Header list of 2tbd.pdb file
Complete list - r 16 2 Bytes
HEADER DNA BINDING PROTEIN 09-JAN-97 2TBD
TITLE SV40 T ANTIGEN DNA-BINDING DOMAIN, NMR, 30 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SV40 T ANTIGEN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DNA BINDING DOMAIN, RESIDUES 131 - 260;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SIMIAN VIRUS 40;
SOURCE 3 ORGANISM_TAXID: 10633;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21
KEYWDS REPLICATION, ORIGIN-BINDING DOMAIN, DNA-BINDING PROTEIN, EARLY
KEYWDS 2 PROTEIN, ACETYLATION, NUCLEAR PROTEIN, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR X.LUO,D.G.SANFORD,P.A.BULLOCK,W.W.BACHOVCHIN
REVDAT 3 16-MAR-22 2TBD 1 KEYWDS REMARK
REVDAT 2 24-FEB-09 2TBD 1 VERSN
REVDAT 1 01-APR-97 2TBD 0
JRNL AUTH X.LUO,D.G.SANFORD,P.A.BULLOCK,W.W.BACHOVCHIN
JRNL TITL SOLUTION STRUCTURE OF THE ORIGIN DNA-BINDING DOMAIN OF SV40
JRNL TITL 2 T-ANTIGEN.
JRNL REF NAT.STRUCT.BIOL. V. 3 1034 1996
JRNL REFN ISSN 1072-8368
JRNL PMID 8946857
JRNL DOI 10.1038/NSB1296-1034
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 2168
REMARK 3 INTERPROTON DISTANCE RESTRAINTS DERIVED FROM NOE MEASUREMENTS,
REMARK 3 AND 123 BACKBONE TORSION ANGLE RESTRAINTS DERIVED FROM COUPLING
REMARK 3 CONSTRAINTS. A TOTAL OF 30 STRUCTURES WERE CALCULATED.
REMARK 4
REMARK 4 2TBD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000178660.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; HNCA; HN(CO)CA;
REMARK 210 HCCH-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX, X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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 ON 13C, 15N-LABELED SV40 T-ANTIGEN DNA BINDING
REMARK 210 DOMAIN.
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 SER A 2 -40.81 -164.89
REMARK 500 1 ASP A 9 -165.43 178.01
REMARK 500 1 PHE A 17 76.85 -150.23
REMARK 500 1 HIS A 20 -72.55 80.18
REMARK 500 1 SER A 24 -173.09 -67.51
REMARK 500 1 THR A 36 158.34 -46.93
REMARK 500 1 LYS A 46 -68.45 -90.03
REMARK 500 1 VAL A 53 118.82 -30.48
REMARK 500 1 PHE A 55 126.26 174.09
REMARK 500 1 SER A 61 -98.13 -108.99
REMARK 500 1 HIS A 64 -165.74 -122.47
REMARK 500 1 PRO A 72 -80.36 -76.45
REMARK 500 1 HIS A 73 174.16 -48.30
REMARK 500 1 PHE A 90 15.62 -149.59
REMARK 500 1 SER A 91 -178.92 161.62
REMARK 500 1 GLU A 101 -71.10 -57.52
REMARK 500 1 MET A 104 -78.86 -43.66
REMARK 500 1 ASP A 111 157.80 -42.44
REMARK 500 1 ILE A 116 -61.74 -104.66
REMARK 500 1 LEU A 124 -92.53 -45.19
REMARK 500 1 LYS A 125 15.50 57.33
REMARK 500 1 HIS A 127 59.08 -90.64
REMARK 500 1 ASP A 128 22.04 -160.17
REMARK 500 1 GLU A 132 149.31 178.80
