Header list of 1zzf.pdb file
Complete list - 9 20 Bytes
HEADER TRANSCRIPTION 14-JUN-05 1ZZF
TITLE THE DNA-BOUND SOLUTION STRUCTURE OF HPV-16 E2 DNA-BINDING DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: REGULATORY PROTEIN E2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: DNA-BINDING DOMAIN;
COMPND 5 SYNONYM: HPV-16 E2 TRANSCRIPTION FACTOR;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN PAPILLOMAVIRUS TYPE 16;
SOURCE 3 ORGANISM_TAXID: 333760;
SOURCE 4 GENE: E2;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: JM109;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTZ18U-E2
KEYWDS DNA-PROTEIN COMPLEX, PAPILLOMAVIRUS TRANSCRIPTION FACTOR, DIMERIC
KEYWDS 2 BETA-BARREL, TRANSCRIPTION
EXPDTA SOLUTION NMR
AUTHOR T.ELISEO,A.D.NADRA,G.DE PRAT-GAY,M.PACI,O.D.CICERO
REVDAT 3 09-MAR-22 1ZZF 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1ZZF 1 VERSN
REVDAT 1 14-MAR-06 1ZZF 0
JRNL AUTH T.ELISEO,A.D.NADRA,G.DE PRAT-GAY,M.PACI,O.D.CICERO
JRNL TITL THE DNA-BOUND SOLUTION STRUCTURE OF HPV-16 E2 DNA-BINDING
JRNL TITL 2 DOMAIN
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.0, X-PLOR
REMARK 3 AUTHORS : BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ZZF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000033301.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 318
REMARK 210 PH : 5.6
REMARK 210 IONIC STRENGTH : 250 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : DNA-E2C COMPLEX (15N) 0.6MM,
REMARK 210 25MM ACETATE+ 10MM PHOSPHATE, PH
REMARK 210 5.6, NACL 250MM, DTT 5MM; DNA-
REMARK 210 E2C COMPLEX (15N, 13C) 0.6MM,
REMARK 210 25MM ACETATE+ 10MM PHOSPHATE, PH
REMARK 210 5.6, NACL 250MM, DTT 5MM; DNA-
REMARK 210 E2C COMPLEX (15N) 0.2MM, 25MM
REMARK 210 ACETATE+ 10MM PHOSPHATE, PH 5.6,
REMARK 210 NACL 250MM, DTT 5MM,
REMARK 210 PHILAMENTOSUS PHAGE 17MG/ML
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 700 MHZ; 400 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW
REMARK 210 METHOD USED : REFINEMENT BY RESTRAINED
REMARK 210 MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
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: NULL
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 HIS A 24 50.62 -92.21
REMARK 500 SER A 33 -161.63 -75.37
REMARK 500 VAL A 42 91.39 51.52
REMARK 500 HIS A 44 14.29 -140.95
REMARK 500 HIS B 24 50.64 -92.24
REMARK 500 SER B 33 -161.69 -75.37
REMARK 500 VAL B 42 91.38 51.49
REMARK 500 HIS B 44 14.14 -140.87
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 ARG A 18 0.25 SIDE CHAIN
REMARK 500 ARG A 20 0.30 SIDE CHAIN
REMARK 500 ARG A 59 0.31 SIDE CHAIN
REMARK 500 ARG B 18 0.25 SIDE CHAIN
REMARK 500 ARG B 20 0.30 SIDE CHAIN
REMARK 500 ARG B 59 0.31 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1R8P RELATED DB: PDB
REMARK 900 HPV-16 E2C SOLUTION STRUCTURE
DBREF 1ZZF A 2 81 UNP P03120 VE2_HPV16 286 365
DBREF 1ZZF B 2 81 UNP P03120 VE2_HPV16 286 365
SEQADV 1ZZF MET A 1 UNP P03120 INITIATING METHIONINE
SEQADV 1ZZF MET B 1 UNP P03120 INITIATING METHIONINE
SEQRES 1 A 81 MET THR PRO ILE VAL HIS LEU LYS GLY ASP ALA ASN THR
SEQRES 2 A 81 LEU LYS CYS LEU ARG TYR ARG PHE LYS LYS HIS CYS THR
SEQRES 3 A 81 LEU TYR THR ALA VAL SER SER THR TRP HIS TRP THR GLY
SEQRES 4 A 81 HIS ASN VAL LYS HIS LYS SER ALA ILE VAL THR LEU THR
SEQRES 5 A 81 TYR ASP SER GLU TRP GLN ARG ASP GLN PHE LEU SER GLN
SEQRES 6 A 81 VAL LYS ILE PRO LYS THR ILE THR VAL SER THR GLY PHE
SEQRES 7 A 81 MET SER ILE
SEQRES 1 B 81 MET THR PRO ILE VAL HIS LEU LYS GLY ASP ALA ASN THR
SEQRES 2 B 81 LEU LYS CYS LEU ARG TYR ARG PHE LYS LYS HIS CYS THR
SEQRES 3 B 81 LEU TYR THR ALA VAL SER SER THR TRP HIS TRP THR GLY
SEQRES 4 B 81 HIS ASN VAL LYS HIS LYS SER ALA ILE VAL THR LEU THR
SEQRES 5 B 81 TYR ASP SER GLU TRP GLN ARG ASP GLN PHE LEU SER GLN
SEQRES 6 B 81 VAL LYS ILE PRO LYS THR ILE THR VAL SER THR GLY PHE
SEQRES 7 B 81 MET SER ILE
HELIX 1 1 ALA A 11 LYS A 22 1 12
HELIX 2 2 LYS A 23 TYR A 28 5 6
HELIX 3 3 SER A 55 SER A 64 1 10
HELIX 4 4 ALA B 11 LYS B 22 1 12
HELIX 5 5 LYS B 23 TYR B 28 5 6
HELIX 6 6 SER B 55 SER B 64 1 10
SHEET 1 A 8 ALA A 30 TRP A 35 0
SHEET 2 A 8 SER A 46 THR A 52 -1 O ILE A 48 N TRP A 35
SHEET 3 A 8 THR A 2 ASP A 10 -1 N VAL A 5 O LEU A 51
SHEET 4 A 8 ILE A 72 SER A 80 -1 O THR A 73 N LYS A 8
SHEET 5 A 8 ILE B 72 SER B 80 -1 O PHE B 78 N PHE A 78
SHEET 6 A 8 THR B 2 ASP B 10 -1 N LYS B 8 O THR B 73
SHEET 7 A 8 SER B 46 THR B 52 -1 O LEU B 51 N VAL B 5
SHEET 8 A 8 ALA B 30 TRP B 35 -1 N SER B 32 O THR B 50
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
Complete list - 9 20 Bytes