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Database: PDB
Entry: 5ZCJ
LinkDB: 5ZCJ
Original site: 5ZCJ 
HEADER    PROTEIN BINDING                         17-FEB-18   5ZCJ              
TITLE     CRYSTAL STRUCTURE OF COMPLEX                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUDOR-INTERACTING REPAIR REGULATOR PROTEIN;                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: NUDT16-LIKE PROTEIN 1,PROTEIN SYNDESMOS;                    
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: TP53-BINDING PROTEIN 1;                                    
COMPND   8 CHAIN: C;                                                            
COMPND   9 SYNONYM: P53BP1;                                                     
COMPND  10 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: NUDT16L1, SDOS, TIRR;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: TP53BP1;                                                       
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    COMPLEX, PROTEIN BINDING                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.WANG,Z.YUAN,Y.CUI,R.XIE,M.WANG,Y.MA,X.YU,X.LIU                      
REVDAT   1   27-JUN-18 5ZCJ    0                                                
JRNL        AUTH   J.WANG,Z.YUAN,Y.CUI,R.XIE,M.WANG,Y.MA,X.YU,X.LIU             
JRNL        TITL   CRYSTAL STRUCTURE OF COMPLEX                                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (DEV_2932)                                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.92                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.150                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 45400                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.191                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.330                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1966                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 19.9178 -  4.8088    0.98     3161   143  0.2029 0.1914        
REMARK   3     2  4.8088 -  3.8258    0.99     3158   143  0.1530 0.1854        
REMARK   3     3  3.8258 -  3.3448    0.99     3178   144  0.1647 0.2067        
REMARK   3     4  3.3448 -  3.0401    0.98     3105   141  0.1725 0.2133        
REMARK   3     5  3.0401 -  2.8229    0.97     3098   142  0.1815 0.1961        
REMARK   3     6  2.8229 -  2.6568    0.98     3141   142  0.1903 0.2260        
REMARK   3     7  2.6568 -  2.5241    0.99     3132   143  0.1938 0.2466        
REMARK   3     8  2.5241 -  2.4144    0.99     3142   141  0.2010 0.2310        
REMARK   3     9  2.4144 -  2.3216    0.99     3130   143  0.2044 0.2293        
REMARK   3    10  2.3216 -  2.2416    0.98     3105   138  0.2020 0.2520        
REMARK   3    11  2.2416 -  2.1716    0.98     3110   141  0.2074 0.2537        
REMARK   3    12  2.1716 -  2.1096    0.95     3004   139  0.2270 0.2355        
REMARK   3    13  2.1096 -  2.0541    0.94     2953   133  0.2420 0.2844        
REMARK   3    14  2.0541 -  2.0040    0.95     3017   133  0.2549 0.2889        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.810           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           4221                                  
REMARK   3   ANGLE     :  0.509           5698                                  
REMARK   3   CHIRALITY :  0.038            624                                  
REMARK   3   PLANARITY :  0.003            732                                  
REMARK   3   DIHEDRAL  :  4.933           3278                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5ZCJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-FEB-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300006809.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-NOV-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 308418                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.920                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.9400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.7 M AMMONIUM TARTRATE, 0.1 M SODIUM    
