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Database: PDB
Entry: 1TOT
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HEADER    TRANSFERASE                             15-JUN-04   1TOT              
TITLE     ZZ DOMAIN OF CBP- A NOVEL FOLD FOR A PROTEIN INTERACTION              
TITLE    2 MODULE                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CREB-BINDING PROTEIN;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: ZZ DOMAIN OF MURINE CBP (RESIDUES 1700-1751);              
COMPND   5 EC: 2.3.1.48;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: CREBBP, CBP;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) [DNAY];                          
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21A                                    
KEYWDS    ZINC BINDING, CBP, TAZ2, TRANSFERASE                                  
EXPDTA    SOLUTION NMR                                                          
NUMMDL    20                                                                    
AUTHOR    G.B.LEGGE,M.A.MARTINEZ-YAMOUT,D.M.HAMBLY,T.TRINH,H.J.DYSON,           
AUTHOR   2 P.E.WRIGHT                                                           
REVDAT   2   24-FEB-09 1TOT    1       VERSN                                    
REVDAT   1   18-JAN-05 1TOT    0                                                
JRNL        AUTH   G.B.LEGGE,M.A.MARTINEZ-YAMOUT,D.M.HAMBLY,T.TRINH,            
JRNL        AUTH 2 B.M.LEE,H.J.DYSON,P.E.WRIGHT                                 
JRNL        TITL   ZZ DOMAIN OF CBP: AN UNUSUAL ZINC FINGER FOLD IN A           
JRNL        TITL 2 PROTEIN INTERACTION MODULE                                   
JRNL        REF    J.MOL.BIOL.                   V. 343  1081 2004              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   15476823                                                     
JRNL        DOI    10.1016/J.JMB.2004.08.087                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : AMBER 8.0                                            
REMARK   3   AUTHORS     : CASE                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THE CALCULATED STRUCTURES ARE BASED       
REMARK   3  ON A TOTAL OF 1846 NOES, AND INCLUDE DUPLICATE NOES. 441            
REMARK   3  INTRARESIDUE, 328 SEQUENTIAL, 157 MEDIUM RANGE, 386 LONG            
REMARK   3  RANGE, 534 AMBIGOUS, 5 DEFINED HYDROGEN BONDS FROM H/D              
REMARK   3  EXCHANGE AND 29 PHI AND 29 PSI CONSTRAINTS AND 22 CHI1              
REMARK   3  CONSTRAINTS.                                                        
REMARK   4                                                                      
REMARK   4 1TOT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-JUL-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB022801.                                      
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 298                                
REMARK 210  PH                             : 6.8                                
REMARK 210  IONIC STRENGTH                 : 10 MM                              
REMARK 210  PRESSURE                       : AMBIENT                            
REMARK 210  SAMPLE CONTENTS                : 2.3 MM SOLUTIONS IN DEGASSED       
REMARK 210                                   10 MM TRIS-D11 PH 6.8, 200 M       
REMARK 210                                   ZNCL2, 10 MM DTT-D10, 0.05% W/     
REMARK 210                                   V SODIUM AZIDE, 94 % H2O, 6 %      
REMARK 210                                   D2O                                
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : 3D_13C-SEPARATED_NOESY, 3D_        
REMARK 210                                   15N-SEPARATED_NOESY,               
REMARK 210                                   HBHA(CCCO)NH TOSCY, CCONH          
REMARK 210                                   TOCSY, HCCH TOSCSY, HCCH COSY,     
REMARK 210                                   HNCO, HN(CA)CO, CBCACONH,          
REMARK 210                                   HNCACB                             
REMARK 210  SPECTROMETER FIELD STRENGTH    : 600 MHZ, 500 MHZ                   
REMARK 210  SPECTROMETER MODEL             : DRX, AMX                           
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : DYANA 1.0, SANE 1.0, AMBER         
REMARK 210                                   8.0, NMRPIPE 1.0, NMRVIEW 5.04     
REMARK 210   METHOD USED                   : TORSION ANGLE DYNAMICS AND         
REMARK 210                                   SIMULATED ANNEALING                
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 100                                
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 20                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LOWEST         
REMARK 210                                   ENERGY                             
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 3D              
REMARK 210  HOMONUCLEAR TECHNIQUES, AND BY CD113 NMR OF A CADMIUM               
REMARK 210  SUBSTITUTED SAMPLE TO CONFIRM METAL COORDINATING LIGANDS AND        
REMARK 210  COORDINATING ATOMS.                                                 
