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Database: PDB
Entry: 3M03
LinkDB: 3M03
Original site: 3M03 
HEADER    DNA BINDING PROTEIN                     02-MAR-10   3M03              
TITLE     CRYSTAL STRUCTURE OF HUMAN ORC6 FRAGMENT                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ORIGIN RECOGNITION COMPLEX SUBUNIT 6;                      
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: MIDDLE DOMAIN, REISDUES 93-187;                            
COMPND   5 SYNONYM: ORC6;                                                       
COMPND   6 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: ORC6;                                                          
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: PGEX4T                                    
KEYWDS    HELIX TURN HELIX, DNA BINDING PROTEIN, ORIGIN RECOGNITION COMPLEX,    
KEYWDS   2 DNA REPLICATION                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.X.LIU,L.J.WU,J.SUN,H.F.WANG,Y.F.LIU                                 
REVDAT   4   05-MAR-14 3M03    1       JRNL   VERSN                             
REVDAT   3   04-MAY-11 3M03    1       JRNL                                     
REVDAT   2   16-MAR-11 3M03    1       TITLE                                    
REVDAT   1   09-MAR-11 3M03    0                                                
JRNL        AUTH   S.X.LIU,M.BALASOV,H.F.WANG,L.J.WU,I.N.CHESNOKOV,Y.F.LIU      
JRNL        TITL   STRUCTURAL ANALYSIS OF HUMAN ORC6 PROTEIN REVEALS A HOMOLOGY 
JRNL        TITL 2 WITH TRANSCRIPTION FACTOR TFIIB                              
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 108  7373 2011              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   21502537                                                     
JRNL        DOI    10.1073/PNAS.1013676108                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 11398                          
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) : 0.228                           
REMARK   3   R VALUE            (WORKING SET) : 0.226                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 572                             
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.57                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 854                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3130                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 37                           
REMARK   3   BIN FREE R VALUE                    : 0.4040                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2101                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 17                                      
REMARK   3   SOLVENT ATOMS            : 58                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 57.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.18                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.25000                                             
REMARK   3    B22 (A**2) : -0.25000                                             
REMARK   3    B33 (A**2) : 0.50000                                              
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): 0.517         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.296         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.210         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.211        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.930                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.910                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2130 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2849 ; 1.399 ; 2.011       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   269 ; 7.461 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    73 ;37.226 ;25.890       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   450 ;21.082 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;14.268 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   350 ; 0.106 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1444 ; 0.010 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  1362 ; 1.107 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2192 ; 1.968 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   768 ; 3.345 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   657 ; 5.290 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    94        A   186                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.0746  21.4964  28.1548              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1252 T22:   0.2716                                     
REMARK   3      T33:   0.0853 T12:  -0.1111                                     
REMARK   3      T13:  -0.0282 T23:   0.0321                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5544 L22:   2.8044                                     
REMARK   3      L33:   4.8695 L12:   0.3267                                     