REMARK 280  ACETATE PH 4.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       55.57200            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       51.96100            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       55.57200            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       51.96100            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLY A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     LYS A   205                                                      
REMARK 465     LEU A   206                                                      
REMARK 465     LEU A   207                                                      
REMARK 465     PRO A   208                                                      
REMARK 465     ALA A   209                                                      
REMARK 465     SER A   210                                                      
REMARK 465     SER A   211                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     GLY B     4                                                      
REMARK 465     SER B     5                                                      
REMARK 465     PRO B   208                                                      
REMARK 465     ALA B   209                                                      
REMARK 465     SER B   210                                                      
REMARK 465     SER B   211                                                      
REMARK 465     GLY C  1455                                                      
REMARK 465     PRO C  1456                                                      
REMARK 465     GLY C  1457                                                      
REMARK 465     SER C  1458                                                      
REMARK 465     ARG C  1459                                                      
REMARK 465     SER C  1460                                                      
REMARK 465     ASP C  1461                                                      
REMARK 465     SER C  1462                                                      
REMARK 465     PRO C  1463                                                      
REMARK 465     GLU C  1464                                                      
REMARK 465     ILE C  1465                                                      
REMARK 465     PRO C  1466                                                      
REMARK 465     PHE C  1467                                                      
REMARK 465     GLN C  1468                                                      
REMARK 465     ALA C  1469                                                      
REMARK 465     ALA C  1470                                                      
REMARK 465     ALA C  1471                                                      
REMARK 465     GLY C  1472                                                      
REMARK 465     PRO C  1473                                                      
REMARK 465     SER C  1474                                                      
REMARK 465     ASP C  1475                                                      
REMARK 465     GLY C  1476                                                      
REMARK 465     LEU C  1477                                                      
REMARK 465     ASP C  1478                                                      
REMARK 465     ALA C  1479                                                      
REMARK 465     SER C  1480                                                      
REMARK 465     SER C  1481                                                      
REMARK 465     PRO C  1482                                                      
REMARK 465     GLY C  1483                                                      
REMARK 465     ASN C  1484                                                      
REMARK 465     SER C  1485                                                      
REMARK 465     ALA C  1607                                                      
REMARK 465     VAL C  1608                                                      
REMARK 465     THR C  1609                                                      
REMARK 465     PRO C  1610                                                      
REMARK 465     LEU C  1611                                                      
