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Database: PDB
Entry: 1R8U
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HEADER    TRANSCRIPTION/TRANSCRIPTION ACTIVATOR   28-OCT-03   1R8U              
TITLE     NMR STRUCTURE OF CBP TAZ1/CITED2 COMPLEX                              
CAVEAT     1R8U    CHIRALITY ERROR AT CYS379B MODEL 13                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CBP/P300-INTERACTING TRANSACTIVATOR 2;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CITED2 CAD (RESIDUES 200-269);                             
COMPND   5 SYNONYM: MSG-RELATED PROTEIN 1, MRG1 PROTEIN, P35SRJ,                
COMPND   6 CITED2;                                                              
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CREB-BINDING PROTEIN;                                      
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: CBP TAZ1 (RESIDUES 334-433);                               
COMPND  12 SYNONYM: CBP;                                                        
COMPND  13 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: CITED2, MRG1;                                                  
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: PET;                                      
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  13 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  14 ORGANISM_TAXID: 10090;                                               
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PET                                       
KEYWDS    ZINC-BINDING MOTIFS, PROTEIN-PROTEIN COMPLEX, TAZ ZINC                
KEYWDS   2 FINGER, TRANSCRIPTION/TRANSCRIPTION ACTIVATOR COMPLEX                
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    R.N.DE GUZMAN,M.MARTINEZ-YAMOUT,H.J.DYSON,P.E.WRIGHT                  
REVDAT   2   24-FEB-09 1R8U    1       VERSN                                    
REVDAT   1   23-MAR-04 1R8U    0                                                
JRNL        AUTH   R.N.DE GUZMAN,M.A.MARTINEZ-YAMOUT,H.J.DYSON,                 
JRNL        AUTH 2 P.E.WRIGHT                                                   
JRNL        TITL   INTERACTION OF THE TAZ1 DOMAIN OF THE CREB-BINDING           
JRNL        TITL 2 PROTEIN WITH THE ACTIVATION DOMAIN OF CITED2:                
JRNL        TITL 3 REGULATION BY COMPETITION BETWEEN INTRINSICALLY              
JRNL        TITL 4 UNSTRUCTURED LIGANDS FOR NON-IDENTICAL BINDING               
JRNL        TITL 5 SITES.                                                       
JRNL        REF    J.BIOL.CHEM.                  V. 279  3042 2004              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   14594809                                                     
JRNL        DOI    10.1074/JBC.M310348200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : AMBER 7.0                                            
REMARK   3   AUTHORS     : DAVID CASE ET AL.                                    
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1R8U COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-NOV-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB020580.                                      
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 298; 298; 298; 298                 
REMARK 210  PH                             : 6.8; 6.8; 6.8; 6.8                 
REMARK 210  IONIC STRENGTH                 : 16 MM; 16 MM; 16 MM; 16 MM         
REMARK 210  PRESSURE                       : 1 ATM; 1 ATM; 1 ATM; 1 ATM         
REMARK 210  SAMPLE CONTENTS                : 0.5MM N15 TAZ1, UNLABELED          
REMARK 210                                   CITED2, 90% H2O, 10% D2O;          
REMARK 210                                   0.5MM UNLABELED TAZ1, N15          
REMARK 210                                   CITED2, 90% H2O, 10% D2O;          
REMARK 210                                   0.5MM C13,N15 TAZ1, UNLABELED      
REMARK 210                                   CITED2, 90% H2O, 10% D2O;          
REMARK 210                                   0.5MM UNLABELED TAZ1, CITED2,      
REMARK 210                                   90% H2O,10% D2O                    
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 3D_15N-SEPARATED_NOESY, 3D_        
REMARK 210                                   13C-SEPARATED_NOESY, 3D_13C-       
REMARK 210                                   SEPARATED_ROESY                    
REMARK 210  SPECTROMETER FIELD STRENGTH    : 800 MHZ, 900 MHZ, 600 MHZ          
REMARK 210  SPECTROMETER MODEL             : AVANCE, DRX                        
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : NMRPIPE 2003, NMRDRAW 4.1.3.,      
REMARK 210                                   DYANA 1.5                          
REMARK 210   METHOD USED                   : AMBER SIMULATED ANNEALING AND      
REMARK 210                                   MINIMIZATION                       
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 50                                 
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH ACCEPTABLE         
REMARK 210                                   COVALENT GEOMETRY                  
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
