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