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Database: PDB
Entry: 2ZIX
LinkDB: 2ZIX
Original site: 2ZIX 
HEADER    HYDROLASE                               25-FEB-08   2ZIX              
TITLE     CRYSTAL STRUCTURE OF THE MUS81-EME1 COMPLEX                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CROSSOVER JUNCTION ENDONUCLEASE MUS81;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: NUCLEASE DOMAIN AND C-TERMINAL DOMAIN, UNP                 
COMPND   5 RESIDUES 246-551;                                                    
COMPND   6 SYNONYM: DNA STRUCTURE SPECIFIC ENDONUCLEASE MUS81;                  
COMPND   7 EC: 3.1.22.-;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: CROSSOVER JUNCTION ENDONUCLEASE EME1;                      
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: NUCLEASE-LIKE DOMAIN AND C-TERMINAL DOMAIN, UNP            
COMPND  13 RESIDUES 246-570;                                                    
COMPND  14 SYNONYM: HMMS4, DNA REPAIR PROTEIN EME1;                             
COMPND  15 EC: 3.1.22.-;                                                        
COMPND  16 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: MUS81;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
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: PCDF DUET;                                
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: EME1;                                                          
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
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: PET DUET                                  
KEYWDS    HELIX-HAIRPIN-HELIX, DNA DAMAGE, DNA RECOMBINATION, DNA               
KEYWDS   2 REPAIR, ENDONUCLEASE, HYDROLASE, MAGNESIUM, METAL-BINDING,           
KEYWDS   3 NUCLEASE, NUCLEUS, POLYMORPHISM, ALTERNATIVE SPLICING,               
KEYWDS   4 PHOSPHOPROTEIN                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.H.CHANG,J.J.KIM,J.M.CHOI,J.H.LEE,Y.CHO                              
REVDAT   2   24-FEB-09 2ZIX    1       VERSN                                    
REVDAT   1   29-APR-08 2ZIX    0                                                
JRNL        AUTH   J.H.CHANG,J.J.KIM,J.M.CHOI,J.H.LEE,Y.CHO                     
JRNL        TITL   CRYSTAL STRUCTURE OF THE MUS81-EME1 COMPLEX                  
JRNL        REF    GENES DEV.                    V.  22  1093 2008              
JRNL        REFN                   ISSN 0890-9369                               
JRNL        PMID   18413719                                                     
JRNL        DOI    10.1101/GAD.1618708                                          
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 8746                           
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) : 0.288                           
REMARK   3   R VALUE            (WORKING SET) : 0.285                           
REMARK   3   FREE R VALUE                     : 0.346                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 441                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.59                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 483                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 72.78                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 25                           
REMARK   3   BIN FREE R VALUE                    : 0.4340                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4154                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.09                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.75000                                              
REMARK   3    B22 (A**2) : 2.75000                                              
REMARK   3    B33 (A**2) : -4.12000                                             
REMARK   3    B12 (A**2) : 1.37000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.869         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.355         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.698        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.842                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.821                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4212 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5692 ; 2.078 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   519 ;13.866 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   193 ;44.204 ;23.264       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   755 ;27.534 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    44 ;21.452 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   669 ; 0.167 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3113 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3506 ; 0.411 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2763 ; 0.344 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   245 ; 0.378 ; 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):   109 ; 0.425 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.361 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED 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  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2ZIX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-MAR-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB028029.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-SEP-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 4A                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10913                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY                : 9.800                              