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  1 ARG B 369   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500  1 ARG B 385   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500  1 ARG B 439   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500  2 ARG A 239   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500  2 ARG A 267   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500  2 ARG B 377   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500  4 ARG B 377   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500  4 ARG B 439   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500  5 ARG B 439   NE  -  CZ  -  NH1 ANGL. DEV. =   4.1 DEGREES          
REMARK 500  6 ARG B 369   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500  6 ARG B 439   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500  7 ARG A 239   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500  7 ARG B 350   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500  7 ARG B 369   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500  8 ARG A 239   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500  8 ARG B 439   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500  9 ARG B 369   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500  9 ARG B 439   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500 10 ARG B 377   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500 10 ARG B 439   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500 11 ARG B 350   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500 11 ARG B 377   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500 11 ARG B 412   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500 12 ARG A 239   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500 13 ARG A 239   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500 15 ARG B 368   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500 15 ARG B 369   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500 15 ARG B 439   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500 16 ARG B 439   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500 17 ARG A 239   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500 17 ARG B 368   NE  -  CZ  -  NH1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500 17 ARG B 369   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500 17 ARG B 385   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500 18 ARG B 368   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500 18 ARG B 369   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500 18 ARG B 439   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500 19 ARG B 350   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500 19 ARG B 369   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500 20 ARG B 368   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 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  1 LYS A 241      -41.39   -142.55                                   
REMARK 500  1 PHE A 255      -19.70    -37.76                                   
REMARK 500  1 THR A 257     -174.11    -68.66                                   
REMARK 500  1 PHE A 259       39.36    -70.79                                   
REMARK 500  1 PRO B 347     -166.97   -100.16                                   
REMARK 500  1 ASN B 373      -28.22   -145.88                                   
REMARK 500  2 PHE A 255      -49.36    -20.54                                   
REMARK 500  2 ASP A 258       21.12   -146.30                                   
REMARK 500  2 ARG A 267       -4.37    -58.55                                   
REMARK 500  2 ALA B 345       58.72   -144.46                                   
REMARK 500  2 ASN B 373      -18.86    -47.03                                   
REMARK 500  2 GLU B 375       15.73   -144.09                                   
REMARK 500  2 ALA B 378     -150.79   -120.48                                   
REMARK 500  2 CYS B 421     -177.15    -69.01                                   
REMARK 500  3 PHE A 253       74.90   -150.93                                   
REMARK 500  3 PHE A 255      -41.81    -28.22                                   
REMARK 500  3 PRO A 265      170.13    -55.46                                   
REMARK 500  3 THR B 344        3.48    -65.31                                   
REMARK 500  3 ASN B 373      -30.19   -142.64                                   
REMARK 500  3 GLU B 375       20.02   -151.54                                   
REMARK 500  3 THR B 422       -8.03   -140.42                                   
REMARK 500  4 LYS A 241      -45.42   -133.65                                   
REMARK 500  4 PHE A 255      -23.15    -35.18                                   
REMARK 500  4 THR B 344      -44.83   -153.23                                   
REMARK 500  4 ASN B 373      -33.54   -147.58                                   
REMARK 500  4 GLU B 375      -39.60   -148.73                                   
REMARK 500  4 VAL B 376       55.95     32.01                                   
REMARK 500  4 ASP B 437       10.88    -61.08                                   
REMARK 500  5 LYS A 241      -41.42   -134.43                                   
REMARK 500  5 PHE A 255      -23.36    -35.32                                   
REMARK 500  5 ARG A 267        8.39    -64.48                                   
REMARK 500  5 ASN B 373      -18.57   -148.06                                   
REMARK 500  5 GLU B 375       15.32   -143.81                                   
REMARK 500  5 SER B 380       11.82   -140.60                                   