REMARK   3      L13:   0.9433 L23:  -0.8621                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1380 S12:   0.1089 S13:   0.3740                       
REMARK   3      S21:   0.0916 S22:  -0.0657 S23:  -0.2669                       
REMARK   3      S31:  -0.5397 S32:   0.7829 S33:   0.2037                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    93        B   187                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.0729   0.2213  30.7350              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0154 T22:   0.1376                                     
REMARK   3      T33:   0.1854 T12:   0.0367                                     
REMARK   3      T13:   0.0221 T23:   0.0436                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0816 L22:   5.8403                                     
REMARK   3      L33:   1.8924 L12:   0.3820                                     
REMARK   3      L13:   0.1885 L23:   0.2478                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0180 S12:  -0.0160 S13:  -0.3290                       
REMARK   3      S21:  -0.0121 S22:   0.0186 S23:   0.0762                       
REMARK   3      S31:   0.0472 S32:   0.2989 S33:  -0.0006                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    97        C   185                          
REMARK   3    ORIGIN FOR THE GROUP (A):  58.8419  10.4321  33.4452              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3118 T22:   0.8047                                     
REMARK   3      T33:   0.4312 T12:   0.0025                                     
REMARK   3      T13:  -0.0062 T23:   0.0943                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  18.4373 L22:   5.2872                                     
REMARK   3      L33:   2.1830 L12:  -3.7986                                     
REMARK   3      L13:   2.6859 L23:   0.2719                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2133 S12:   1.0534 S13:  -0.1351                       
REMARK   3      S21:   0.2776 S22:   0.2661 S23:   0.0302                       
REMARK   3      S31:  -0.2157 S32:  -0.1461 S33:  -0.0528                       
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 3M03 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-MAR-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB057938.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-NOV-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
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 FR-E SUPERBRIGHT            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12005                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 38.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.24                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MES, LI2SO4, PEG4000, PH 6.5, VAPOR      
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 289K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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    93                                                      
REMARK 465     ASP A   187                                                      
REMARK 465     MET C    93                                                      
REMARK 465     SER C    94                                                      
REMARK 465     ASN C    95                                                      
REMARK 465     ILE C    96                                                      
REMARK 465     GLN C   129                                                      
REMARK 465     GLN C   130                                                      
REMARK 465     VAL C   156                                                      
REMARK 465     VAL C   186                                                      
REMARK 465     ASP C   187                                                      
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    CYS B 107       41.93   -144.65                                   
REMARK 500    GLN C 104       23.33    -79.07                                   
REMARK 500    SER C 124       76.99   -172.23                                   
REMARK 500    LEU C 125      -40.71   -159.71                                   
REMARK 500    PRO C 138      -17.10    -47.81                                   
REMARK 500    LEU C 152       20.87    -74.64                                   
REMARK 500    GLN C 184       40.01    -97.42                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL A 167        22.6      L          L   OUTSIDE RANGE           
REMARK 500    LEU C 125        22.5      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1                   
DBREF  3M03 A   94   187  UNP    Q9Y5N6   ORC6_HUMAN      94    187             
DBREF  3M03 B   94   187  UNP    Q9Y5N6   ORC6_HUMAN      94    187             
DBREF  3M03 C   94   187  UNP    Q9Y5N6   ORC6_HUMAN      94    187             
SEQADV 3M03 MET A   93  UNP  Q9Y5N6              EXPRESSION TAG                 
