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Database: PDB
Entry: 3ABD
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Original site: 3ABD 
HEADER    CELL CYCLE/REPLICATION                  07-DEC-09   3ABD              
TITLE     STRUCTURE OF HUMAN REV7 IN COMPLEX WITH A HUMAN REV3 FRAGMENT IN A    
TITLE    2 MONOCLINIC CRYSTAL                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2B;         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: REV7, MAD2-LIKE 2, HREV7;                                   
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: DNA POLYMERASE ZETA CATALYTIC SUBUNIT;                     
COMPND   9 CHAIN: X, Y;                                                         
COMPND  10 FRAGMENT: RESIDUES 1847-1898;                                        
COMPND  11 SYNONYM: REV3, HREV3;                                                
COMPND  12 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: REV7;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PETDUET;                                  
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: REV3;                                                          
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PETDUET                                   
KEYWDS    DNA POLYMERASE, HORMA, DNA REPLICATION, TRANSLESION DNA SYNTHESIS,    
KEYWDS   2 CELL CYCLE, CELL DIVISION, MITOSIS, DNA DAMAGE, DNA REPAIR, DNA-     
KEYWDS   3 BINDING, DNA-DIRECTED DNA POLYMERASE, CELL CYCLE-REPLICATION COMPLEX 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.HARA,H.HASHIMOTO,Y.MURAKUMO,S.KOBAYASHI,T.KOGAME,S.UNZAI,S.AKASHI,  
AUTHOR   2 S.TAKEDA,T.SHIMIZU,M.SATO                                            
REVDAT   4   11-OCT-17 3ABD    1       REMARK                                   
REVDAT   3   13-JUL-11 3ABD    1       VERSN                                    
REVDAT   2   21-APR-10 3ABD    1       JRNL                                     
REVDAT   1   16-FEB-10 3ABD    0                                                
JRNL        AUTH   K.HARA,H.HASHIMOTO,Y.MURAKUMO,S.KOBAYASHI,T.KOGAME,S.UNZAI,  
JRNL        AUTH 2 S.AKASHI,S.TAKEDA,T.SHIMIZU,M.SATO                           
JRNL        TITL   CRYSTAL STRUCTURE OF HUMAN REV7 IN COMPLEX WITH A HUMAN REV3 
JRNL        TITL 2 FRAGMENT AND STRUCTURAL IMPLICATION OF THE INTERACTION       
JRNL        TITL 3 BETWEEN DNA POLYMERASE {ZETA} AND REV1                       
JRNL        REF    J.BIOL.CHEM.                  V. 285 12299 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   20164194                                                     
JRNL        DOI    10.1074/JBC.M109.092403                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0066                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.96                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 33833                          
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) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.241                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1780                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2050                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2170                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 88                           
REMARK   3   BIN FREE R VALUE                    : 0.2600                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3360                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 257                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 25.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.13000                                             
REMARK   3    B22 (A**2) : -0.03000                                             
REMARK   3    B33 (A**2) : 0.17000                                              
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): 0.153         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.151         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.099         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.618         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3361 ; 0.020 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3165 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4577 ; 1.689 ; 1.979       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7361 ; 1.115 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   411 ; 5.976 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   136 ;29.522 ;24.779       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   583 ;15.204 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;27.738 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   551 ; 0.098 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3608 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   594 ; 0.008 ; 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):  2104 ; 0.927 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   822 ; 0.250 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3453 ; 1.716 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1257 ; 2.742 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1124 ; 4.445 ; 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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    12        A   211                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.3730   0.1100  10.4440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0542 T22:   0.0701                                     
REMARK   3      T33:   0.0105 T12:  -0.0001                                     
REMARK   3      T13:  -0.0045 T23:  -0.0214                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2894 L22:   2.0152                                     
