GenomeNet

Database: PDB
Entry: 1W0T
LinkDB: 1W0T
Original site: 1W0T 
HEADER    DNA-BINDING PROTEIN                     11-JUN-04   1W0T              
TITLE     HTRF1 DNA-BINDING DOMAIN IN COMPLEX WITH TELOMERIC DNA.               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TELOMERIC REPEAT BINDING FACTOR 1;                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: DNA-BINDING DOMAIN, RESIDUES 379-431;                      
COMPND   5 SYNONYM: TTAGGG REPEAT-BINDING FACTOR 1, NIMA- INTERACTING           
COMPND   6  PROTEIN 2, TELOMERIC PROTEIN PIN2/TRF1;                             
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: 5'-D(*CP*TP*GP*TP*TP*AP*GP*GP*GP*TP                        
COMPND  10  *TP*AP*GP*GP*GP*TP*TP*AP*G)-3';                                     
COMPND  11 CHAIN: C;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: 5'-D(*TP*CP*TP*AP*AP*CP*CP*CP*TP*AP                        
COMPND  15  *AP*CP*CP*CP*TP*AP*AP*CP*A)-3';                                     
COMPND  16 CHAIN: D;                                                            
COMPND  17 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: ROSETTA;                                   
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PET13A;                                   
SOURCE   9 OTHER_DETAILS: SYNTHETIC GENE;                                       
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 MOL_ID: 3;                                                           
SOURCE  13 SYNTHETIC: YES                                                       
KEYWDS    TELOMERE, DNA-BINDING PROTEIN, HOMEODOMAIN, MITOSIS, CELL             
KEYWDS   2 CYCLE, NUCLEAR PROTEIN, CHROMOSOMAL PROTEIN,                         
KEYWDS   3 PHOSPHORYLATION, ADP-RIBOSYLATION                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.I.COURT,L.M.CHAPMAN,L.FAIRALL,D.RHODES                              
REVDAT   4   09-JUN-09 1W0T    1       REMARK ATOM                              
REVDAT   3   24-FEB-09 1W0T    1       VERSN                                    
REVDAT   2   11-JAN-05 1W0T    1       JRNL                                     
REVDAT   1   22-DEC-04 1W0T    0                                                
JRNL        AUTH   R.I.COURT,L.M.CHAPMAN,L.FAIRALL,D.RHODES                     
JRNL        TITL   HOW THE HUMAN TELOMERIC PROTEINS TRF1 AND TRF2               
JRNL        TITL 2 RECOGNIZE TELOMERIC DNA: A VIEW FROM                         
JRNL        TITL 3 HIGH-RESOLUTION CRYSTAL STRUCTURES                           
JRNL        REF    EMBO REP.                     V.   6    39 2005              
JRNL        REFN                   ISSN 1469-3178                               
JRNL        PMID   15608617                                                     
JRNL        DOI    10.1038/SJ.EMBOR.7400314                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
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) : 23.62                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1187150.11                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.000000                       
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 22407                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.252                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.9                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2226                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.13                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.9                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3355                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.262                        
REMARK   3   BIN FREE R VALUE                    : 0.292                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.8                          
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 364                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.015                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 916                                     
REMARK   3   NUCLEIC ACID ATOMS       : 771                                     
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 72                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.8                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.8                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 13.67                                                
REMARK   3    B22 (A**2) : -4.76                                                
REMARK   3    B33 (A**2) : -8.92                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.28                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.17                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.31                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.24                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.1                             
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 18.4                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.22                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 4.40  ; 1.50                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 6.73  ; 2.00                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.68  ; 2.00                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.72  ; 2.50                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.384795                                             
REMARK   3   BSOL        : 67.3951                                              
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1W0T COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-JUN-04.                  
REMARK 100 THE PDBE ID CODE IS EBI-15368.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-NOV-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 5                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22407                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 23.620                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : 0.06400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.2000                             
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) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.20600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: SOLVE, AUTOSHARP                                      
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 62.34                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLISED IN              
REMARK 280  50 MM MES, PH 6.0, 0.1 M KCL, 2 MM MGCL2 AND 10 %                   
REMARK 280  PEG 400 AND CRYOPROTECTED IN 20 % GLYCEROL                          
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       19.22150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.35300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.18000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.35300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       19.22150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.18000            
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 GENERATING THE BIOMOLECULE                                           
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D, B                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  BINDS THE TELOMERIC DOUBLE-STRANDED TTAGGG REPEAT AND               
REMARK 400  NEGATIVELY REGULATES TELOMERE LENGTH.                               