SEQADV 3M03 MET B   93  UNP  Q9Y5N6              EXPRESSION TAG                 
SEQADV 3M03 MET C   93  UNP  Q9Y5N6              EXPRESSION TAG                 
SEQRES   1 A   95  MET SER ASN ILE GLY ILE ARG ASP LEU ALA VAL GLN PHE          
SEQRES   2 A   95  SER CYS ILE GLU ALA VAL ASN MET ALA SER LYS ILE LEU          
SEQRES   3 A   95  LYS SER TYR GLU SER SER LEU PRO GLN THR GLN GLN VAL          
SEQRES   4 A   95  ASP LEU ASP LEU SER ARG PRO LEU PHE THR SER ALA ALA          
SEQRES   5 A   95  LEU LEU SER ALA CYS LYS ILE LEU LYS LEU LYS VAL ASP          
SEQRES   6 A   95  LYS ASN LYS MET VAL ALA THR SER GLY VAL LYS LYS ALA          
SEQRES   7 A   95  ILE PHE ASP ARG LEU CYS LYS GLN LEU GLU LYS ILE GLY          
SEQRES   8 A   95  GLN GLN VAL ASP                                              
SEQRES   1 B   95  MET SER ASN ILE GLY ILE ARG ASP LEU ALA VAL GLN PHE          
SEQRES   2 B   95  SER CYS ILE GLU ALA VAL ASN MET ALA SER LYS ILE LEU          
SEQRES   3 B   95  LYS SER TYR GLU SER SER LEU PRO GLN THR GLN GLN VAL          
SEQRES   4 B   95  ASP LEU ASP LEU SER ARG PRO LEU PHE THR SER ALA ALA          
SEQRES   5 B   95  LEU LEU SER ALA CYS LYS ILE LEU LYS LEU LYS VAL ASP          
SEQRES   6 B   95  LYS ASN LYS MET VAL ALA THR SER GLY VAL LYS LYS ALA          
SEQRES   7 B   95  ILE PHE ASP ARG LEU CYS LYS GLN LEU GLU LYS ILE GLY          
SEQRES   8 B   95  GLN GLN VAL ASP                                              
SEQRES   1 C   95  MET SER ASN ILE GLY ILE ARG ASP LEU ALA VAL GLN PHE          
SEQRES   2 C   95  SER CYS ILE GLU ALA VAL ASN MET ALA SER LYS ILE LEU          
SEQRES   3 C   95  LYS SER TYR GLU SER SER LEU PRO GLN THR GLN GLN VAL          
SEQRES   4 C   95  ASP LEU ASP LEU SER ARG PRO LEU PHE THR SER ALA ALA          
SEQRES   5 C   95  LEU LEU SER ALA CYS LYS ILE LEU LYS LEU LYS VAL ASP          
SEQRES   6 C   95  LYS ASN LYS MET VAL ALA THR SER GLY VAL LYS LYS ALA          
SEQRES   7 C   95  ILE PHE ASP ARG LEU CYS LYS GLN LEU GLU LYS ILE GLY          
SEQRES   8 C   95  GLN GLN VAL ASP                                              
HET    MES  A   1      12                                                       
HET    SO4  B   1       5                                                       
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETNAM     SO4 SULFATE ION                                                      
FORMUL   4  MES    C6 H13 N O4 S                                                
FORMUL   5  SO4    O4 S 2-                                                      
FORMUL   6  HOH   *58(H2 O)                                                     
HELIX    1   1 GLY A   97  SER A  106  1                                  10    
HELIX    2   2 CYS A  107  GLU A  109  5                                   3    
HELIX    3   3 ALA A  110  SER A  123  1                                  14    
HELIX    4   4 PRO A  126  LEU A  133  1                                   8    
HELIX    5   5 ARG A  137  LEU A  152  1                                  16    
HELIX    6   6 ASP A  157  THR A  164  1                                   8    
HELIX    7   7 LYS A  168  GLN A  184  1                                  17    
HELIX    8   8 GLY B   97  SER B  106  1                                  10    
HELIX    9   9 CYS B  107  GLU B  109  5                                   3    
HELIX   10  10 ALA B  110  LEU B  125  1                                  16    
HELIX   11  11 PRO B  126  LEU B  133  1                                   8    
HELIX   12  12 ARG B  137  LYS B  153  1                                  17    
HELIX   13  13 ASP B  157  GLY B  166  1                                  10    
HELIX   14  14 LYS B  168  GLN B  184  1                                  17    
HELIX   15  15 ARG C   99  GLN C  104  1                                   6    
HELIX   16  16 CYS C  107  GLU C  109  5                                   3    
HELIX   17  17 ALA C  110  GLU C  122  1                                  13    
HELIX   18  18 ARG C  137  LEU C  152  1                                  16    
HELIX   19  19 ASP C  157  GLY C  166  1                                  10    
HELIX   20  20 LYS C  168  LYS C  181  1                                  14    
SSBOND   1 CYS C  107    CYS C  149                          1555   1555  2.74  
CISPEP   1 LEU C  125    PRO C  126          0       -27.49                     
SITE     1 AC1  6 ARG A 137  PRO A 138  LEU A 139  SER A 165                    
SITE     2 AC1  6 VAL A 167  GLN B 129                                          
SITE     1 AC2  2 GLN A 104  LYS B 169                                          
CRYST1  104.571  104.571   30.936  90.00  90.00  90.00 P 4          12          
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      0.009563  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009563  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.032325        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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