REMARK 500  6 LYS A 241      -44.36   -132.68                                   
REMARK 500  6 PHE A 255      -25.19    -39.68                                   
REMARK 500  6 PRO B 347     -167.94   -100.15                                   
REMARK 500  6 ASN B 373      -30.09   -148.60                                   
REMARK 500  6 GLU B 375       25.15   -150.64                                   
REMARK 500  6 GLN B 398       12.94   -146.09                                   
REMARK 500  6 ASP B 425       38.51    -72.01                                   
REMARK 500  7 PHE A 255      -35.93    -23.35                                   
REMARK 500  7 ASP A 258       -4.50   -144.79                                   
REMARK 500  7 PHE A 259       39.52    -78.07                                   
REMARK 500  7 SER A 266      -40.06   -138.80                                   
REMARK 500  7 ASN B 373      -29.29   -143.69                                   
REMARK 500  7 GLU B 375       20.27   -149.83                                   
REMARK 500  7 VAL B 376       92.29    -63.95                                   
REMARK 500  7 THR B 422      -14.23   -140.50                                   
REMARK 500  8 PHE A 255      -28.00    -35.10                                   
REMARK 500  8 THR A 257      -79.50      0.17                                   
REMARK 500  8 LYS A 262      105.57    -54.93                                   
REMARK 500  8 ASN B 373      -31.66   -150.36                                   
REMARK 500  8 ALA B 378      -30.53   -156.37                                   
REMARK 500  8 SER B 380      -37.37   -146.02                                   
REMARK 500  9 THR A 257       83.67     13.11                                   
REMARK 500  9 ASP A 258       78.76   -151.94                                   
REMARK 500  9 LYS A 262      -31.33   -136.94                                   
REMARK 500  9 VAL A 268      -43.80   -132.17                                   
REMARK 500  9 THR B 344       86.91      0.27                                   
REMARK 500  9 ASN B 373      -15.01   -142.74                                   
REMARK 500  9 THR B 422       -2.54   -142.70                                   
REMARK 500  9 ARG B 423       22.29   -145.77                                   
REMARK 500 10 LYS A 241      -40.44   -135.34                                   
REMARK 500 10 PHE A 255      -25.63    -38.38                                   
REMARK 500 10 SER A 266      -29.16   -153.96                                   
REMARK 500 10 THR B 344      106.91    -54.35                                   
REMARK 500 10 ALA B 345      121.99    -39.87                                   
REMARK 500 10 ASN B 373      -34.84   -151.77                                   
REMARK 500 10 GLU B 375       20.32   -146.36                                   
REMARK 500 10 ALA B 378      -12.67   -153.26                                   
REMARK 500 10 THR B 422       -3.67   -140.16                                   
REMARK 500 11 LYS A 241      -37.81   -134.71                                   
REMARK 500 11 THR A 257      128.36    -35.35                                   
REMARK 500 11 ARG A 267       25.33   -151.66                                   
REMARK 500 11 THR B 344      -43.38   -148.97                                   
REMARK 500 11 ASN B 373       56.07     27.14                                   
REMARK 500 11 GLU B 375       11.32   -141.81                                   
REMARK 500 11 VAL B 376       64.40    -66.88                                   
REMARK 500 11 CYS B 379      107.94    -55.88                                   
REMARK 500 11 GLN B 398       13.99   -148.00                                   
REMARK 500 11 CYS B 403      109.91    -59.84                                   
REMARK 500 12 ILE A 223      153.47    -46.94                                   
REMARK 500 12 LYS A 241      -44.89   -139.49                                   
REMARK 500 12 PHE A 255      -30.47    -38.08                                   
REMARK 500 12 ASP A 258       30.84    -82.35                                   
REMARK 500 12 SER A 266      -50.19   -150.80                                   
REMARK 500 12 GLU B 375      -14.10   -140.07                                   
REMARK 500 12 GLN B 398       11.08   -140.46                                   
REMARK 500 12 LYS B 438       44.92    -76.78                                   
REMARK 500 13 LYS A 241      -42.87   -141.58                                   
REMARK 500 13 PHE A 255      -32.26    -35.65                                   
REMARK 500 13 GLN A 263      -29.65   -151.05                                   
REMARK 500 13 GLU B 375       14.82   -148.44                                   
REMARK 500 13 ALA B 378        1.89    -68.44                                   
REMARK 500 13 CYS B 379      153.84    -47.01                                   
REMARK 500 13 SER B 380        9.25   -153.16                                   
REMARK 500 13 GLN B 398       12.73   -150.11                                   
REMARK 500 14 PHE A 222     -167.67   -127.83                                   
REMARK 500 14 PHE A 255      -17.95    -37.58                                   
REMARK 500 14 PRO B 343       31.78    -76.04                                   
REMARK 500 14 THR B 344      108.55    -53.62                                   