REMARK 200  R MERGE                    (I) : 0.13100                            
REMARK 200  R SYM                      (I) : 0.09400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.52                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30300                            
REMARK 200  R SYM FOR SHELL            (I) : 0.35900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2ZIU                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BTP, 1.25M LI2SO4, 100MM            
REMARK 280  MGCL2, 2MM CDCL2, VAPOR DIFFUSION, HANGING DROP, PH 6.5,            
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.80300            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      117.60600            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      117.60600            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       58.80300            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6510 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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   245                                                      
REMARK 465     SER A   246                                                      
REMARK 465     ALA A   247                                                      
REMARK 465     GLU A   248                                                      
REMARK 465     LEU A   249                                                      
REMARK 465     ALA A   250                                                      
REMARK 465     SER A   251                                                      
REMARK 465     GLU A   252                                                      
REMARK 465     ALA A   253                                                      
REMARK 465     GLY A   254                                                      
REMARK 465     VAL A   255                                                      
REMARK 465     GLN A   256                                                      
REMARK 465     GLN A   257                                                      
REMARK 465     GLN A   258                                                      
REMARK 465     GLY A   281                                                      
REMARK 465     GLY A   282                                                      
REMARK 465     HIS A   283                                                      
REMARK 465     PRO A   317                                                      
REMARK 465     ARG A   318                                                      
REMARK 465     ASP A   319                                                      
REMARK 465     PRO A   320                                                      
REMARK 465     TRP A   433                                                      
REMARK 465     GLY A   434                                                      
REMARK 465     THR A   435                                                      
REMARK 465     PRO A   436                                                      
REMARK 465     GLY A   437                                                      
REMARK 465     ASN A   438                                                      
REMARK 465     PRO A   439                                                      
REMARK 465     GLU A   440                                                      
REMARK 465     SER A   441                                                      
REMARK 465     GLY A   442                                                      
REMARK 465     ALA A   443                                                      
REMARK 465     MET A   444                                                      
REMARK 465     THR A   445                                                      
REMARK 465     SER A   446                                                      
REMARK 465     PRO A   447                                                      
REMARK 465     ASN A   448                                                      
REMARK 465     MET B   230                                                      
REMARK 465     GLY B   231                                                      
REMARK 465     SER B   232                                                      
REMARK 465     SER B   233                                                      
REMARK 465     HIS B   234                                                      
REMARK 465     HIS B   235                                                      
REMARK 465     HIS B   236                                                      
REMARK 465     HIS B   237                                                      
REMARK 465     HIS B   238                                                      
REMARK 465     HIS B   239                                                      
REMARK 465     SER B   240                                                      
REMARK 465     GLN B   241                                                      
REMARK 465     ASP B   242                                                      
REMARK 465     PRO B   243                                                      
REMARK 465     ASN B   244                                                      
REMARK 465     SER B   245                                                      
REMARK 465     GLU B   246                                                      
REMARK 465     ARG B   296                                                      
REMARK 465     ALA B   297                                                      
REMARK 465     GLY B   298                                                      
REMARK 465     PRO B   299                                                      