REMARK   3      L33:   1.6599 L12:  -0.0947                                     
REMARK   3      L13:   0.5621 L23:   0.3264                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0021 S12:  -0.1184 S13:   0.0032                       
REMARK   3      S21:   0.1358 S22:   0.0176 S23:   0.0158                       
REMARK   3      S31:   0.0018 S32:  -0.1246 S33:  -0.0155                       
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    10        B   211                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.0050  22.7090  41.3890              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0861 T22:   0.0581                                     
REMARK   3      T33:   0.0152 T12:   0.0184                                     
REMARK   3      T13:   0.0080 T23:  -0.0244                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9878 L22:   2.1264                                     
REMARK   3      L33:   1.7329 L12:  -0.0363                                     
REMARK   3      L13:  -0.0117 L23:   0.5576                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0755 S12:   0.0512 S13:  -0.0225                       
REMARK   3      S21:  -0.2108 S22:  -0.0372 S23:  -0.0120                       
REMARK   3      S31:  -0.0057 S32:  -0.0142 S33:  -0.0383                       
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 3ABD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-DEC-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000029044.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-OCT-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-5A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35667                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.05500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
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   (%): 33.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 2000 MME, 0.8M SODIUM FORMATE,   
REMARK 280  0.1M TRIS-HCL PH 7.5,, VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  TEMPERATURE 293K                                                    
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       25.00450            
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                                                    
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2240 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, X                                  
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, Y                                  
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   -15                                                      
REMARK 465     GLY A   -14                                                      
REMARK 465     SER A   -13                                                      
REMARK 465     SER A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     HIS A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     SER A    -5                                                      
REMARK 465     GLN A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     PRO A    -2                                                      
REMARK 465     ASN A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     LEU A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     GLN A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     LEU A     9                                                      
REMARK 465     ASN A    10                                                      
REMARK 465     PHE A    11                                                      
REMARK 465     LEU A   107                                                      
REMARK 465     LEU A   108                                                      
REMARK 465     SER A   109                                                      
REMARK 465     ILE A   110                                                      
REMARK 465     SER A   111                                                      
REMARK 465     SER A   112                                                      
REMARK 465     GLU A   154                                                      
REMARK 465     ALA A   155                                                      
REMARK 465     ALA A   156                                                      
REMARK 465     THR A   157                                                      
REMARK 465     ARG A   158                                                      
REMARK 465     ASN A   159                                                      
REMARK 465     MET A   160                                                      
REMARK 465     GLU A   161                                                      
REMARK 465     LYS A   162                                                      
REMARK 465     ILE A   163                                                      
REMARK 465     GLN A   164                                                      
REMARK 465     VAL A   165                                                      
REMARK 465     ILE A   166                                                      
REMARK 465     LYS A   167                                                      
REMARK 465     MET X  1847                                                      
REMARK 465     LEU X  1848                                                      
REMARK 465     THR X  1849                                                      
REMARK 465     PRO X  1850                                                      
REMARK 465     THR X  1851                                                      
REMARK 465     PRO X  1852                                                      
