Header list of 1r8p.pdb file
Complete list - c 21 2 Bytes
HEADER TRANSCRIPTION 28-OCT-03 1R8P
TITLE HPV-16 E2C SOLUTION STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: REGULATORY PROTEIN E2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: DNA BINDING DOMAIN;
COMPND 5 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: PTZ18
KEYWDS DIMERIC BETA-BARREL, DNA BINDING PROTEIN, TRANSCRIPTION FACTOR,
KEYWDS 2 TRANSCRIPTION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.D.NADRA,T.ELISEO,D.O.CICERO
REVDAT 6 21-DEC-22 1R8P 1 SEQADV
REVDAT 5 02-MAR-22 1R8P 1 REMARK
REVDAT 4 24-FEB-09 1R8P 1 VERSN
REVDAT 3 01-MAR-05 1R8P 1 JRNL
REVDAT 2 07-DEC-04 1R8P 1 JRNL
REVDAT 1 23-NOV-04 1R8P 0
JRNL AUTH A.D.NADRA,T.ELISEO,Y.-K.MOK,C.L.ALMEIDA,M.BYCROFT,M.PACI,
JRNL AUTH 2 G.DE PRAT-GAY,D.O.CICERO
JRNL TITL SOLUTION STRUCTURE OF THE HPV-16 E2 DNA BINDING DOMAIN, A
JRNL TITL 2 TRANSCRIPTIONAL REGULATOR WITH A DIMERIC BETA-BARREL FOLD
JRNL REF J.BIOMOL.NMR V. 30 211 2004
JRNL REFN ISSN 0925-2738
JRNL PMID 15702528
JRNL DOI 10.1023/B:JNMR.0000048942.96866.76
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.0, X-PLOR 3.85
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER, A.T. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURE DETERMINATION PROTOCOL AND
REMARK 3 STRUCTURAL STATISTICS ARE GIVEN IN THE REFERENCE IN THE JRNL
REMARK 3 RECORD.
REMARK 4
REMARK 4 1R8P COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-NOV-03.
REMARK 100 THE DEPOSITION ID IS D_1000020575.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 50MM PHOSPHATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.8MM 15N-LABELED HPV-16 E2C,
REMARK 210 50MM SODIUM PHOSPHATE, 5MM DTT;
REMARK 210 0.9MM 13C,15N-LABELED HPV-16 E2C,
REMARK 210 50MM SODIUM PHOSPHATE, 5MM DTT;
REMARK 210 0.2MM 15N-LABELED HPV-16 E2C,
REMARK 210 50MM SODIUM PHOSPHATE, 5MM DTT
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 97.027.12.56, NMRVIEW
REMARK 210 5.0, X-PLOR 3.85
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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 : 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: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
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
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 HIS A 24 33.92 -95.23
REMARK 500 1 THR A 26 54.09 -96.90
REMARK 500 1 LEU A 27 -32.02 -147.78
REMARK 500 1 ALA A 30 118.85 -160.10