REMARK 465     SER B   300                                                      
REMARK 465     GLU B   301                                                      
REMARK 465     ASP B   302                                                      
REMARK 465     ARG B   303                                                      
REMARK 465     GLU B   304                                                      
REMARK 465     GLN B   330                                                      
REMARK 465     GLY B   331                                                      
REMARK 465     SER B   332                                                      
REMARK 465     LEU B   333                                                      
REMARK 465     ASP B   334                                                      
REMARK 465     SER B   335                                                      
REMARK 465     THR B   336                                                      
REMARK 465     MET B   337                                                      
REMARK 465     LYS B   338                                                      
REMARK 465     GLY B   339                                                      
REMARK 465     LYS B   340                                                      
REMARK 465     GLU B   341                                                      
REMARK 465     LYS B   368                                                      
REMARK 465     CYS B   369                                                      
REMARK 465     PHE B   370                                                      
REMARK 465     SER B   371                                                      
REMARK 465     ALA B   372                                                      
REMARK 465     GLN B   373                                                      
REMARK 465     ASN B   374                                                      
REMARK 465     PRO B   375                                                      
REMARK 465     PRO B   376                                                      
REMARK 465     ARG B   377                                                      
REMARK 465     ARG B   378                                                      
REMARK 465     GLY B   379                                                      
REMARK 465     LYS B   380                                                      
REMARK 465     GLN B   381                                                      
REMARK 465     GLY B   382                                                      
REMARK 465     ALA B   383                                                      
REMARK 465     ASN B   384                                                      
REMARK 465     LYS B   385                                                      
REMARK 465     GLN B   386                                                      
REMARK 465     THR B   387                                                      
REMARK 465     LYS B   388                                                      
REMARK 465     LYS B   389                                                      
REMARK 465     GLN B   390                                                      
REMARK 465     GLN B   391                                                      
REMARK 465     GLN B   392                                                      
REMARK 465     ARG B   393                                                      
REMARK 465     GLN B   394                                                      
REMARK 465     PRO B   395                                                      
REMARK 465     GLU B   396                                                      
REMARK 465     ALA B   397                                                      
REMARK 465     SER B   398                                                      
REMARK 465     ILE B   399                                                      
REMARK 465     GLY B   400                                                      
REMARK 465     SER B   401                                                      
REMARK 465     MET B   402                                                      
REMARK 465     VAL B   403                                                      
REMARK 465     PHE B   448                                                      
REMARK 465     LYS B   449                                                      
REMARK 465     GLY B   537                                                      
REMARK 465     VAL B   538                                                      
REMARK 465     THR B   539                                                      
REMARK 465     SER B   540                                                      
REMARK 465     ALA B   569                                                      
REMARK 465     ASP B   570                                                      
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     LYS B 450    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   N    ALA A   312     OE1  GLU A   325              1.69            
REMARK 500   O    ASP A   495     OG   SER A   498              1.85            
REMARK 500   O    GLY A   418     NH2  ARG A   421              1.89            
REMARK 500   OG1  THR A   518     OG   SER A   521              1.92            
REMARK 500   OE1  GLU A   261     O    LEU A   428              1.95            
REMARK 500   O    LEU A   536     CB   LEU A   540              1.95            
REMARK 500   O    SER B   493     N    MET B   496              1.95            
REMARK 500   O    GLY B   265     N    LEU B   269              1.96            