REMARK 500 14 PRO B 347     -158.87    -99.66                                   
REMARK 500 14 ASN B 373      -33.47   -151.06                                   
REMARK 500 14 GLU B 375       14.14   -150.51                                   
REMARK 500 14 LEU B 381      109.27    -59.54                                   
REMARK 500 15 LYS A 241      -42.97   -136.35                                   
REMARK 500 15 PHE A 253       77.79   -151.48                                   
REMARK 500 15 THR A 257      -64.93     -1.71                                   
REMARK 500 15 ASP A 258       30.84   -142.85                                   
REMARK 500 15 CYS A 261       19.58    -55.80                                   
REMARK 500 15 SER A 266      -24.51   -157.55                                   
REMARK 500 15 THR B 344      -45.98   -164.44                                   
REMARK 500 15 ASN B 373       33.08     33.98                                   
REMARK 500 15 GLU B 375      -29.30   -160.62                                   
REMARK 500 15 SER B 380       14.72   -140.60                                   
REMARK 500 16 THR A 257      114.21    -15.45                                   
REMARK 500 16 THR B 344      -42.18   -133.61                                   
REMARK 500 16 ASN B 373      -15.05   -141.56                                   
REMARK 500 16 ALA B 378       22.82    -70.28                                   
REMARK 500 16 ASP B 425       18.18     47.68                                   
REMARK 500 17 ASP A 221      -45.65   -150.90                                   
REMARK 500 17 PHE A 253       73.78   -151.69                                   
REMARK 500 17 PHE A 255      -51.92    -19.76                                   
REMARK 500 17 THR B 344       27.17   -144.58                                   
REMARK 500 17 ASN B 373       -5.18   -147.13                                   
REMARK 500 17 GLU B 375       -1.98   -147.26                                   
REMARK 500 17 ALA B 378      109.90    -59.94                                   
REMARK 500 17 ARG B 423       68.16     20.84                                   
REMARK 500 17 ASP B 425       12.28   -154.24                                   
REMARK 500 18 LYS A 241      -43.22   -133.51                                   
REMARK 500 18 PHE A 255      -38.61    -24.78                                   
REMARK 500 18 THR A 257      170.36    -58.75                                   
REMARK 500 18 THR B 344      -28.10   -146.18                                   
REMARK 500 18 ASN B 373      -19.56    -47.53                                   
REMARK 500 18 GLU B 375      -20.89   -140.57                                   
REMARK 500 19 THR A 257       93.10      7.17                                   
REMARK 500 19 PHE A 259       98.27    -69.19                                   
REMARK 500 19 THR B 344       -2.48   -145.08                                   
REMARK 500 19 ASN B 373      -13.81   -144.70                                   
REMARK 500 19 THR B 422       37.00     34.38                                   
REMARK 500 19 ASP B 425       -3.78   -147.72                                   
REMARK 500 20 GLU A 242       98.90      0.52                                   
REMARK 500 20 PHE A 255      -33.65    -30.48                                   
REMARK 500 20 LYS A 262       44.60    -75.45                                   
REMARK 500 20 SER A 266      -47.31   -157.62                                   
REMARK 500 20 ALA B 345       55.31     38.20                                   
REMARK 500 20 PRO B 347     -157.78   -101.63                                   
REMARK 500 20 ASN B 373      -47.66   -133.79                                   
REMARK 500 20 SER B 380       20.29   -141.31                                   
REMARK 500 20 LYS B 438       49.10    -76.71                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500  1 ARG B 350         0.08    SIDE_CHAIN                              
REMARK 500  1 HIS B 417         0.13    SIDE_CHAIN                              
REMARK 500  2 HIS B 417         0.11    SIDE_CHAIN                              
REMARK 500  3 HIS B 417         0.10    SIDE_CHAIN                              
REMARK 500  4 ARG B 369         0.09    SIDE_CHAIN                              
REMARK 500  4 HIS B 417         0.10    SIDE_CHAIN                              
REMARK 500  5 HIS B 417         0.11    SIDE_CHAIN                              
REMARK 500  6 ARG B 412         0.08    SIDE_CHAIN                              
REMARK 500  6 HIS B 417         0.11    SIDE_CHAIN                              
REMARK 500  7 HIS B 417         0.10    SIDE_CHAIN                              
REMARK 500  8 HIS B 417         0.10    SIDE_CHAIN                              
REMARK 500  9 HIS B 417         0.11    SIDE_CHAIN                              
REMARK 500 10 HIS B 417         0.10    SIDE_CHAIN                              
REMARK 500 12 HIS B 417         0.11    SIDE_CHAIN                              
REMARK 500 13 HIS B 362         0.08    SIDE_CHAIN                              
REMARK 500 13 HIS B 417         0.12    SIDE_CHAIN                              
REMARK 500 15 HIS B 417         0.10    SIDE_CHAIN                              
REMARK 500 17 HIS B 417         0.11    SIDE_CHAIN                              