REMARK 500 1 LYS A 43 -67.38 -131.35
REMARK 500 1 HIS A 44 -158.59 -154.86
REMARK 500 1 SER A 46 31.52 -141.42
REMARK 500 1 ALA A 47 152.65 -37.20
REMARK 500 1 PRO A 69 154.40 -39.90
REMARK 500 1 HIS B 24 34.05 -95.23
REMARK 500 1 THR B 26 54.06 -96.71
REMARK 500 1 LEU B 27 -32.02 -147.76
REMARK 500 1 LYS B 43 -68.44 -130.57
REMARK 500 1 HIS B 44 -157.74 -153.78
REMARK 500 1 SER B 46 32.25 -140.73
REMARK 500 1 ALA B 47 152.91 -37.94
REMARK 500 1 PRO B 69 154.50 -40.38
REMARK 500 2 HIS A 24 41.30 -95.15
REMARK 500 2 THR A 29 -62.83 -94.84
REMARK 500 2 HIS A 40 -29.46 179.70
REMARK 500 2 ASN A 41 113.12 -176.78
REMARK 500 2 HIS A 44 140.94 -36.75
REMARK 500 2 LYS A 45 42.06 -81.83
REMARK 500 2 ALA A 47 117.91 -170.60
REMARK 500 2 SER A 55 134.11 -171.15
REMARK 500 2 GLN A 65 -73.03 -95.52
REMARK 500 2 PRO A 69 179.01 -56.26
REMARK 500 2 HIS B 24 41.63 -94.82
REMARK 500 2 THR B 29 -63.23 -94.80
REMARK 500 2 HIS B 40 -31.09 179.38
REMARK 500 2 ASN B 41 115.18 -174.98
REMARK 500 2 HIS B 44 140.92 -36.07
REMARK 500 2 LYS B 45 44.04 -82.28
REMARK 500 2 ALA B 47 117.88 -169.96
REMARK 500 2 SER B 55 135.01 -170.71
REMARK 500 2 GLN B 65 -73.50 -95.68
REMARK 500 2 PRO B 69 178.55 -57.00
REMARK 500 3 HIS A 24 39.67 -95.42
REMARK 500 3 LEU A 27 -43.95 -148.11
REMARK 500 3 THR A 38 -155.82 -75.95
REMARK 500 3 VAL A 42 -168.46 -118.06
REMARK 500 3 LYS A 43 -70.47 -149.73
REMARK 500 3 ALA A 47 145.69 -35.99
REMARK 500 3 HIS B 24 40.01 -95.11
REMARK 500 3 LEU B 27 -44.38 -148.16
REMARK 500 3 THR B 38 -155.69 -76.03
REMARK 500 3 VAL B 42 -168.88 -117.65
REMARK 500 3 LYS B 43 -70.37 -149.39
REMARK 500 3 ALA B 47 145.87 -36.74
REMARK 500 4 THR A 2 105.23 -43.71
REMARK 500
REMARK 500 THIS ENTRY HAS 255 RAMACHANDRAN OUTLIERS.
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 1 ARG A 18 0.28 SIDE CHAIN
REMARK 500 1 ARG A 59 0.15 SIDE CHAIN
REMARK 500 1 ARG B 18 0.28 SIDE CHAIN
REMARK 500 1 ARG B 59 0.15 SIDE CHAIN
REMARK 500 2 ARG A 18 0.13 SIDE CHAIN
REMARK 500 2 ARG A 20 0.30 SIDE CHAIN
REMARK 500 2 ARG A 59 0.24 SIDE CHAIN
REMARK 500 2 ARG B 18 0.12 SIDE CHAIN
REMARK 500 2 ARG B 20 0.30 SIDE CHAIN
REMARK 500 2 ARG B 59 0.24 SIDE CHAIN
REMARK 500 3 ARG A 18 0.20 SIDE CHAIN
REMARK 500 3 ARG A 20 0.28 SIDE CHAIN
REMARK 500 3 ARG A 59 0.24 SIDE CHAIN
REMARK 500 3 ARG B 18 0.20 SIDE CHAIN
REMARK 500 3 ARG B 20 0.28 SIDE CHAIN
REMARK 500 3 ARG B 59 0.24 SIDE CHAIN
REMARK 500 4 ARG A 18 0.20 SIDE CHAIN
REMARK 500 4 ARG A 20 0.19 SIDE CHAIN