REMARK 465     ASP X  1853                                                      
REMARK 465     SER X  1854                                                      
REMARK 465     SER X  1855                                                      
REMARK 465     PRO X  1856                                                      
REMARK 465     ARG X  1857                                                      
REMARK 465     SER X  1858                                                      
REMARK 465     THR X  1859                                                      
REMARK 465     SER X  1860                                                      
REMARK 465     SER X  1861                                                      
REMARK 465     PRO X  1862                                                      
REMARK 465     SER X  1863                                                      
REMARK 465     GLN X  1864                                                      
REMARK 465     SER X  1865                                                      
REMARK 465     LYS X  1866                                                      
REMARK 465     ASN X  1867                                                      
REMARK 465     GLY X  1868                                                      
REMARK 465     SER X  1869                                                      
REMARK 465     PHE X  1870                                                      
REMARK 465     THR X  1871                                                      
REMARK 465     PRO X  1872                                                      
REMARK 465     ARG X  1873                                                      
REMARK 465     LEU X  1895                                                      
REMARK 465     ASP X  1896                                                      
REMARK 465     HIS X  1897                                                      
REMARK 465     ASP X  1898                                                      
REMARK 465     MET B   -15                                                      
REMARK 465     GLY B   -14                                                      
REMARK 465     SER B   -13                                                      
REMARK 465     SER B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     HIS B    -9                                                      
REMARK 465     HIS B    -8                                                      
REMARK 465     HIS B    -7                                                      
REMARK 465     HIS B    -6                                                      
REMARK 465     SER B    -5                                                      
REMARK 465     GLN B    -4                                                      
REMARK 465     ASP B    -3                                                      
REMARK 465     PRO B    -2                                                      
REMARK 465     ASN B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     GLN B     7                                                      
REMARK 465     ASP B     8                                                      
REMARK 465     LEU B     9                                                      
REMARK 465     GLU B   154                                                      
REMARK 465     ALA B   155                                                      
REMARK 465     ALA B   156                                                      
REMARK 465     THR B   157                                                      
REMARK 465     ARG B   158                                                      
REMARK 465     ASN B   159                                                      
REMARK 465     MET B   160                                                      
REMARK 465     MET Y  1847                                                      
REMARK 465     LEU Y  1848                                                      
REMARK 465     THR Y  1849                                                      
REMARK 465     PRO Y  1850                                                      
REMARK 465     THR Y  1851                                                      
REMARK 465     PRO Y  1852                                                      
REMARK 465     ASP Y  1853                                                      
REMARK 465     SER Y  1854                                                      
REMARK 465     SER Y  1855                                                      
REMARK 465     PRO Y  1856                                                      
REMARK 465     ARG Y  1857                                                      
REMARK 465     SER Y  1858                                                      
REMARK 465     THR Y  1859                                                      
REMARK 465     SER Y  1860                                                      
REMARK 465     SER Y  1861                                                      
REMARK 465     PRO Y  1862                                                      
REMARK 465     SER Y  1863                                                      
REMARK 465     GLN Y  1864                                                      
REMARK 465     SER Y  1865                                                      
REMARK 465     LYS Y  1866                                                      
REMARK 465     ASN Y  1867                                                      
REMARK 465     GLY Y  1868                                                      
REMARK 465     SER Y  1869                                                      
REMARK 465     PHE Y  1870                                                      