REMARK 500 18 HIS B 417         0.11    SIDE_CHAIN                              
REMARK 500 19 HIS B 417         0.11    SIDE_CHAIN                              
REMARK 500 20 HIS B 417         0.12    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 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: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500   M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                
REMARK 500  13 CYS B 379       131.2                     ALPHA-CARBON           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                           1  ZN B 440  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 366   SG                                                     
REMARK 620 2 CYS B 379   SG  107.4                                              
REMARK 620 3 CYS B 384   SG  111.5 110.0                                        
REMARK 620 4 HIS B 362   NE2 109.6 107.5 110.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                           1  ZN B 441  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 403   SG                                                     
REMARK 620 2 CYS B 408   SG  111.8                                              
REMARK 620 3 HIS B 393   NE2 109.4 110.5                                        
REMARK 620 4 CYS B 397   SG  106.9 110.2 107.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                           1  ZN B 442  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 421   SG                                                     
REMARK 620 2 CYS B 429   SG  105.7                                              
REMARK 620 3 CYS B 426   SG  112.9 111.7                                        
REMARK 620 4 HIS B 417   NE2 108.8 111.6 106.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 440                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 441                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 442                  
DBREF  1R8U A  220   269  UNP    Q99967   CIT2_HUMAN     220    269             
DBREF  1R8U B  340   439  GB     19547885 AAL87531       334    433             
SEQRES   1 A   50  THR ASP PHE ILE ASP GLU GLU VAL LEU MET SER LEU VAL          
SEQRES   2 A   50  ILE GLU MET GLY LEU ASP ARG ILE LYS GLU LEU PRO GLU          
SEQRES   3 A   50  LEU TRP LEU GLY GLN ASN GLU PHE ASP PHE MET THR ASP          
SEQRES   4 A   50  PHE VAL CYS LYS GLN GLN PRO SER ARG VAL SER                  
SEQRES   1 B  100  ALA THR GLY PRO THR ALA ASP PRO GLU LYS ARG LYS LEU          
SEQRES   2 B  100  ILE GLN GLN GLN LEU VAL LEU LEU LEU HIS ALA HIS LYS          
SEQRES   3 B  100  CYS GLN ARG ARG GLU GLN ALA ASN GLY GLU VAL ARG ALA          
SEQRES   4 B  100  CYS SER LEU PRO HIS CYS ARG THR MET LYS ASN VAL LEU          
SEQRES   5 B  100  ASN HIS MET THR HIS CYS GLN ALA GLY LYS ALA CYS GLN          
SEQRES   6 B  100  VAL ALA HIS CYS ALA SER SER ARG GLN ILE ILE SER HIS          
SEQRES   7 B  100  TRP LYS ASN CYS THR ARG HIS ASP CYS PRO VAL CYS LEU          
SEQRES   8 B  100  PRO LEU LYS ASN ALA SER ASP LYS ARG                          
HET     ZN  B 440       1                                                       
HET     ZN  B 441       1                                                       
HET     ZN  B 442       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   3   ZN    3(ZN 2+)                                                     
HELIX    1   1 ASP A  224  GLY A  236  1                                  13    
HELIX    2   2 LEU A  237  ILE A  240  5                                   4    
HELIX    3   3 GLN A  250  ASP A  254  5                                   5    
HELIX    4   4 PRO A  265  SER A  269  5                                   5    
HELIX    5   5 PRO B  347  ALA B  372  1                                  26    
HELIX    6   6 HIS B  383  THR B  395  1                                  13    
HELIX    7   7 VAL B  405  THR B  422  1                                  18    
HELIX    8   8 VAL B  428  SER B  436  1                                   9    
HELIX    9   9 ASP B  437  ARG B  439  5                                   3    
LINK        ZN    ZN B 440                 SG  CYS B 366     1555   1555  2.30  
LINK        ZN    ZN B 440                 SG  CYS B 379     1555   1555  2.29  
LINK        ZN    ZN B 440                 SG  CYS B 384     1555   1555  2.30  
LINK        ZN    ZN B 440                 NE2 HIS B 362     1555   1555  2.09  
LINK        ZN    ZN B 441                 SG  CYS B 403     1555   1555  2.29  
LINK        ZN    ZN B 441                 SG  CYS B 408     1555   1555  2.30  
LINK        ZN    ZN B 441                 NE2 HIS B 393     1555   1555  2.09  
LINK        ZN    ZN B 441                 SG  CYS B 397     1555   1555  2.29  
LINK        ZN    ZN B 442                 SG  CYS B 421     1555   1555  2.30  
LINK        ZN    ZN B 442                 SG  CYS B 429     1555   1555  2.30  
LINK        ZN    ZN B 442                 SG  CYS B 426     1555   1555  2.28  
LINK        ZN    ZN B 442                 NE2 HIS B 417     1555   1555  2.07  
SITE     1 AC1  4 HIS B 362  CYS B 366  CYS B 379  CYS B 384                    
SITE     1 AC2  4 HIS B 393  CYS B 397  CYS B 403  CYS B 408                    
SITE     1 AC3  4 HIS B 417  CYS B 421  CYS B 426  CYS B 429                    
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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