REMARK 465     THR C  1612                                                      
REMARK 465     LYS C  1613                                                      
REMARK 465     ALA C  1614                                                      
REMARK 465     ALA C  1615                                                      
REMARK 465     ASP C  1616                                                      
REMARK 465     ILE C  1617                                                      
REMARK 465     SER C  1618                                                      
REMARK 465     LEU C  1619                                                      
REMARK 465     ASP C  1620                                                      
REMARK 465     ASN C  1621                                                      
REMARK 465     LEU C  1622                                                      
REMARK 465     VAL C  1623                                                      
REMARK 465     GLU C  1624                                                      
REMARK 465     GLY C  1625                                                      
REMARK 465     LYS C  1626                                                      
REMARK 465     ARG C  1627                                                      
REMARK 465     LYS C  1628                                                      
REMARK 465     ARG C  1629                                                      
REMARK 465     ARG C  1630                                                      
REMARK 465     SER C  1631                                                      
REMARK 465     ASN C  1632                                                      
REMARK 465     VAL C  1633                                                      
REMARK 465     SER C  1634                                                      
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   O    GLY A    83     NH2  ARG A   133              2.12            
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    PHE A  41       16.92     57.78                                   
REMARK 500    ARG A  47      -72.10     63.71                                   
REMARK 500    LEU A  89      132.06     70.86                                   
REMARK 500    LEU A 137      -87.61   -122.22                                   
REMARK 500    VAL A 154      -30.87   -131.30                                   
REMARK 500    ARG B  43      -40.69   -149.58                                   
REMARK 500    ARG B  47      -66.15     65.58                                   
REMARK 500    CYS B  88       24.86    -70.60                                   
REMARK 500    LEU B 137      -98.08   -117.61                                   
REMARK 500    VAL B 154      -30.40   -131.47                                   
REMARK 500    GLU C1551       17.60     86.76                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5ZCJ A    6   211  UNP    Q9BRJ7   TIRR_HUMAN       6    211             
DBREF  5ZCJ B    6   211  UNP    Q9BRJ7   TIRR_HUMAN       6    211             
DBREF  5ZCJ C 1459  1634  UNP    Q12888   TP53B_HUMAN   1459   1634             
SEQADV 5ZCJ GLY A    2  UNP  Q9BRJ7              EXPRESSION TAG                 
SEQADV 5ZCJ PRO A    3  UNP  Q9BRJ7              EXPRESSION TAG                 
SEQADV 5ZCJ GLY A    4  UNP  Q9BRJ7              EXPRESSION TAG                 
SEQADV 5ZCJ SER A    5  UNP  Q9BRJ7              EXPRESSION TAG                 
SEQADV 5ZCJ GLY B    2  UNP  Q9BRJ7              EXPRESSION TAG                 
SEQADV 5ZCJ PRO B    3  UNP  Q9BRJ7              EXPRESSION TAG                 
SEQADV 5ZCJ GLY B    4  UNP  Q9BRJ7              EXPRESSION TAG                 
SEQADV 5ZCJ SER B    5  UNP  Q9BRJ7              EXPRESSION TAG                 
SEQADV 5ZCJ GLY C 1455  UNP  Q12888              EXPRESSION TAG                 
SEQADV 5ZCJ PRO C 1456  UNP  Q12888              EXPRESSION TAG                 
SEQADV 5ZCJ GLY C 1457  UNP  Q12888              EXPRESSION TAG                 
SEQADV 5ZCJ SER C 1458  UNP  Q12888              EXPRESSION TAG                 
SEQRES   1 A  210  GLY PRO GLY SER VAL PRO GLU LEU LYS GLN ILE SER ARG          