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  7 TYR A   7   CB  -  CG  -  CD2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500  8 ARG A  19   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500  8 ARG A  19   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500 10 ARG A  19   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500 17 ARG A  19   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500 19 ARG A  19   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 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 PHE A   5       10.79   -147.01                                   
REMARK 500  1 VAL A  24      -65.32   -101.27                                   
REMARK 500  1 THR A  37      -45.70   -130.93                                   
REMARK 500  2 ASN A  10        0.44    -67.80                                   
REMARK 500  2 VAL A  24      -63.66   -103.42                                   
REMARK 500  3 PHE A   5       16.30   -147.16                                   
REMARK 500  3 ASN A  10        0.57    -66.92                                   
REMARK 500  3 VAL A  24      -61.30   -103.26                                   
REMARK 500  3 LYS A  38        0.49    -68.63                                   
REMARK 500  3 SER A  39       47.39     39.44                                   
REMARK 500  3 LEU A  49        8.61     84.11                                   
REMARK 500  4 PHE A   5       23.13   -154.17                                   
REMARK 500  4 ASN A  10        1.19    -67.22                                   
REMARK 500  5 PHE A   5       25.95   -159.95                                   
REMARK 500  6 ASN A  10        0.48    -68.69                                   
REMARK 500  6 VAL A  24      -60.14   -104.50                                   
REMARK 500  7 PHE A   5       17.96   -151.47                                   
REMARK 500  7 VAL A  24      -62.02   -102.41                                   
REMARK 500  7 SER A  39       46.02     33.98                                   
REMARK 500  7 LEU A  51       54.07   -148.98                                   
REMARK 500  8 PHE A   5       25.64   -162.29                                   
REMARK 500  8 VAL A  24      -62.09   -101.04                                   
REMARK 500  8 THR A  37      -52.53   -128.04                                   
REMARK 500  8 LYS A  43       97.86    -68.38                                   
REMARK 500  8 LEU A  49       -1.21     76.84                                   
REMARK 500  8 LEU A  51       34.66   -145.63                                   
REMARK 500  9 PHE A   5       13.27   -152.27                                   
REMARK 500  9 ASN A  10        1.27    -66.46                                   
REMARK 500  9 VAL A  24      -65.38   -120.17                                   
REMARK 500 10 ASP A   3     -133.79   -137.33                                   
REMARK 500 11 ASN A  10        0.51    -68.23                                   
REMARK 500 11 VAL A  24      -61.09   -102.63                                   
REMARK 500 11 SER A  39       52.42     31.61                                   
REMARK 500 11 LEU A  49       -6.12   -144.91                                   
REMARK 500 12 PHE A   5       21.94   -149.72                                   
REMARK 500 12 LYS A  38        0.94    -68.39                                   
REMARK 500 12 SER A  39       47.64     35.91                                   
REMARK 500 13 PHE A   5       12.20   -154.27                                   
REMARK 500 13 ASN A  10        0.88    -67.69                                   
REMARK 500 13 LYS A  13       18.53     59.75                                   
REMARK 500 13 THR A  37      -53.48   -128.62                                   
REMARK 500 13 THR A  41       25.66    -66.83                                   
REMARK 500 13 LEU A  49       -1.59   -151.84                                   
REMARK 500 14 VAL A  24      -60.23   -107.84                                   
REMARK 500 14 ASP A  27       38.10     38.96                                   
REMARK 500 14 LEU A  49      -16.86   -140.12                                   
REMARK 500 14 LEU A  51       74.36   -119.59                                   
REMARK 500 15 PHE A   5       10.64   -147.80                                   
REMARK 500 15 ASN A  10        0.22    -68.70                                   
REMARK 500 15 VAL A  24      -61.88    -99.75                                   
REMARK 500 15 THR A  37      -49.36   -132.05                                   
REMARK 500 15 HIS A  40       86.89    -69.19                                   
REMARK 500 15 THR A  41       11.12    -64.50                                   
REMARK 500 15 LEU A  49      -19.30   -145.28                                   
REMARK 500 16 PHE A   5       17.54   -148.25                                   
REMARK 500 17 SER A  39       48.97     31.69                                   
REMARK 500 17 LEU A  51       -3.50   -141.14                                   
REMARK 500 18 ASP A   3     -158.65   -141.82                                   
REMARK 500 18 PHE A   5       16.93   -145.44                                   
REMARK 500 18 VAL A  24      -61.49    -90.36                                   
REMARK 500 18 THR A  37      -47.62   -130.75                                   
REMARK 500 18 THR A  41       23.83    -63.06                                   
REMARK 500 19 PHE A   5       14.84   -151.90                                   