REMARK 500   OE1  GLU B   247     NZ   LYS B   250              1.97            
REMARK 500   O    CYS A   341     N    SER A   343              1.99            
REMARK 500   O    ALA A   463     N    LYS A   465              1.99            
REMARK 500   O    LEU A   328     N    HIS A   330              2.02            
REMARK 500   CG1  ILE B   253     O    ARG B   279              2.02            
REMARK 500   OD2  ASP A   307     N    ARG A   334              2.04            
REMARK 500   O    VAL B   312     N    SER B   360              2.05            
REMARK 500   NH1  ARG A   268     O    GLU A   314              2.06            
REMARK 500   O    GLU A   369     CE1  HIS A   371              2.06            
REMARK 500   NE1  TRP B   482     O    TYR B   504              2.07            
REMARK 500   OD2  ASP A   274     OE1  GLU A   277              2.07            
REMARK 500   O    ASP A   458     CA   GLY A   462              2.07            
REMARK 500   O    LEU B   509     N    GLN B   512              2.08            
REMARK 500   O    ARG B   483     N    ILE B   486              2.08            
REMARK 500   O    LYS A   524     O    ARG A   530              2.09            
REMARK 500   O    LEU B   555     N    MET B   557              2.10            
REMARK 500   CB   ASP A   329     OE1  GLU A   362              2.11            
REMARK 500   O    GLN B   524     O    SER B   550              2.14            
REMARK 500   O    ASN A   390     N    GLN A   392              2.14            
REMARK 500   O    ASP A   458     N    GLY A   462              2.15            
REMARK 500   O    VAL B   255     O    THR B   292              2.16            
REMARK 500   O    PRO A   534     OG   SER A   537              2.16            
REMARK 500   O    ALA A   535     N    ARG A   538              2.18            
REMARK 500   O    MET B   496     N    ALA B   499              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    GLY B   266     O    GLY B   266     6555     1.90            
REMARK 500   CD   PRO A   380     NH1  ARG A   538     4555     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PRO A 380   CG    PRO A 380   CD      0.163                       
REMARK 500    ARG B 484   CG    ARG B 484   CD      0.238                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 339   N   -  CA  -  C   ANGL. DEV. = -23.6 DEGREES          
REMARK 500    PRO A 380   N   -  CA  -  C   ANGL. DEV. =  16.8 DEGREES          
REMARK 500    ASP B 365   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 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    GLU A 261     -126.23   -130.40                                   
REMARK 500    LEU A 262        4.83    161.11                                   
REMARK 500    ARG A 263      121.79    129.34                                   
REMARK 500    PRO A 264       19.07    -59.57                                   
REMARK 500    GLU A 266      -68.39   -108.03                                   
REMARK 500    LEU A 270      178.06    178.07                                   
REMARK 500    VAL A 273     -151.46    -80.40                                   
REMARK 500    ASP A 274     -168.22   -124.61                                   
REMARK 500    THR A 278     -117.04   -125.91                                   
REMARK 500    ARG A 279       55.00    -40.34                                   
REMARK 500    PRO A 285       78.06    -62.19                                   
REMARK 500    GLU A 286      -10.15    -40.61                                   
REMARK 500    LEU A 287       22.23   -148.91                                   
REMARK 500    LEU A 288      -94.77    -74.12                                   
REMARK 500    ARG A 289        8.27    -68.40                                   
REMARK 500    HIS A 295       89.16     40.47                                   
REMARK 500    THR A 297       87.27    -69.04                                   
REMARK 500    VAL A 305       -1.94    178.68                                   
REMARK 500    ASP A 307      -83.58    -40.01                                   
REMARK 500    VAL A 309      170.41    171.73                                   
REMARK 500    TRP A 310       86.36    -55.53                                   
REMARK 500    ALA A 312     -170.53    -66.57                                   
REMARK 500    THR A 315       63.79     72.53                                   
REMARK 500    GLU A 325       77.83   -174.33                                   
REMARK 500    VAL A 327      140.57     69.70                                   
REMARK 500    ASP A 329       -1.02    -29.49                                   
REMARK 500    ARG A 334      119.30    154.84                                   
REMARK 500    CYS A 341      -71.14    -45.14                                   
REMARK 500    SER A 342       -0.74    -47.69                                   
REMARK 500    ASP A 346      -76.46   -155.14                                   
REMARK 500    ARG A 348      -35.50    -27.91                                   
REMARK 500    PHE A 349      -88.94    -35.60                                   
REMARK 500    GLU A 351      -71.21    -74.66                                   
REMARK 500    LEU A 356       59.97     37.00                                   
REMARK 500    LYS A 357      -86.10   -102.29                                   
REMARK 500    CYS A 359     -135.41     19.87                                   
REMARK 500    GLU A 362      -79.66     30.82                                   
REMARK 500    GLU A 369     -138.27    -90.85                                   