REMARK 465     THR Y  1871                                                      
REMARK 465     PRO Y  1872                                                      
REMARK 465     ARG Y  1873                                                      
REMARK 465     ASP Y  1896                                                      
REMARK 465     HIS Y  1897                                                      
REMARK 465     ASP Y  1898                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLN A   13   CG   CD   OE1  NE2                                  
REMARK 480     LYS A   44   CD   CE   NZ                                        
REMARK 480     ARG A   45   NE   CZ   NH1  NH2                                  
REMARK 480     GLU A   76   CD   OE1  OE2                                       
REMARK 480     LYS A   77   CD   CE   NZ                                        
REMARK 480     LYS A   90   CD   CE   NZ                                        
REMARK 480     ASP A  113   CG   OD1  OD2                                       
REMARK 480     LEU A  115   CG   CD1  CD2                                       
REMARK 480     LYS B   44   CE   NZ                                             
REMARK 480     ARG B   45   CZ   NH1  NH2                                       
REMARK 480     LYS B   46   CD   CE   NZ                                        
REMARK 480     LYS B   90   CD   CE   NZ                                        
REMARK 480     LEU B  108   CG   CD1  CD2                                       
REMARK 480     GLU B  161   CG   CD   OE1  OE2                                  
REMARK 480     LYS B  162   CD   CE   NZ                                        
REMARK 480     GLN B  164   CG   CD   OE1  NE2                                  
REMARK 480     LYS B  167   CB   CG   CD   CE   NZ                              
REMARK 480     ASP B  168   CB   CG   OD1  OD2                                  
REMARK 480     GLN B  177   CG   CD   OE1  NE2                                  
REMARK 480     THR Y 1874   CB   OG1  CG2                                       
REMARK 480     GLU Y 1889   CG   CD   OE1  OE2                                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3ABE   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN IN A TETRAGONAL CRYSTAL                             
DBREF  3ABD A    1   211  UNP    Q9UI95   MD2L2_HUMAN      1    211             
DBREF  3ABD X 1847  1898  UNP    O60673   DPOLZ_HUMAN   1847   1898             
DBREF  3ABD B    1   211  UNP    Q9UI95   MD2L2_HUMAN      1    211             
DBREF  3ABD Y 1847  1898  UNP    O60673   DPOLZ_HUMAN   1847   1898             
SEQADV 3ABD MET A  -15  UNP  Q9UI95              INITIATING METHIONINE          
SEQADV 3ABD GLY A  -14  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD SER A  -13  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD SER A  -12  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD HIS A  -11  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD HIS A  -10  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD HIS A   -9  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD HIS A   -8  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD HIS A   -7  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD HIS A   -6  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD SER A   -5  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD GLN A   -4  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD ASP A   -3  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD PRO A   -2  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD ASN A   -1  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD SER A    0  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD ALA A  124  UNP  Q9UI95    ARG   124 ENGINEERED                     
SEQADV 3ABD MET B  -15  UNP  Q9UI95              INITIATING METHIONINE          
SEQADV 3ABD GLY B  -14  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD SER B  -13  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD SER B  -12  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD HIS B  -11  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD HIS B  -10  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD HIS B   -9  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD HIS B   -8  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD HIS B   -7  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD HIS B   -6  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD SER B   -5  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD GLN B   -4  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD ASP B   -3  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD PRO B   -2  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD ASN B   -1  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD SER B    0  UNP  Q9UI95              EXPRESSION TAG                 
SEQADV 3ABD ALA B  124  UNP  Q9UI95    ARG   124 ENGINEERED                     
SEQRES   1 A  227  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 A  227  PRO ASN SER MET THR THR LEU THR ARG GLN ASP LEU ASN          
SEQRES   3 A  227  PHE GLY GLN VAL VAL ALA ASP VAL LEU CYS GLU PHE LEU          
SEQRES   4 A  227  GLU VAL ALA VAL HIS LEU ILE LEU TYR VAL ARG GLU VAL          
SEQRES   5 A  227  TYR PRO VAL GLY ILE PHE GLN LYS ARG LYS LYS TYR ASN          
SEQRES   6 A  227  VAL PRO VAL GLN MET SER CYS HIS PRO GLU LEU ASN GLN          
SEQRES   7 A  227  TYR ILE GLN ASP THR LEU HIS CYS VAL LYS PRO LEU LEU          
SEQRES   8 A  227  GLU LYS ASN ASP VAL GLU LYS VAL VAL VAL VAL ILE LEU          
SEQRES   9 A  227  ASP LYS GLU HIS ARG PRO VAL GLU LYS PHE VAL PHE GLU          
SEQRES  10 A  227  ILE THR GLN PRO PRO LEU LEU SER ILE SER SER ASP SER          