SEQRES   2 A  210  VAL GLU ALA MET ARG LEU GLY PRO GLY TRP SER HIS SER          
SEQRES   3 A  210  CYS HIS ALA MET LEU TYR ALA ALA ASN PRO GLY GLN LEU          
SEQRES   4 A  210  PHE GLY ARG ILE PRO MET ARG PHE SER VAL LEU MET GLN          
SEQRES   5 A  210  MET ARG PHE ASP GLY LEU LEU GLY PHE PRO GLY GLY PHE          
SEQRES   6 A  210  VAL ASP ARG ARG PHE TRP SER LEU GLU ASP GLY LEU ASN          
SEQRES   7 A  210  ARG VAL LEU GLY LEU GLY LEU GLY CYS LEU ARG LEU THR          
SEQRES   8 A  210  GLU ALA ASP TYR LEU SER SER HIS LEU THR GLU GLY PRO          
SEQRES   9 A  210  HIS ARG VAL VAL ALA HIS LEU TYR ALA ARG GLN LEU THR          
SEQRES  10 A  210  LEU GLU GLN LEU HIS ALA VAL GLU ILE SER ALA VAL HIS          
SEQRES  11 A  210  SER ARG ASP HIS GLY LEU GLU VAL LEU GLY LEU VAL ARG          
SEQRES  12 A  210  VAL PRO LEU TYR THR GLN LYS ASP ARG VAL GLY GLY PHE          
SEQRES  13 A  210  PRO ASN PHE LEU SER ASN ALA PHE VAL SER THR ALA LYS          
SEQRES  14 A  210  CYS GLN LEU LEU PHE ALA LEU LYS VAL LEU ASN MET MET          
SEQRES  15 A  210  PRO GLU GLU LYS LEU VAL GLU ALA LEU ALA ALA ALA THR          
SEQRES  16 A  210  GLU LYS GLN LYS LYS ALA LEU GLU LYS LEU LEU PRO ALA          
SEQRES  17 A  210  SER SER                                                      
SEQRES   1 B  210  GLY PRO GLY SER VAL PRO GLU LEU LYS GLN ILE SER ARG          
SEQRES   2 B  210  VAL GLU ALA MET ARG LEU GLY PRO GLY TRP SER HIS SER          
SEQRES   3 B  210  CYS HIS ALA MET LEU TYR ALA ALA ASN PRO GLY GLN LEU          
SEQRES   4 B  210  PHE GLY ARG ILE PRO MET ARG PHE SER VAL LEU MET GLN          
SEQRES   5 B  210  MET ARG PHE ASP GLY LEU LEU GLY PHE PRO GLY GLY PHE          
SEQRES   6 B  210  VAL ASP ARG ARG PHE TRP SER LEU GLU ASP GLY LEU ASN          
SEQRES   7 B  210  ARG VAL LEU GLY LEU GLY LEU GLY CYS LEU ARG LEU THR          
SEQRES   8 B  210  GLU ALA ASP TYR LEU SER SER HIS LEU THR GLU GLY PRO          
SEQRES   9 B  210  HIS ARG VAL VAL ALA HIS LEU TYR ALA ARG GLN LEU THR          
SEQRES  10 B  210  LEU GLU GLN LEU HIS ALA VAL GLU ILE SER ALA VAL HIS          
SEQRES  11 B  210  SER ARG ASP HIS GLY LEU GLU VAL LEU GLY LEU VAL ARG          
SEQRES  12 B  210  VAL PRO LEU TYR THR GLN LYS ASP ARG VAL GLY GLY PHE          
SEQRES  13 B  210  PRO ASN PHE LEU SER ASN ALA PHE VAL SER THR ALA LYS          
SEQRES  14 B  210  CYS GLN LEU LEU PHE ALA LEU LYS VAL LEU ASN MET MET          
SEQRES  15 B  210  PRO GLU GLU LYS LEU VAL GLU ALA LEU ALA ALA ALA THR          
SEQRES  16 B  210  GLU LYS GLN LYS LYS ALA LEU GLU LYS LEU LEU PRO ALA          
SEQRES  17 B  210  SER SER                                                      
SEQRES   1 C  180  GLY PRO GLY SER ARG SER ASP SER PRO GLU ILE PRO PHE          
SEQRES   2 C  180  GLN ALA ALA ALA GLY PRO SER ASP GLY LEU ASP ALA SER          
SEQRES   3 C  180  SER PRO GLY ASN SER PHE VAL GLY LEU ARG VAL VAL ALA          
SEQRES   4 C  180  LYS TRP SER SER ASN GLY TYR PHE TYR SER GLY LYS ILE          
SEQRES   5 C  180  THR ARG ASP VAL GLY ALA GLY LYS TYR LYS LEU LEU PHE          
SEQRES   6 C  180  ASP ASP GLY TYR GLU CYS ASP VAL LEU GLY LYS ASP ILE          
SEQRES   7 C  180  LEU LEU CYS ASP PRO ILE PRO LEU ASP THR GLU VAL THR          
SEQRES   8 C  180  ALA LEU SER GLU ASP GLU TYR PHE SER ALA GLY VAL VAL          
SEQRES   9 C  180  LYS GLY HIS ARG LYS GLU SER GLY GLU LEU TYR TYR SER          
SEQRES  10 C  180  ILE GLU LYS GLU GLY GLN ARG LYS TRP TYR LYS ARG MET          
SEQRES  11 C  180  ALA VAL ILE LEU SER LEU GLU GLN GLY ASN ARG LEU ARG          
SEQRES  12 C  180  GLU GLN TYR GLY LEU GLY PRO TYR GLU ALA VAL THR PRO          
SEQRES  13 C  180  LEU THR LYS ALA ALA ASP ILE SER LEU ASP ASN LEU VAL          
SEQRES  14 C  180  GLU GLY LYS ARG LYS ARG ARG SER ASN VAL SER                  
FORMUL   4  HOH   *393(H2 O)                                                    
HELIX    1 AA1 SER A   13  MET A   18  1                                   6    
HELIX    2 AA2 PHE A   41  ARG A   43  5                                   3    
HELIX    3 AA3 SER A   73  LEU A   86  1                                  14    
HELIX    4 AA4 THR A   92  ALA A   94  5                                   3    
HELIX    5 AA5 THR A  118  VAL A  130  1                                  13    