REMARK 500    GLU A 370      132.73    -16.83                                   
REMARK 500    HIS A 371       15.25   -141.57                                   
REMARK 500    SER A 373     -144.58     95.16                                   
REMARK 500    SER A 378      -27.44   -177.33                                   
REMARK 500    PRO A 380       80.24     39.45                                   
REMARK 500    GLU A 381      -56.53    -17.57                                   
REMARK 500    SER A 382      -94.78    -26.92                                   
REMARK 500    VAL A 388      -84.90    -52.89                                   
REMARK 500    THR A 389      -65.18    -28.52                                   
REMARK 500    ASN A 390      -65.79    -23.82                                   
REMARK 500    THR A 391       -1.16    -45.89                                   
REMARK 500    ILE A 394      -62.01   -121.53                                   
REMARK 500    ASP A 395      -53.88    -25.77                                   
REMARK 500    PHE A 397     -132.63   -121.40                                   
REMARK 500    THR A 402       79.89    -57.75                                   
REMARK 500    LYS A 406      -88.25    -59.07                                   
REMARK 500    TYR A 411      -54.36    -29.73                                   
REMARK 500    LEU A 414       -8.29    -47.73                                   
REMARK 500    LEU A 415      -69.98   -121.28                                   
REMARK 500    THR A 416      -13.21    -45.11                                   
REMARK 500    ARG A 417      -17.39   -143.69                                   
REMARK 500    LEU A 419       59.86    -66.11                                   
REMARK 500    GLN A 424      172.88      2.02                                   
REMARK 500    HIS A 426     -122.15    -92.82                                   
REMARK 500    THR A 427      -27.95   -166.68                                   
REMARK 500    LEU A 428      134.36     62.16                                   
REMARK 500    SER A 430       55.26   -164.01                                   
REMARK 500    ARG A 431      -74.39    -41.11                                   
REMARK 500    LEU A 453      -87.70   -159.55                                   
REMARK 500    LEU A 454      -61.98   -148.35                                   
REMARK 500    THR A 455     -123.82     68.96                                   
REMARK 500    SER A 457      -43.17     50.57                                   
REMARK 500    ASP A 458      -63.90    -18.41                                   
REMARK 500    ASN A 460      -73.02    -47.32                                   
REMARK 500    ILE A 464      -42.96     -0.06                                   
REMARK 500    ASN A 466      -29.70    178.94                                   
REMARK 500    LYS A 467      -72.86    -40.80                                   
REMARK 500    VAL A 471       20.38    -70.22                                   
REMARK 500    PHE A 475       56.56    -63.69                                   
REMARK 500    ALA A 476      -48.31   -172.10                                   
REMARK 500    LEU A 479      -73.82    -73.81                                   
REMARK 500    GLN A 481       68.47    -42.19                                   
REMARK 500    SER A 486     -174.13    -64.59                                   
REMARK 500    ALA A 491      -93.15     28.55                                   
REMARK 500    ALA A 492      -39.13    148.39                                   
REMARK 500    ASP A 495      -70.14    -58.96                                   
REMARK 500    THR A 499      164.20    136.23                                   
REMARK 500    CYS A 510      137.18    136.67                                   
REMARK 500    LEU A 519      -61.59    -17.69                                   
REMARK 500    SER A 521      -65.76    -21.29                                   
REMARK 500    THR A 522     -136.67   -118.79                                   
REMARK 500    ILE A 523      -51.36    147.29                                   
REMARK 500    LYS A 524      -42.07    117.29                                   
REMARK 500    CYS A 525      167.10     53.14                                   
REMARK 500    GLN A 529       97.00     41.31                                   
REMARK 500    ASN A 531      139.19      2.70                                   
REMARK 500    PRO A 534      -75.30    -63.09                                   
REMARK 500    ALA A 535      -87.94    -10.59                                   
REMARK 500    LEU A 536      -67.73     -6.95                                   
REMARK 500    ARG A 538      -85.68    -64.80                                   
REMARK 500    THR A 539      -63.03    -27.49                                   
REMARK 500    GLN A 542       13.64    -51.11                                   
REMARK 500    LEU A 543      -34.79   -144.59                                   
REMARK 500    CYS A 545      -20.23   -144.84                                   
REMARK 500    SER A 546      101.94    -47.99                                   
REMARK 500    TYR A 547       33.22    -70.51                                   
REMARK 500    PRO A 549      117.68    -16.20                                   
REMARK 500    CYS B 248      -44.65   -160.02                                   
REMARK 500    LEU B 249     -125.16    -53.13                                   
REMARK 500    LYS B 250      166.36     57.45                                   
