASP GLU VAL GLU ARG ILE LYS ASP ILE LEU GLN LYS          
SEQRES   6 A  167  TRP SER ASP VAL ASP GLU MET ASP LEU ILE LEU THR LEU          
SEQRES   7 A  167  GLY GLY ALA GLY PHE THR PRO ARG ASP VAL THR PRO GLU          
SEQRES   8 A  167  ALA THR LYS LYS VAL ILE GLU ARG GLU THR PRO GLY LEU          
SEQRES   9 A  167  LEU PHE VAL MET MET GLN GLU SER LEU LYS ILE THR PRO          
SEQRES  10 A  167  PHE ALA MET LEU SER ARG SER ALA ALA GLY ILE ARG GLY          
SEQRES  11 A  167  SER THR LEU ILE ILE ASN MET PRO GLY ASN PRO ASN ALA          
SEQRES  12 A  167  VAL ALA GLU CYS MET GLU ALA LEU LEU PRO ALA LEU LYS          
SEQRES  13 A  167  HIS ALA LEU LYS GLN ILE LYS GLY ASP LYS ARG                  
SEQRES   1 B  167  VAL PRO GLY PRO GLU TYR LYS VAL ALA ILE LEU THR VAL          
SEQRES   2 B  167  SER ASP THR VAL SER ALA GLY ALA GLY PRO ASP ARG SER          
SEQRES   3 B  167  GLY PRO ARG ALA VAL SER VAL VAL ASP SER SER SER GLU          
SEQRES   4 B  167  LYS LEU GLY GLY ALA LYS VAL VAL ALA THR ALA VAL VAL          
SEQRES   5 B  167  PRO ASP GLU VAL GLU ARG ILE LYS ASP ILE LEU GLN LYS          
SEQRES   6 B  167  TRP SER ASP VAL ASP GLU MET ASP LEU ILE LEU THR LEU          
SEQRES   7 B  167  GLY GLY ALA GLY PHE THR PRO ARG ASP VAL THR PRO GLU          
SEQRES   8 B  167  ALA THR LYS LYS VAL ILE GLU ARG GLU THR PRO GLY LEU          
SEQRES   9 B  167  LEU PHE VAL MET MET GLN GLU SER LEU LYS ILE THR PRO          
SEQRES  10 B  167  PHE ALA MET LEU SER ARG SER ALA ALA GLY ILE ARG GLY          
SEQRES  11 B  167  SER THR LEU ILE ILE ASN MET PRO GLY ASN PRO ASN ALA          
SEQRES  12 B  167  VAL ALA GLU CYS MET GLU ALA LEU LEU PRO ALA LEU LYS          
SEQRES  13 B  167  HIS ALA LEU LYS GLN ILE LYS GLY ASP LYS ARG                  
SEQRES   1 C  167  VAL PRO GLY PRO GLU TYR LYS VAL ALA ILE LEU THR VAL          
SEQRES   2 C  167  SER ASP THR VAL SER ALA GLY ALA GLY PRO ASP ARG SER          
SEQRES   3 C  167  GLY PRO ARG ALA VAL SER VAL VAL ASP SER SER SER GLU          
SEQRES   4 C  167  LYS LEU GLY GLY ALA LYS VAL VAL ALA THR ALA VAL VAL          
SEQRES   5 C  167  PRO ASP GLU VAL GLU ARG ILE LYS ASP ILE LEU GLN LYS          
SEQRES   6 C  167  TRP SER ASP VAL ASP GLU MET ASP LEU ILE LEU THR LEU          
SEQRES   7 C  167  GLY GLY ALA GLY PHE THR PRO ARG ASP VAL THR PRO GLU          
SEQRES   8 C  167  ALA THR LYS LYS VAL ILE GLU ARG GLU THR PRO GLY LEU          
SEQRES   9 C  167  LEU PHE VAL MET MET GLN GLU SER LEU LYS ILE THR PRO          
SEQRES  10 C  167  PHE ALA MET LEU SER ARG SER ALA ALA GLY ILE ARG GLY          
SEQRES  11 C  167  SER THR LEU ILE ILE ASN MET PRO GLY ASN PRO ASN ALA          
SEQRES  12 C  167  VAL ALA GLU CYS MET GLU ALA LEU LEU PRO ALA LEU LYS          
SEQRES  13 C  167  HIS ALA LEU LYS GLN ILE LYS GLY ASP LYS ARG                  
FORMUL   4  HOH   *49(H2 O)                                                     
HELIX    1   1 SER A   14  ALA A   19  1                                   6    
HELIX    2   2 ARG A   25  SER A   37  1                                  13    
HELIX    3   3 GLU A   55  VAL A   69  1                                  15    
HELIX    4   4 VAL A   88  ILE A   97  1                                  10    
HELIX    5   5 THR A  101  THR A  116  1                                  16    
HELIX    6   6 PRO A  117  SER A  122  5                                   6    
HELIX    7   7 ASN A  140  GLY A  164  1                                  25    
