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Database: PDB
Entry: 1I27
LinkDB: 1I27
Original site: 1I27 
HEADER    TRANSCRIPTION                           07-FEB-01   1I27              
TITLE     CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF THE RAP74 SUBUNIT OF    
TITLE    2 HUMAN TRANSCRIPTION FACTOR IIF (TFIIF)                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSCRIPTION FACTOR IIF;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RAP74 SUBUNIT, C-TERMINAL DOMAIN;                          
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: RAP74;                                                         
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: PGEX-6P-1                                 
KEYWDS    GENERAL TRANSCRIPTION FACTOR, RAP74, RAP30, TFIIF, RNA POLYMERASE II, 
KEYWDS   2 WINGED-HELIX DOMAIN, TRANSCRIPTION                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.KAMADA,J.DE ANGELIS,R.G.ROEDER,S.K.BURLEY                           
REVDAT   3   03-FEB-21 1I27    1       AUTHOR JRNL   REMARK SEQADV              
REVDAT   3 2                   1       LINK                                     
REVDAT   2   24-FEB-09 1I27    1       VERSN                                    
REVDAT   1   07-MAR-01 1I27    0                                                
JRNL        AUTH   K.KAMADA,J.DE ANGELIS,R.G.ROEDER,S.K.BURLEY                  
JRNL        TITL   CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF THE RAP74      
JRNL        TITL 2 SUBUNIT OF HUMAN TRANSCRIPTION FACTOR IIF.                   
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  98  3115 2001              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   11248041                                                     
JRNL        DOI    10.1073/PNAS.051631098                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.02 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.02                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   CROSS-VALIDATION METHOD           : NULL                           
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.127                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.126                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.146                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 2927                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 58608                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.115                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.115                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.134                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.020                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 2437                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 48549                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 585                                           
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 1                                             
REMARK   3   SOLVENT ATOMS      : 151                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : NULL                    
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : NULL                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL                    
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : NULL                    
REMARK   3   NUMBER OF RESTRAINTS                     : NULL                    
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.007                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.025                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : NULL                    
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.317                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.068                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.071                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.010                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : NULL                    
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : NULL                    
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : NULL                    
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER                        
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1I27 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-FEB-01.                  
REMARK 100 THE DEPOSITION ID IS D_1000012810.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-JUL-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 200.0                              
REMARK 200  PH                             : 6.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97000                            
REMARK 200  MONOCHROMATOR                  : ROSENBAUM-ROCK MONOCHROMATOR       
REMARK 200  OPTICS                         : VERTICAL FOCUSING MIRROR           
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : SBC-2                              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58701                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.020                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 12.30                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : 0.05900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.02                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.54                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.33500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 31.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: ZINC SULFATE, LITHIUM CHLORIDE, PEG      
REMARK 280  2000 MME, POLYVINYLPYRROLIDONE 15K, GLUCOSAMINE HYDROCHLORIDE,      
REMARK 280  PH 6.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 282K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       14.52600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       24.08050            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       21.51200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       24.08050            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       14.52600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       21.51200            
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 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    GLN A 495   CA  -  CB  -  CG  ANGL. DEV. =  15.2 DEGREES          
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                              ZN A 999  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 503   OE1                                                    
REMARK 620 2 GLU A 503   OE2  54.9                                              
REMARK 620 3 HIS A 512   NE2  86.1 123.9                                        
REMARK 620 4 GLU A 517   O   166.7 119.1 105.9                                  
REMARK 620 5 GLU A 517   OXT 130.3  86.6  93.0  56.0                            
REMARK 620 6 HOH A1001   O    77.5 102.9 105.9  93.7 148.1                      
REMARK 620 N                    1     2     3     4     5                       
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 999                  
DBREF  1I27 A  449   517  UNP    P35269   T2FA_HUMAN     449    517             
SEQADV 1I27 GLY A  445  UNP  P35269              CLONING ARTIFACT               
SEQADV 1I27 PRO A  446  UNP  P35269              CLONING ARTIFACT               
SEQADV 1I27 LEU A  447  UNP  P35269              CLONING ARTIFACT               
SEQADV 1I27 GLY A  448  UNP  P35269              CLONING ARTIFACT               
SEQRES   1 A   73  GLY PRO LEU GLY SER GLY ASP VAL GLN VAL THR GLU ASP          
SEQRES   2 A   73  ALA VAL ARG ARG TYR LEU THR ARG LYS PRO MET THR THR          
SEQRES   3 A   73  LYS ASP LEU LEU LYS LYS PHE GLN THR LYS LYS THR GLY          
SEQRES   4 A   73  LEU SER SER GLU GLN THR VAL ASN VAL LEU ALA GLN ILE          
SEQRES   5 A   73  LEU LYS ARG LEU ASN PRO GLU ARG LYS MET ILE ASN ASP          
SEQRES   6 A   73  LYS MET HIS PHE SER LEU LYS GLU                              
HET     ZN  A 999       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  HOH   *151(H2 O)                                                    
HELIX    1   1 GLY A  445  SER A  449  5                                   5    
HELIX    2   2 THR A  455  LYS A  466  1                                  12    
HELIX    3   3 THR A  469  LYS A  476  1                                   8    
HELIX    4   4 GLN A  478  GLY A  483  1                                   6    
HELIX    5   5 SER A  485  ASN A  501  1                                  17    
SHEET    1   A 2 GLU A 503  ILE A 507  0                                        
SHEET    2   A 2 LYS A 510  SER A 514 -1  O  LYS A 510   N  ILE A 507           
LINK         OE1 GLU A 503                ZN    ZN A 999     4466   1555  2.61  
LINK         OE2 GLU A 503                ZN    ZN A 999     4466   1555  1.97  
LINK         NE2 HIS A 512                ZN    ZN A 999     1555   1555  2.01  
LINK         O   GLU A 517                ZN    ZN A 999     4466   1555  2.09  
LINK         OXT GLU A 517                ZN    ZN A 999     4466   1555  2.43  
LINK        ZN    ZN A 999                 O   HOH A1001     1555   1555  2.02  
SITE     1 AC1  4 GLU A 503  HIS A 512  GLU A 517  HOH A1001                    
CRYST1   29.052   43.024   48.161  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.034421  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.023243  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020764        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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