REMARK 500    HIS B 251      -16.72     87.03                                   
REMARK 500    ASP B 257      104.18    -51.52                                   
REMARK 500    PRO B 258       15.24    -57.19                                   
REMARK 500    LEU B 260       43.42    121.08                                   
REMARK 500    LEU B 261      -38.11   -149.49                                   
REMARK 500    GLN B 262       39.70    -71.79                                   
REMARK 500    MET B 263      -70.32   -114.90                                   
REMARK 500    GLN B 268      -16.89    150.54                                   
REMARK 500    LEU B 269      -73.24   -120.17                                   
REMARK 500    ALA B 272       25.16    -68.15                                   
REMARK 500    LEU B 273      -16.91   -142.30                                   
REMARK 500    GLU B 277      121.92   -177.41                                   
REMARK 500    CYS B 278     -175.43   -175.20                                   
REMARK 500    CYS B 280     -158.62   -122.81                                   
REMARK 500    ALA B 284     -153.71    -51.42                                   
REMARK 500    GLN B 285     -126.85   -168.72                                   
REMARK 500    ALA B 286      -48.76   -146.28                                   
REMARK 500    PRO B 288       30.27    -68.24                                   
REMARK 500    CYS B 289        8.62    -64.49                                   
REMARK 500    SER B 290     -133.32   -106.17                                   
REMARK 500    VAL B 291      141.48    156.73                                   
REMARK 500    TRP B 306       86.12    164.45                                   
REMARK 500    GLU B 308      142.50    -28.98                                   
REMARK 500    VAL B 312     -175.05   -170.92                                   
REMARK 500    ARG B 317     -128.57   -114.37                                   
REMARK 500    GLU B 319      -85.58   -113.87                                   
REMARK 500    MET B 324       43.62    -90.54                                   
REMARK 500    LEU B 343      -78.17    -60.66                                   
REMARK 500    THR B 348       70.01    -64.88                                   
REMARK 500    ASP B 349      -17.64    156.08                                   
REMARK 500    ALA B 358       23.94     81.79                                   
REMARK 500    LEU B 359      152.63    -47.20                                   
REMARK 500    SER B 360     -148.36    -83.29                                   
REMARK 500    LEU B 361      155.66    160.24                                   
REMARK 500    VAL B 364       78.18   -102.02                                   
REMARK 500    ASP B 365      -61.39    -24.31                                   
REMARK 500    GLN B 366       11.86     88.00                                   
REMARK 500    VAL B 406       24.52    -64.25                                   
REMARK 500    ASP B 407       -1.44   -147.34                                   
REMARK 500    ASP B 414       47.29    177.26                                   
REMARK 500    LEU B 415      -74.33   -119.31                                   
REMARK 500    LEU B 417       13.67    -56.80                                   
REMARK 500    ALA B 421      157.54     99.00                                   
REMARK 500    ALA B 423      110.06    176.88                                   
REMARK 500    VAL B 426      168.72     71.00                                   
REMARK 500    GLN B 427       57.58   -153.68                                   
REMARK 500    SER B 428     -176.42    156.43                                   
REMARK 500    LYS B 430       76.02    -55.20                                   
REMARK 500    GLU B 431      -10.41   -147.77                                   
REMARK 500    LEU B 432       74.96    -52.51                                   
REMARK 500    ALA B 433      -33.10    145.01                                   
REMARK 500    ASP B 434       19.80    -69.69                                   
REMARK 500    PHE B 435        4.60   -175.40                                   
REMARK 500    THR B 440      -87.84     99.20                                   
REMARK 500    LYS B 441     -179.66    -68.85                                   
REMARK 500    ALA B 442     -105.83     94.77                                   
REMARK 500    VAL B 443       12.21    -68.76                                   
REMARK 500    ALA B 444       40.04    -69.96                                   
REMARK 500    GLU B 445     -124.89    161.31                                   
REMARK 500    ALA B 446      -46.27   -140.41                                   
REMARK 500    ARG B 452      -94.00   -137.74                                   
REMARK 500    THR B 456      -38.09    -39.93                                   
REMARK 500    SER B 458      -29.40     96.95                                   
REMARK 500    GLU B 462      -74.15   -166.25                                   
REMARK 500    LEU B 473      -80.40    -27.04                                   
REMARK 500    ALA B 474      164.09    -18.68                                   
REMARK 500    ALA B 479      -65.34    -19.38                                   
REMARK 500    TRP B 482       74.77    -39.76                                   
REMARK 500    ARG B 483      -67.83    150.12                                   
REMARK 500    ARG B 484      -15.99    -49.51                                   
REMARK 500    GLN B 487      -76.62    -47.55                                   