HELIX    6 AA6 GLY A  156  SER A  162  1                                   7    
HELIX    7 AA7 VAL A  166  LEU A  180  1                                  15    
HELIX    8 AA8 PRO A  184  LEU A  203  1                                  20    
HELIX    9 AA9 SER B   13  MET B   18  1                                   6    
HELIX   10 AB1 PHE B   41  ARG B   43  5                                   3    
HELIX   11 AB2 SER B   73  LEU B   86  1                                  14    
HELIX   12 AB3 THR B   92  ALA B   94  5                                   3    
HELIX   13 AB4 THR B  118  HIS B  131  1                                  14    
HELIX   14 AB5 GLY B  156  SER B  162  1                                   7    
HELIX   15 AB6 VAL B  166  LEU B  180  1                                  15    
HELIX   16 AB7 PRO B  184  GLU B  204  1                                  21    
HELIX   17 AB8 SER C 1589  ARG C 1595  1                                   7    
HELIX   18 AB9 LEU C 1596  GLY C 1601  1                                   6    
SHEET    1 AA1 6 LYS A  10  GLN A  11  0                                        
SHEET    2 AA1 6 TYR A  96  LEU A 101 -1  O  LEU A 101   N  LYS A  10           
SHEET    3 AA1 6 VAL A 108  LEU A 117 -1  O  ALA A 110   N  HIS A 100           
SHEET    4 AA1 6 SER A  25  LEU A  40  1  N  MET A  31   O  TYR A 113           
SHEET    5 AA1 6 ILE A  44  ARG A  55 -1  O  ARG A  47   N  ASN A  36           
SHEET    6 AA1 6 GLY A  64  VAL A  67  0                                        
SHEET    1 AA2 4 LEU A  60  GLY A  61  0                                        
SHEET    2 AA2 4 ILE A  44  ARG A  55 -1  N  GLN A  53   O  GLY A  61           
SHEET    3 AA2 4 SER A  25  LEU A  40 -1  N  ASN A  36   O  ARG A  47           
SHEET    4 AA2 4 VAL A 139  VAL A 145  0                                        
SHEET    1 AA3 6 LYS B  10  GLN B  11  0                                        
SHEET    2 AA3 6 TYR B  96  LEU B 101 -1  O  LEU B 101   N  LYS B  10           
SHEET    3 AA3 6 VAL B 108  LEU B 117 -1  O  ALA B 110   N  HIS B 100           
SHEET    4 AA3 6 SER B  25  LEU B  40  1  N  SER B  27   O  HIS B 111           
SHEET    5 AA3 6 ILE B  44  ARG B  55 -1  O  ILE B  44   N  LEU B  40           
SHEET    6 AA3 6 GLY B  64  VAL B  67  0                                        
SHEET    1 AA4 4 LEU B  60  GLY B  61  0                                        
SHEET    2 AA4 4 ILE B  44  ARG B  55 -1  N  GLN B  53   O  GLY B  61           
SHEET    3 AA4 4 SER B  25  LEU B  40 -1  N  LEU B  40   O  ILE B  44           
SHEET    4 AA4 4 VAL B 139  ARG B 144  0                                        
SHEET    1 AA5 5 GLU C1524  LEU C1528  0                                        
SHEET    2 AA5 5 LYS C1514  PHE C1519 -1  N  TYR C1515   O  VAL C1527           
SHEET    3 AA5 5 TYR C1502  GLY C1511 -1  N  THR C1507   O  LYS C1516           
SHEET    4 AA5 5 ARG C1490  ALA C1493 -1  N  ALA C1493   O  TYR C1502           
SHEET    5 AA5 5 ILE C1532  LEU C1533 -1  O  LEU C1533   N  VAL C1492           
SHEET    1 AA6 5 GLN C1577  LYS C1582  0                                        
SHEET    2 AA6 5 GLU C1567  LYS C1574 -1  N  TYR C1570   O  TYR C1581           
SHEET    3 AA6 5 PHE C1553  GLU C1564 -1  N  LYS C1559   O  SER C1571           
SHEET    4 AA6 5 GLU C1543  LEU C1547 -1  N  ALA C1546   O  SER C1554           
SHEET    5 AA6 5 VAL C1586  ILE C1587 -1  O  ILE C1587   N  THR C1545           
CISPEP   1 GLY A  104    PRO A  105          0         4.11                     
CISPEP   2 GLY B  104    PRO B  105          0        -3.10                     
CISPEP   3 LEU B  206    LEU B  207          0         1.78                     
CISPEP   4 ASP C 1536    PRO C 1537          0        -1.87                     
CISPEP   5 GLY C 1603    PRO C 1604          0         2.98                     
CRYST1  111.144  103.922   61.470  90.00  95.46  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008997  0.000000  0.000860        0.00000                         
SCALE2      0.000000  0.009623  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016342        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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