REMARK 500 4 ARG A 59 0.29 SIDE CHAIN
REMARK 500 4 ARG B 18 0.20 SIDE CHAIN
REMARK 500 4 ARG B 20 0.20 SIDE CHAIN
REMARK 500 4 ARG B 59 0.29 SIDE CHAIN
REMARK 500 5 ARG A 18 0.30 SIDE CHAIN
REMARK 500 5 ARG A 20 0.27 SIDE CHAIN
REMARK 500 5 ARG A 59 0.32 SIDE CHAIN
REMARK 500 5 ARG B 18 0.30 SIDE CHAIN
REMARK 500 5 ARG B 20 0.27 SIDE CHAIN
REMARK 500 5 ARG B 59 0.32 SIDE CHAIN
REMARK 500 6 ARG A 18 0.19 SIDE CHAIN
REMARK 500 6 ARG A 20 0.21 SIDE CHAIN
REMARK 500 6 ARG A 59 0.27 SIDE CHAIN
REMARK 500 6 ARG B 18 0.19 SIDE CHAIN
REMARK 500 6 ARG B 20 0.21 SIDE CHAIN
REMARK 500 6 ARG B 59 0.27 SIDE CHAIN
REMARK 500 7 ARG A 18 0.27 SIDE CHAIN
REMARK 500 7 ARG A 20 0.20 SIDE CHAIN
REMARK 500 7 ARG A 59 0.10 SIDE CHAIN
REMARK 500 7 ARG B 18 0.27 SIDE CHAIN
REMARK 500 7 ARG B 20 0.20 SIDE CHAIN
REMARK 500 7 ARG B 59 0.10 SIDE CHAIN
REMARK 500 8 ARG A 18 0.21 SIDE CHAIN
REMARK 500 8 ARG A 20 0.10 SIDE CHAIN
REMARK 500 8 ARG A 59 0.31 SIDE CHAIN
REMARK 500 8 ARG B 18 0.21 SIDE CHAIN
REMARK 500 8 ARG B 20 0.10 SIDE CHAIN
REMARK 500 8 ARG B 59 0.31 SIDE CHAIN
REMARK 500 9 ARG A 18 0.25 SIDE CHAIN
REMARK 500 9 ARG A 20 0.28 SIDE CHAIN
REMARK 500 9 ARG A 59 0.31 SIDE CHAIN
REMARK 500 9 ARG B 18 0.26 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 114 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BY9 RELATED DB: PDB
REMARK 900 HPV-16 E2C X-RAY STRUCTURE
REMARK 900 RELATED ID: 1F9F RELATED DB: PDB
REMARK 900 HPV-18 E2C X-RAY STRUCTURE
REMARK 900 RELATED ID: 1DHM RELATED DB: PDB
REMARK 900 HPV-31 E2C NMR STRUCTURE
REMARK 900 RELATED ID: 1DBD RELATED DB: PDB
REMARK 900 BPV-1 E2C NMR STRUCTURE
DBREF 1R8P A 2 81 UNP P03120 VE2_HPV16 286 365
DBREF 1R8P B 2 81 UNP P03120 VE2_HPV16 286 365
SEQADV 1R8P MET A 1 UNP P03120 INITIATING METHIONINE
SEQADV 1R8P 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 ASP A 10 HIS A 24 1 15
HELIX 2 2 SER A 55 VAL A 66 1 12
HELIX 3 3 ASP B 10 HIS B 24 1 15
HELIX 4 4 SER B 55 VAL B 66 1 12
SHEET 1 A 8 ALA A 30 VAL A 31 0
SHEET 2 A 8 ILE A 48 THR A 52 -1 O THR A 52 N ALA A 30
SHEET 3 A 8 THR A 2 LYS A 8 -1 N VAL A 5 O LEU A 51
SHEET 4 A 8 THR A 76 SER A 80 -1 O MET A 79 N THR A 2
SHEET 5 A 8 THR B 76 SER B 80 -1 O PHE B 78 N PHE A 78
SHEET 6 A 8 THR B 2 LYS B 8 -1 N THR B 2 O MET B 79
SHEET 7 A 8 ILE B 48 THR B 52 -1 O LEU B 51 N VAL B 5
SHEET 8 A 8 ALA B 30 VAL B 31 -1 N ALA B 30 O THR B 52
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 - c 21 2 Bytes