REMARK 500    GLN B 488       64.22    -62.08                                   
REMARK 500    ASN B 490     -114.96     64.13                                   
REMARK 500    ARG B 491       58.39    -41.73                                   
REMARK 500    LEU B 494      -23.15    -20.65                                   
REMARK 500    MET B 496      -73.30   -124.13                                   
REMARK 500    ALA B 497       18.36    -63.14                                   
REMARK 500    ALA B 503      -30.43   -174.95                                   
REMARK 500    PRO B 507      -76.72    -46.78                                   
REMARK 500    LEU B 509      -72.16    -63.93                                   
REMARK 500    PHE B 518      165.91    -29.03                                   
REMARK 500    SER B 519     -126.03    -24.73                                   
REMARK 500    LYS B 521       68.48   -107.22                                   
REMARK 500    GLU B 522      -39.82   -166.51                                   
REMARK 500    ASN B 525       69.15   -109.33                                   
REMARK 500    ASP B 529       66.40    -66.84                                   
REMARK 500    ILE B 530      156.79    175.90                                   
REMARK 500    VAL B 532      -51.50    103.28                                   
REMARK 500    SER B 542       29.80   -163.88                                   
REMARK 500    ARG B 543     -168.31     93.24                                   
REMARK 500    GLU B 548       12.44    -61.33                                   
REMARK 500    ARG B 552       13.17    -57.28                                   
REMARK 500    GLN B 556       -5.82     44.53                                   
REMARK 500    THR B 558      -69.60   -141.38                                   
REMARK 500    HIS B 563       29.20   -177.50                                   
REMARK 500    LEU B 566       55.81     16.09                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ARG A  268     VAL A  269                 -147.78                    
REMARK 500 ASP A  338     ASP A  339                 -100.39                    
REMARK 500 SER A  378     LEU A  379                 -141.50                    
REMARK 500 LEU A  379     PRO A  380                 -131.49                    
REMARK 500 ARG A  431     PRO A  432                   39.04                    
REMARK 500 LEU A  453     LEU A  454                 -136.86                    
REMARK 500 ALA B  272     LEU B  273                  145.53                    
REMARK 500 MET B  276     GLU B  277                  149.72                    
REMARK 500 CYS B  278     ARG B  279                  141.50                    
REMARK 500 THR B  351     ALA B  352                  143.14                    
REMARK 500 LYS B  430     GLU B  431                  148.53                    
REMARK 500 LYS B  450     LEU B  451                 -111.21                    
REMARK 500 LEU B  461     GLU B  462                  143.51                    
REMARK 500 SER B  463     ASP B  464                  144.57                    
REMARK 500 LEU B  560     GLN B  561                 -149.20                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2ZIU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2ZIV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2ZIW   RELATED DB: PDB                                   
DBREF  2ZIX A  246   551  UNP    Q96NY9   MUS81_HUMAN    246    551             
DBREF  2ZIX B  246   570  UNP    Q96AY2   EME1_HUMAN     246    570             
SEQADV 2ZIX MET A  245  UNP  Q96NY9              INITIATING METHIONINE          
SEQADV 2ZIX MET B  230  UNP  Q96AY2              EXPRESSION TAG                 
SEQADV 2ZIX GLY B  231  UNP  Q96AY2              EXPRESSION TAG                 
SEQADV 2ZIX SER B  232  UNP  Q96AY2              EXPRESSION TAG                 
SEQADV 2ZIX SER B  233  UNP  Q96AY2              EXPRESSION TAG                 
SEQADV 2ZIX HIS B  234  UNP  Q96AY2              EXPRESSION TAG                 
SEQADV 2ZIX HIS B  235  UNP  Q96AY2              EXPRESSION TAG                 
SEQADV 2ZIX HIS B  236  UNP  Q96AY2              EXPRESSION TAG                 
SEQADV 2ZIX HIS B  237  UNP  Q96AY2              EXPRESSION TAG                 
SEQADV 2ZIX HIS B  238  UNP  Q96AY2              EXPRESSION TAG                 
SEQADV 2ZIX HIS B  239  UNP  Q96AY2              EXPRESSION TAG                 
SEQADV 2ZIX SER B  240  UNP  Q96AY2              EXPRESSION TAG                 
SEQADV 2ZIX GLN B  241  UNP  Q96AY2              EXPRESSION TAG                 
SEQADV 2ZIX ASP B  242  UNP  Q96AY2              EXPRESSION TAG                 
SEQADV 2ZIX PRO B  243  UNP  Q96AY2              EXPRESSION TAG                 
SEQADV 2ZIX ASN B  244  UNP  Q96AY2              EXPRESSION TAG                 
SEQADV 2ZIX SER B  245  UNP  Q96AY2              EXPRESSION TAG                 
SEQRES   1 A  307  MET SER ALA GLU LEU ALA SER GLU ALA GLY VAL GLN GLN          
SEQRES   2 A  307  GLN PRO LEU GLU LEU ARG PRO GLY GLU TYR ARG VAL LEU          
SEQRES   3 A  307  LEU CYS VAL ASP ILE GLY GLU THR ARG GLY GLY GLY HIS          
SEQRES   4 A  307  ARG PRO GLU LEU LEU ARG GLU LEU GLN ARG LEU HIS VAL          
SEQRES   5 A  307  THR HIS THR VAL ARG LYS LEU HIS VAL GLY ASP PHE VAL          
SEQRES   6 A  307  TRP VAL ALA GLN GLU THR ASN PRO ARG ASP PRO ALA ASN          
SEQRES   7 A  307  PRO GLY GLU LEU VAL LEU ASP HIS ILE VAL GLU ARG LYS          
SEQRES   8 A  307  ARG LEU ASP ASP LEU CYS SER SER ILE ILE ASP GLY ARG          
