Header list of 1vfc.pdb file
Complete list - r 2 2 Bytes
HEADER STRUCTURAL PROTEIN/DNA 12-APR-04 1VFC TITLE SOLUTION STRUCTURE OF THE DNA COMPLEX OF HUMAN TRF2 COMPND MOL_ID: 1; COMPND 2 MOLECULE: SHORT G-RICH STRAND; COMPND 3 CHAIN: B; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: SHORT C-RICH STARND; COMPND 7 CHAIN: C; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: TELOMERIC REPEAT BINDING FACTOR 2; COMPND 11 CHAIN: A; COMPND 12 FRAGMENT: DNA BINDING DOMAIN; COMPND 13 SYNONYM: TRF2, TTAGGG REPEAT BINDING FACTOR 2, TELOMERIC DNA BINDING COMPND 14 PROTEIN; COMPND 15 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.; SOURCE 4 MOL_ID: 2; SOURCE 5 SYNTHETIC: YES; SOURCE 6 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS.; SOURCE 7 MOL_ID: 3; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_COMMON: HUMAN; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 13 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PET23B KEYWDS MYB, HELIX-TURN-HELIX, TELOMERE, PROTEIN-DNA COMPLEX, STRUCTURAL KEYWDS 2 PROTEIN-DNA COMPLEX EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR Y.NISHIMURA,S.HANAOKA REVDAT 3 02-MAR-22 1VFC 1 REMARK REVDAT 2 24-FEB-09 1VFC 1 VERSN REVDAT 1 17-MAY-05 1VFC 0 JRNL AUTH S.HANAOKA,A.NAGADOI,Y.NISHIMURA JRNL TITL COMPARISON BETWEEN TRF2 AND TRF1 OF THEIR TELOMERIC JRNL TITL 2 DNA-BOUND STRUCTURES AND DNA-BINDING ACTIVITIES JRNL REF PROTEIN SCI. V. 14 119 2005 JRNL REFN ISSN 0961-8368 JRNL PMID 15608118 JRNL DOI 10.1110/PS.04983705 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 2.0, CNS 1.0 REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), REMARK 3 BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI, REMARK 3 NILGES, PANNU,READ,RICE,SIMONSON,WARREN (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF REMARK 3 1450 RESTRAINTS, 1412 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 38 REMARK 3 DIHEDRAL ANGLE RESTRAINTS. REMARK 4 REMARK 4 1VFC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-APR-04. REMARK 100 THE DEPOSITION ID IS D_1000006555. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 6.9 REMARK 210 IONIC STRENGTH : 0.005M REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 1.0-1.5MM TRF2 LABELED WITH 15N REMARK 210 AND 13C, AND DNA; 5MM POTASSIUM REMARK 210 PHOSPHATE BUFFER, 90% H2O, 10% REMARK 210 D2O; 1.0-1.5MM TRF2 LABELED WITH REMARK 210 15N,AND DNA; 5MM POTASSIUM REMARK 210 PHOSPHATE BUFFER, 90% H2O, 10% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D 13C REMARK 210 -EDITED(F1), 13C-FILTERED(F3) REMARK 210 NOESY; 3D 15N-EDITED(F2), 15N/ REMARK 210 13C-FILTERED(F3) NOESY; 3D_13C- REMARK 210 SEPARATED_TOCSY; 3D_13C- REMARK 210 SEPARATED_COSY; 3D_15N-SEPARATED_ REMARK 210 NOESY; HNHA REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : DMX; AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : SPARKY 3.98, CNS 1.0 REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 200 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 : NULL REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY. 