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     LYS A   431                                                      
REMARK 465     LYS B   431                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER;                                
REMARK 480 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 480 I=INSERTION CODE):                                                   
REMARK 480   M RES CSSEQI  ATOMS                                                
REMARK 480     LYS A 379    CG   CD   CE   NZ                                   
REMARK 480     GLN A 381    CG   CD  OE1  NE2                                   
REMARK 480     LEU A 384    CB   CG  CD1  CD2                                   
REMARK 480     GLU A 386    CB   CG   CD  OE1  OE2                              
REMARK 480     LYS A 397    CD   CE   NZ                                        
REMARK 480     LYS A 405    CG   CD   CE   NZ                                   
REMARK 480     LYS A 411    CB   CG   CD   CE   NZ                              
REMARK 480     ASN A 413    CB   CG  OD1  ND2                                   
REMARK 480     LYS A 429    CB   CG   CD   CE   NZ                              
REMARK 480     LYS B 379    CG   CD   CE   NZ                                   
REMARK 480     GLN B 381    CD  OE1  NE2                                        
REMARK 480     LEU B 384    CB   CG  CD1  CD2                                   
REMARK 480     GLU B 386    CB   CG   CD  OE1  OE2                              
REMARK 480     LYS B 389    CD   CE   NZ                                        
REMARK 480     LYS B 411    CG   CD   CE   NZ                                   
REMARK 480     ASN B 413    CG  OD1  ND2                                        
REMARK 480     ASN B 414    CG  OD1  ND2                                        
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     DA C  12   O4' -  C1' -  N9  ANGL. DEV. =  -2.7 DEGREES          
REMARK 500     DC D  13   O3' -  P   -  OP1 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500     DC D  13   O3' -  P   -  OP2 ANGL. DEV. =  -6.7 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 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    ASN A 402       54.34    -99.39                                   
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     DG C   3         0.06    SIDE CHAIN                              
REMARK 500     DA C  12         0.05    SIDE CHAIN                              
REMARK 500     DA C  18         0.06    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1BA5   RELATED DB: PDB                                   
REMARK 900  DNA-BINDING DOMAIN OF HUMAN TELOMERIC                               
REMARK 900  PROTEIN, HTRF1,NMR, 18 STRUCTURES                                   
REMARK 900 RELATED ID: 1H6O   RELATED DB: PDB                                   
REMARK 900  DIMERISATION DOMAIN FROM HUMAN TRF1                                 
REMARK 900 RELATED ID: 1ITY   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE DNA BINDING DOMAIN                        
REMARK 900   OF HUMAN TRF1                                                      
REMARK 900 RELATED ID: 1IV6   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF THE DNA COMPLEX OF                            
REMARK 900  HUMAN TRF1                                                          
REMARK 900 RELATED ID: 1W0U   RELATED DB: PDB                                   
REMARK 900  HTRF2 DNA-BINDING DOMAIN IN COMPLEX WITH                            
REMARK 900  TELOMERIC DNA                                                       
DBREF  1W0T A  379   431  UNP    P54274   TRF1_HUMAN     379    431             
DBREF  1W0T B  379   431  UNP    P54274   TRF1_HUMAN     379    431             
DBREF  1W0T C    1    19  PDB    1W0T     1W0T             1     19             
DBREF  1W0T D    1    19  PDB    1W0T     1W0T             1     19             
SEQRES   1 C   19   DC  DT  DG  DT  DT  DA  DG  DG  DG  DT  DT  DA  DG          
SEQRES   2 C   19   DG  DG  DT  DT  DA  DG                                      
SEQRES   1 D   19   DT  DC  DT  DA  DA  DC  DC  DC  DT  DA  DA  DC  DC          
SEQRES   2 D   19   DC  DT  DA  DA  DC  DA                                      
SEQRES   1 A   53  LYS ARG GLN ALA TRP LEU TRP GLU GLU ASP LYS ASN LEU          
SEQRES   2 A   53  ARG SER GLY VAL ARG LYS TYR GLY GLU GLY ASN TRP SER          
SEQRES   3 A   53  LYS ILE LEU LEU HIS TYR LYS PHE ASN ASN ARG THR SER          
SEQRES   4 A   53  VAL MET LEU LYS ASP ARG TRP ARG THR MET LYS LYS LEU          
SEQRES   5 A   53  LYS                                                          
SEQRES   1 B   53  LYS ARG GLN ALA TRP LEU TRP GLU GLU ASP LYS ASN LEU          
SEQRES   2 B   53  ARG SER GLY VAL ARG LYS TYR GLY GLU GLY ASN TRP SER          
SEQRES   3 B   53  LYS ILE LEU LEU HIS TYR LYS PHE ASN ASN ARG THR SER          
SEQRES   4 B   53  VAL MET LEU LYS ASP ARG TRP ARG THR MET LYS LYS LEU          
SEQRES   5 B   53  LYS                                                          
FORMUL   5  HOH   *72(H2 O1)                                                    
HELIX    1   1 LEU A  384  GLY A  399  1                                  16    
HELIX    2   2 ASN A  402  TYR A  410  1                                   9    
HELIX    3   3 THR A  416  LYS A  429  1                                  14    
HELIX    4   4 LEU B  384  GLY B  399  1                                  16    
HELIX    5   5 ASN B  402  TYR B  410  1                                   9    
HELIX    6   6 THR B  416  LYS B  429  1                                  14    
CRYST1   38.443   72.360  116.706  90.00  90.00  90.00 P 21 21 21    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      0.026012  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013820  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008568        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system