SEQRES   9 A  307  PHE ARG GLU GLN LYS PHE ARG LEU LYS ARG CYS GLY LEU          
SEQRES  10 A  307  GLU ARG ARG VAL TYR LEU VAL GLU GLU HIS GLY SER VAL          
SEQRES  11 A  307  HIS ASN LEU SER LEU PRO GLU SER THR LEU LEU GLN ALA          
SEQRES  12 A  307  VAL THR ASN THR GLN VAL ILE ASP GLY PHE PHE VAL LYS          
SEQRES  13 A  307  ARG THR ALA ASP ILE LYS GLU SER ALA ALA TYR LEU ALA          
SEQRES  14 A  307  LEU LEU THR ARG GLY LEU GLN ARG LEU TYR GLN GLY HIS          
SEQRES  15 A  307  THR LEU ARG SER ARG PRO TRP GLY THR PRO GLY ASN PRO          
SEQRES  16 A  307  GLU SER GLY ALA MET THR SER PRO ASN PRO LEU CYS SER          
SEQRES  17 A  307  LEU LEU THR PHE SER ASP PHE ASN ALA GLY ALA ILE LYS          
SEQRES  18 A  307  ASN LYS ALA GLN SER VAL ARG GLU VAL PHE ALA ARG GLN          
SEQRES  19 A  307  LEU MET GLN VAL ARG GLY VAL SER GLY GLU LYS ALA ALA          
SEQRES  20 A  307  ALA LEU VAL ASP ARG TYR SER THR PRO ALA SER LEU LEU          
SEQRES  21 A  307  ALA ALA TYR ASP ALA CYS ALA THR PRO LYS GLU GLN GLU          
SEQRES  22 A  307  THR LEU LEU SER THR ILE LYS CYS GLY ARG LEU GLN ARG          
SEQRES  23 A  307  ASN LEU GLY PRO ALA LEU SER ARG THR LEU SER GLN LEU          
SEQRES  24 A  307  TYR CYS SER TYR GLY PRO LEU THR                              
SEQRES   1 B  341  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 B  341  PRO ASN SER GLU GLU CYS LEU LYS HIS ILE ILE VAL VAL          
SEQRES   3 B  341  LEU ASP PRO VAL LEU LEU GLN MET GLU GLY GLY GLY GLN          
SEQRES   4 B  341  LEU LEU GLY ALA LEU GLN THR MET GLU CYS ARG CYS VAL          
SEQRES   5 B  341  ILE GLU ALA GLN ALA VAL PRO CYS SER VAL THR TRP ARG          
SEQRES   6 B  341  ARG ARG ALA GLY PRO SER GLU ASP ARG GLU ASP TRP VAL          
SEQRES   7 B  341  GLU GLU PRO THR VAL LEU VAL LEU LEU ARG ALA GLU ALA          
SEQRES   8 B  341  PHE VAL SER MET ILE ASP ASN GLY LYS GLN GLY SER LEU          
SEQRES   9 B  341  ASP SER THR MET LYS GLY LYS GLU THR LEU GLN GLY PHE          
SEQRES  10 B  341  VAL THR ASP ILE THR ALA LYS THR ALA GLY LYS ALA LEU          
SEQRES  11 B  341  SER LEU VAL ILE VAL ASP GLN GLU LYS CYS PHE SER ALA          
SEQRES  12 B  341  GLN ASN PRO PRO ARG ARG GLY LYS GLN GLY ALA ASN LYS          
SEQRES  13 B  341  GLN THR LYS LYS GLN GLN GLN ARG GLN PRO GLU ALA SER          
SEQRES  14 B  341  ILE GLY SER MET VAL SER ARG VAL ASP ALA GLU GLU ALA          
SEQRES  15 B  341  LEU VAL ASP LEU GLN LEU HIS THR GLU ALA GLN ALA GLN          
SEQRES  16 B  341  ILE VAL GLN SER TRP LYS GLU LEU ALA ASP PHE THR CYS          
SEQRES  17 B  341  ALA PHE THR LYS ALA VAL ALA GLU ALA PRO PHE LYS LYS          
SEQRES  18 B  341  LEU ARG ASP GLU THR THR PHE SER PHE CYS LEU GLU SER          
SEQRES  19 B  341  ASP TRP ALA GLY GLY VAL LYS VAL ASP LEU ALA GLY ARG          
SEQRES  20 B  341  GLY LEU ALA LEU VAL TRP ARG ARG GLN ILE GLN GLN LEU          
SEQRES  21 B  341  ASN ARG VAL SER LEU GLU MET ALA SER ALA VAL VAL ASN          
SEQRES  22 B  341  ALA TYR PRO SER PRO GLN LEU LEU VAL GLN ALA TYR GLN          
SEQRES  23 B  341  GLN CYS PHE SER ASP LYS GLU ARG GLN ASN LEU LEU ALA          
SEQRES  24 B  341  ASP ILE GLN VAL ARG ARG GLY GLU GLY VAL THR SER THR          
SEQRES  25 B  341  SER ARG ARG ILE GLY PRO GLU LEU SER ARG ARG ILE TYR          
SEQRES  26 B  341  LEU GLN MET THR THR LEU GLN PRO HIS LEU SER LEU ASP          
SEQRES  27 B  341  SER ALA ASP                                                  
HELIX    1   1 LEU A  291  HIS A  295  5                                   5    
HELIX    2   2 LEU A  340  ILE A  345  1                                   6    
HELIX    3   3 GLY A  347  LYS A  353  1                                   7    
HELIX    4   4 PRO A  380  ILE A  394  1                                  15    
HELIX    5   5 ASP A  404  ALA A  409  1                                   6    
HELIX    6   6 ALA A  409  ARG A  417  1                                   9    
HELIX    7   7 ALA A  461  LYS A  465  5                                   5    
HELIX    8   8 GLU A  473  GLN A  478  1                                   6    
HELIX    9   9 THR A  499  ALA A  509  1                                  11    
HELIX   10  10 THR A  512  GLN A  516  5                                   5    
HELIX   11  11 GLY A  533  CYS A  545  1                                  13    
HELIX   12  12 GLU B  319  MET B  324  1                                   6    
HELIX   13  13 LEU B  480  GLN B  485  1                                   6    
HELIX   14  14 SER B  506  TYR B  514  1                                   9    
HELIX   15  15 SER B  550  LEU B  555  1                                   6    
SHEET    1   A 2 HIS A 330  VAL A 332  0                                        
SHEET    2   A 2 ARG A 363  VAL A 365  1  O  VAL A 365   N  ILE A 331           
SHEET    1   B 2 VAL B 254  LEU B 256  0                                        
SHEET    2   B 2 CYS B 280  ILE B 282  1  O  VAL B 281   N  LEU B 256           
SHEET    1   C 2 LEU B 315  ARG B 317  0                                        
SHEET    2   C 2 VAL B 362  VAL B 364  1  O  VAL B 364   N  LEU B 316           
CISPEP   1 ARG A  284    PRO A  285          0       -24.71                     
CISPEP   2 ALA A  491    ALA A  492          0       -19.98                     
CRYST1   85.814   85.814  176.409  90.00  90.00 120.00 P 31 2 1      6          
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      0.011653  0.006728  0.000000        0.00000                         
SCALE2      0.000000  0.013456  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005669        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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