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 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, 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: 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 ASP A 439 108.77 59.82 REMARK 500 1 THR A 441 -77.32 -141.38 REMARK 500 1 ASN A 443 109.90 62.68 REMARK 500 1 THR A 445 83.22 -158.26 REMARK 500 1 ASN A 469 69.92 -102.65 REMARK 500 1 VAL A 480 -69.39 -122.89 REMARK 500 1 ASN A 481 56.54 -118.98 REMARK 500 2 ASP A 439 30.44 -150.02 REMARK 500 2 THR A 441 -51.18 -161.49 REMARK 500 2 ASN A 443 144.39 62.81 REMARK 500 2 LYS A 446 -142.60 -115.71 REMARK 500 3 SER A 440 177.37 63.11 REMARK 500 3 THR A 441 -78.00 -171.10 REMARK 500 3 THR A 445 32.01 -143.15 REMARK 500 3 ASN A 469 71.66 -102.95 REMARK 500 3 VAL A 480 -69.40 -127.64 REMARK 500 3 ASN A 481 57.04 -113.58 REMARK 500 4 ASP A 439 30.98 -141.08 REMARK 500 4 THR A 441 -66.32 -152.28 REMARK 500 4 ASN A 443 153.70 61.37 REMARK 500 4 THR A 445 84.68 62.56 REMARK 500 4 LYS A 446 -78.85 -78.73 REMARK 500 4 LYS A 447 -48.24 -134.72 REMARK 500 4 GLN A 448 42.07 -160.53 REMARK 500 4 ASN A 469 68.68 -100.54 REMARK 500 4 PRO A 478 48.80 -75.09 REMARK 500 4 ASN A 481 53.98 -100.13 REMARK 500 5 THR A 441 -72.50 -156.83 REMARK 500 5 ASN A 443 177.40 58.90 REMARK 500 5 THR A 445 88.85 -157.38 REMARK 500 5 LYS A 446 -111.18 -97.90 REMARK 500 5 ASN A 469 72.45 -103.35 REMARK 500 6 SER A 440 138.31 64.18 REMARK 500 6 THR A 441 -64.75 -142.86 REMARK 500 6 ASN A 443 114.31 60.67 REMARK 500 6 ILE A 444 112.77 -160.08 REMARK 500 6 LYS A 447 102.33 -164.81 REMARK 500 7 SER A 440 130.73 63.76 REMARK 500 7 THR A 441 -73.85 -127.50 REMARK 500 7 ASN A 443 157.15 63.30 REMARK 500 7 THR A 445 86.69 53.88 REMARK 500 7 TRP A 450 175.61 48.65 REMARK 500 7 ASN A 469 69.92 -102.72 REMARK 500 8 THR A 441 -50.47 -162.23 REMARK 500 8 ASN A 443 80.64 69.51 REMARK 500 8 ILE A 444 95.21 40.24 REMARK 500 8 THR A 445 151.70 61.84 REMARK 500 8 LYS A 446 33.25 -166.37 REMARK 500 8 TRP A 450 174.93 48.20 REMARK 500 8 ASN A 469 73.46 -102.81 REMARK 500 REMARK 500 THIS ENTRY HAS 129 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1VF9 RELATED DB: PDB REMARK 900 HUMAN TRF2 DBREF 1VFC A 438 500 UNP Q15554 TERF2_HUMAN 438 500 DBREF 1VFC B 1 13 PDB 1VFC 1VFC 1 13 DBREF 1VFC C 14 26 PDB 1VFC 1VFC 14 26 SEQRES 1 B 13 DG DT DT DA DG DG DG DT DT DA DG DG DG SEQRES 1 C 13 DC DC DC DT DA DA DC DC DC DT DA DA DC SEQRES 1 A 63 GLU ASP SER THR THR ASN ILE THR LYS LYS GLN LYS TRP SEQRES 2 A 63 THR VAL GLU GLU SER GLU TRP VAL LYS ALA GLY VAL GLN SEQRES 3 A 63 LYS TYR GLY GLU GLY ASN TRP ALA ALA ILE SER LYS ASN SEQRES 4 A 63 TYR PRO PHE VAL ASN ARG THR ALA VAL MET ILE LYS ASP SEQRES 5 A 63 ARG TRP ARG THR MET LYS ARG LEU GLY MET ASN HELIX 1 1 THR A 451 TYR A 465 1 15 HELIX 2 2 ASN A 469 TYR A 477 1 9 HELIX 3 3 THR A 483 LEU A 497 1 15 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
Complete list - r 2 2 Bytes