HELIX    8   8 SER B   14  ALA B   19  1                                   6    
HELIX    9   9 SER B   26  SER B   37  1                                  12    
HELIX   10  10 GLU B   55  VAL B   69  1                                  15    
HELIX   11  11 VAL B   88  ILE B   97  1                                  10    
HELIX   12  12 THR B  101  THR B  116  1                                  16    
HELIX   13  13 PRO B  117  SER B  122  5                                   6    
HELIX   14  14 ASN B  140  GLY B  164  1                                  25    
HELIX   15  15 SER C   14  ALA C   19  1                                   6    
HELIX   16  16 ARG C   25  SER C   38  1                                  14    
HELIX   17  17 GLU C   55  VAL C   69  1                                  15    
HELIX   18  18 VAL C   88  ILE C   97  1                                  10    
HELIX   19  19 THR C  101  LYS C  114  1                                  14    
HELIX   20  20 THR C  116  SER C  122  5                                   7    
HELIX   21  21 ASN C  140  GLY C  164  1                                  25    
SHEET    1  AA 6 ALA A  44  VAL A  52  0                                        
SHEET    2  AA 6 TYR A   6  VAL A  13  1  O  TYR A   6   N  LYS A  45           
SHEET    3  AA 6 LEU A  74  LEU A  78  1  O  LEU A  74   N  ALA A   9           
SHEET    4  AA 6 THR A 132  MET A 137  1  O  LEU A 133   N  ILE A  75           
SHEET    5  AA 6 ALA A 126  ARG A 129 -1  O  GLY A 127   N  ILE A 134           
SHEET    6  AA 6 ARG A  99  GLU A 100 -1  O  ARG A  99   N  ILE A 128           
SHEET    1  BA 6 ALA B  44  VAL B  52  0                                        
SHEET    2  BA 6 TYR B   6  VAL B  13  1  O  TYR B   6   N  LYS B  45           
SHEET    3  BA 6 LEU B  74  LEU B  78  1  O  LEU B  74   N  ALA B   9           
SHEET    4  BA 6 THR B 132  MET B 137  1  O  LEU B 133   N  ILE B  75           
SHEET    5  BA 6 ALA B 126  ARG B 129 -1  O  GLY B 127   N  ILE B 134           
SHEET    6  BA 6 ARG B  99  GLU B 100 -1  O  ARG B  99   N  ILE B 128           
SHEET    1  CA 6 ALA C  44  VAL C  52  0                                        
SHEET    2  CA 6 TYR C   6  VAL C  13  1  O  TYR C   6   N  LYS C  45           
SHEET    3  CA 6 LEU C  74  LEU C  78  1  O  LEU C  74   N  ALA C   9           
SHEET    4  CA 6 THR C 132  MET C 137  1  O  LEU C 133   N  ILE C  75           
SHEET    5  CA 6 ALA C 126  ARG C 129 -1  O  GLY C 127   N  ILE C 134           
SHEET    6  CA 6 ARG C  99  GLU C 100 -1  O  ARG C  99   N  ILE C 128           
CRYST1  122.486  122.486  174.360  90.00  90.00  90.00 I 41 2 2     48          
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      0.008164  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008164  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005735        0.00000                         
MTRIX1   1  0.491908  0.630518  0.600395       53.60710    1                    
MTRIX2   1 -0.360731 -0.480023  0.799657       44.82480    1                    
MTRIX3   1  0.792401 -0.609939 -0.008679      -84.97820    1                    
MTRIX1   2  0.496506 -0.378581  0.781126       -3.61500    1                    
MTRIX2   2  0.621857 -0.472707 -0.624373      110.09260    1                    
MTRIX3   2  0.605619  0.795754  0.000722      -14.45150    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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