REMARK 500 19 ASN A  10        0.98    -65.34                                   
REMARK 500 19 ASP A  27       39.94     37.14                                   
REMARK 500 19 LEU A  49      -22.11   -145.43                                   
REMARK 500 20 PHE A   5       19.65   -156.75                                   
REMARK 500 20 ASN A  10        4.99    -69.96                                   
REMARK 500 20 VAL A  24      -64.57    -99.80                                   
REMARK 500 20 SER A  39       40.93     34.08                                   
REMARK 500 20 HIS A  40       95.44    -64.02                                   
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 A   4         0.08    SIDE_CHAIN                              
REMARK 500  4 TYR A   7         0.13    SIDE_CHAIN                              
REMARK 500  4 ARG A  19         0.12    SIDE_CHAIN                              
REMARK 500  5 TYR A   7         0.11    SIDE_CHAIN                              
REMARK 500  5 ARG A  19         0.08    SIDE_CHAIN                              
REMARK 500  6 ARG A  19         0.10    SIDE_CHAIN                              
REMARK 500  7 TYR A   7         0.15    SIDE_CHAIN                              
REMARK 500  7 ARG A  19         0.10    SIDE_CHAIN                              
REMARK 500  9 ARG A   4         0.08    SIDE_CHAIN                              
REMARK 500  9 TYR A   7         0.10    SIDE_CHAIN                              
REMARK 500  9 ARG A  19         0.10    SIDE_CHAIN                              
REMARK 500 11 TYR A   7         0.10    SIDE_CHAIN                              
REMARK 500 11 ARG A  19         0.09    SIDE_CHAIN                              
REMARK 500 12 TYR A   7         0.10    SIDE_CHAIN                              
REMARK 500 13 HIS A  14         0.08    SIDE_CHAIN                              
REMARK 500 15 ARG A  19         0.08    SIDE_CHAIN                              
REMARK 500 16 ARG A  19         0.09    SIDE_CHAIN                              
REMARK 500 19 TYR A   7         0.08    SIDE_CHAIN                              
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 A  53  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  40   NE2                                                    
REMARK 620 2 CYS A  25   SG  121.0                                              
REMARK 620 3 CYS A  22   SG  104.7 107.3                                        
REMARK 620 4 HIS A  42   ND1 101.5 111.1 111.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                           1  ZN A  54  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A  12   SG                                                     
REMARK 620 2 CYS A   9   SG  103.6                                              
REMARK 620 3 CYS A  31   SG  117.2 105.9                                        
REMARK 620 4 CYS A  34   SG  114.4 112.3 103.5                                  
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 A 53                   
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 54                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1F81   RELATED DB: PDB                                   
REMARK 900 NEIGHBORING DOMAIN IN MURINE CBP                                     
DBREF  1TOT A    1    52  UNP    P45481   CBP_MOUSE     1700   1751             
SEQRES   1 A   52  GLY GLN ASP ARG PHE VAL TYR THR CYS ASN GLU CYS LYS          
SEQRES   2 A   52  HIS HIS VAL GLU THR ARG TRP HIS CYS THR VAL CYS GLU          
SEQRES   3 A   52  ASP TYR ASP LEU CYS ILE ASN CYS TYR ASN THR LYS SER          
SEQRES   4 A   52  HIS THR HIS LYS MET VAL LYS TRP GLY LEU GLY LEU ASP          
HET     ZN  A  53       1                                                       
HET     ZN  A  54       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   2   ZN    2(ZN 2+)                                                     
HELIX    1   1 CYS A   31  SER A   39  1                                   9    
SHEET    1   A 2 TYR A   7  THR A   8  0                                        
SHEET    2   A 2 HIS A  15  VAL A  16 -1  O  VAL A  16   N  TYR A   7           
SHEET    1   B 3 ASP A  29  LEU A  30  0                                        
SHEET    2   B 3 ARG A  19  CYS A  22 -1  N  TRP A  20   O  LEU A  30           
SHEET    3   B 3 MET A  44  TRP A  47 -1  O  TRP A  47   N  ARG A  19           
LINK        ZN    ZN A  53                 NE2 HIS A  40     1555   1555  2.09  
LINK        ZN    ZN A  54                 SG  CYS A  12     1555   1555  2.30  
LINK        ZN    ZN A  53                 SG  CYS A  25     1555   1555  2.32  
LINK        ZN    ZN A  53                 SG  CYS A  22     1555   1555  2.30  
LINK        ZN    ZN A  53                 ND1 HIS A  42     1555   1555  2.10  
LINK        ZN    ZN A  54                 SG  CYS A   9     1555   1555  2.27  
LINK        ZN    ZN A  54                 SG  CYS A  31     1555   1555  2.29  
LINK        ZN    ZN A  54                 SG  CYS A  34     1555   1555  2.30  
SITE     1 AC1  5 CYS A  22  VAL A  24  CYS A  25  HIS A  40                    
SITE     2 AC1  5 HIS A  42                                                     
SITE     1 AC2  4 CYS A   9  CYS A  12  CYS A  31  CYS A  34                    
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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