SEQRES  11 A  227  LEU LEU SER HIS VAL GLU GLN LEU LEU ALA ALA PHE ILE          
SEQRES  12 A  227  LEU LYS ILE SER VAL CYS ASP ALA VAL LEU ASP HIS ASN          
SEQRES  13 A  227  PRO PRO GLY CYS THR PHE THR VAL LEU VAL HIS THR ARG          
SEQRES  14 A  227  GLU ALA ALA THR ARG ASN MET GLU LYS ILE GLN VAL ILE          
SEQRES  15 A  227  LYS ASP PHE PRO TRP ILE LEU ALA ASP GLU GLN ASP VAL          
SEQRES  16 A  227  HIS MET HIS ASP PRO ARG LEU ILE PRO LEU LYS THR MET          
SEQRES  17 A  227  THR SER ASP ILE LEU LYS MET GLN LEU TYR VAL GLU GLU          
SEQRES  18 A  227  ARG ALA HIS LYS GLY SER                                      
SEQRES   1 X   52  MET LEU THR PRO THR PRO ASP SER SER PRO ARG SER THR          
SEQRES   2 X   52  SER SER PRO SER GLN SER LYS ASN GLY SER PHE THR PRO          
SEQRES   3 X   52  ARG THR ALA ASN ILE LEU LYS PRO LEU MET SER PRO PRO          
SEQRES   4 X   52  SER ARG GLU GLU ILE MET ALA THR LEU LEU ASP HIS ASP          
SEQRES   1 B  227  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 B  227  PRO ASN SER MET THR THR LEU THR ARG GLN ASP LEU ASN          
SEQRES   3 B  227  PHE GLY GLN VAL VAL ALA ASP VAL LEU CYS GLU PHE LEU          
SEQRES   4 B  227  GLU VAL ALA VAL HIS LEU ILE LEU TYR VAL ARG GLU VAL          
SEQRES   5 B  227  TYR PRO VAL GLY ILE PHE GLN LYS ARG LYS LYS TYR ASN          
SEQRES   6 B  227  VAL PRO VAL GLN MET SER CYS HIS PRO GLU LEU ASN GLN          
SEQRES   7 B  227  TYR ILE GLN ASP THR LEU HIS CYS VAL LYS PRO LEU LEU          
SEQRES   8 B  227  GLU LYS ASN ASP VAL GLU LYS VAL VAL VAL VAL ILE LEU          
SEQRES   9 B  227  ASP LYS GLU HIS ARG PRO VAL GLU LYS PHE VAL PHE GLU          
SEQRES  10 B  227  ILE THR GLN PRO PRO LEU LEU SER ILE SER SER ASP SER          
SEQRES  11 B  227  LEU LEU SER HIS VAL GLU GLN LEU LEU ALA ALA PHE ILE          
SEQRES  12 B  227  LEU LYS ILE SER VAL CYS ASP ALA VAL LEU ASP HIS ASN          
SEQRES  13 B  227  PRO PRO GLY CYS THR PHE THR VAL LEU VAL HIS THR ARG          
SEQRES  14 B  227  GLU ALA ALA THR ARG ASN MET GLU LYS ILE GLN VAL ILE          
SEQRES  15 B  227  LYS ASP PHE PRO TRP ILE LEU ALA ASP GLU GLN ASP VAL          
SEQRES  16 B  227  HIS MET HIS ASP PRO ARG LEU ILE PRO LEU LYS THR MET          
SEQRES  17 B  227  THR SER ASP ILE LEU LYS MET GLN LEU TYR VAL GLU GLU          
SEQRES  18 B  227  ARG ALA HIS LYS GLY SER                                      
SEQRES   1 Y   52  MET LEU THR PRO THR PRO ASP SER SER PRO ARG SER THR          
SEQRES   2 Y   52  SER SER PRO SER GLN SER LYS ASN GLY SER PHE THR PRO          
SEQRES   3 Y   52  ARG THR ALA ASN ILE LEU LYS PRO LEU MET SER PRO PRO          
SEQRES   4 Y   52  SER ARG GLU GLU ILE MET ALA THR LEU LEU ASP HIS ASP          
FORMUL   5  HOH   *257(H2 O)                                                    
HELIX    1   1 GLY A   12  ARG A   34  1                                  23    
HELIX    2   2 PRO A   38  GLY A   40  5                                   3    
HELIX    3   3 HIS A   57  LYS A   77  1                                  21    
HELIX    4   4 SER A  114  VAL A  132  1                                  19    
HELIX    5   5 CYS A  133  VAL A  136  5                                   4    
HELIX    6   6 ASP A  175  HIS A  180  1                                   6    
HELIX    7   7 SER X 1886  LEU X 1894  1                                   9    
HELIX    8   8 PHE B   11  ARG B   34  1                                  24    
HELIX    9   9 PRO B   38  GLY B   40  5                                   3    
HELIX   10  10 HIS B   57  LYS B   77  1                                  21    
HELIX   11  11 SER B  114  VAL B  132  1                                  19    
HELIX   12  12 CYS B  133  VAL B  136  5                                   4    
HELIX   13  13 ASP B  175  HIS B  180  1                                   6    
HELIX   14  14 SER Y 1886  LEU Y 1894  1                                   9    
SHEET    1   A 2 PHE A  42  LYS A  47  0                                        
SHEET    2   A 2 VAL A  50  SER A  55 -1  O  VAL A  50   N  LYS A  47           
SHEET    1   B 7 TRP A 171  LEU A 173  0                                        
SHEET    2   B 7 ILE X1877  PRO X1880 -1  O  LYS X1879   N  ILE A 172           
SHEET    3   B 7 THR A 145  THR A 152 -1  N  VAL A 150   O  LEU X1878           
SHEET    4   B 7 VAL A  80  LEU A  88 -1  N  VAL A  84   O  LEU A 149           
SHEET    5   B 7 PRO A  94  THR A 103 -1  O  VAL A  95   N  ILE A  87           
SHEET    6   B 7 LYS A 198  ARG A 206 -1  O  LYS A 198   N  THR A 103           
SHEET    7   B 7 PRO A 184  THR A 193 -1  N  LYS A 190   O  LEU A 201           
SHEET    1   C 2 PHE B  42  LYS B  47  0                                        
SHEET    2   C 2 VAL B  50  SER B  55 -1  O  VAL B  52   N  ARG B  45           
SHEET    1   D 7 TRP B 171  LEU B 173  0                                        
SHEET    2   D 7 ILE Y1877  PRO Y1880 -1  O  LYS Y1879   N  ILE B 172           
SHEET    3   D 7 THR B 145  THR B 152 -1  N  VAL B 150   O  LEU Y1878           
SHEET    4   D 7 VAL B  80  LEU B  88 -1  N  VAL B  84   O  LEU B 149           
SHEET    5   D 7 PRO B  94  THR B 103 -1  O  VAL B  95   N  ILE B  87           
SHEET    6   D 7 LYS B 198  ARG B 206 -1  O  TYR B 202   N  VAL B  99           
SHEET    7   D 7 PRO B 184  MET B 192 -1  N  LYS B 190   O  LEU B 201           
CRYST1   43.870   50.009  107.275  90.00  96.90  90.00 P 1 21 1      4          
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      0.022795  0.000000  0.002759        0.00000                         
SCALE2      0.000000  0.019996  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009390        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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