REMARK 500 2 VAL A 4 105.53 -42.99
REMARK 500 2 ASP A 9 -172.27 173.04
REMARK 500 2 PHE A 17 70.89 -160.08
REMARK 500 2 ALA A 21 133.75 -174.16
REMARK 500 2 PHE A 23 54.42 -109.32
REMARK 500 2 LYS A 46 -71.45 -82.86
REMARK 500 2 VAL A 53 129.59 -35.14
REMARK 500 2 PHE A 55 129.79 164.14
REMARK 500 2 SER A 61 -97.46 -113.67
REMARK 500 2 HIS A 64 -156.75 -149.67
REMARK 500 2 PRO A 72 -90.78 -74.21
REMARK 500 2 HIS A 73 177.86 -50.13
REMARK 500 2 TYR A 83 -66.04 -90.52
REMARK 500 2 GLU A 101 -78.92 -49.85
REMARK 500 2 ASP A 111 151.20 -42.30
REMARK 500 2 ILE A 116 -61.23 -120.30
REMARK 500 2 LYS A 125 -148.52 -142.28
REMARK 500 2 HIS A 127 -150.20 -57.85
REMARK 500 2 GLU A 132 143.68 66.04
REMARK 500 2 SER A 133 -38.67 -145.53
REMARK 500 3 SER A 2 158.33 -43.20
REMARK 500 3 LYS A 3 77.70 52.64
REMARK 500 3 VAL A 4 96.67 -43.38
REMARK 500 3 PHE A 17 71.13 -154.95
REMARK 500 3 HIS A 20 29.52 47.90
REMARK 500 3 LYS A 46 -75.90 -86.01
REMARK 500
REMARK 500 THIS ENTRY HAS 736 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 26 0.32 SIDE CHAIN
REMARK 500 1 ARG A 58 0.31 SIDE CHAIN
REMARK 500 1 ARG A 74 0.15 SIDE CHAIN
REMARK 500 1 ARG A 76 0.30 SIDE CHAIN
REMARK 500 1 ARG A 110 0.24 SIDE CHAIN
REMARK 500 2 ARG A 58 0.29 SIDE CHAIN
REMARK 500 2 ARG A 74 0.24 SIDE CHAIN
REMARK 500 2 ARG A 110 0.32 SIDE CHAIN
REMARK 500 3 ARG A 26 0.22 SIDE CHAIN
REMARK 500 3 ARG A 58 0.29 SIDE CHAIN
REMARK 500 3 ARG A 74 0.23 SIDE CHAIN
REMARK 500 3 ARG A 76 0.09 SIDE CHAIN
REMARK 500 3 ARG A 110 0.24 SIDE CHAIN
REMARK 500 4 ARG A 26 0.30 SIDE CHAIN
REMARK 500 4 ARG A 58 0.22 SIDE CHAIN
REMARK 500 4 ARG A 74 0.11 SIDE CHAIN
REMARK 500 4 ARG A 76 0.15 SIDE CHAIN
REMARK 500 4 ARG A 110 0.23 SIDE CHAIN
REMARK 500 5 ARG A 26 0.32 SIDE CHAIN
REMARK 500 5 ARG A 74 0.30 SIDE CHAIN
REMARK 500 5 ARG A 76 0.24 SIDE CHAIN
REMARK 500 5 ARG A 110 0.24 SIDE CHAIN
REMARK 500 6 ARG A 26 0.17 SIDE CHAIN
REMARK 500 6 ARG A 58 0.22 SIDE CHAIN
REMARK 500 6 ARG A 74 0.09 SIDE CHAIN
REMARK 500 6 ARG A 76 0.12 SIDE CHAIN
REMARK 500 6 ARG A 110 0.14 SIDE CHAIN
REMARK 500 7 ARG A 26 0.27 SIDE CHAIN
REMARK 500 7 ARG A 58 0.31 SIDE CHAIN
REMARK 500 7 ARG A 74 0.32 SIDE CHAIN
REMARK 500 7 ARG A 76 0.32 SIDE CHAIN
REMARK 500 7 ARG A 110 0.25 SIDE CHAIN
REMARK 500 8 ARG A 26 0.15 SIDE CHAIN
REMARK 500 8 ARG A 58 0.18 SIDE CHAIN
REMARK 500 8 ARG A 74 0.25 SIDE CHAIN
REMARK 500 8 ARG A 76 0.32 SIDE CHAIN
REMARK 500 8 ARG A 110 0.32 SIDE CHAIN
REMARK 500 9 ARG A 26 0.23 SIDE CHAIN
REMARK 500 9 ARG A 58 0.32 SIDE CHAIN
REMARK 500 9 ARG A 74 0.09 SIDE CHAIN
REMARK 500 9 ARG A 76 0.20 SIDE CHAIN
REMARK 500 9 ARG A 110 0.08 SIDE CHAIN
REMARK 500 10 ARG A 26 0.29 SIDE CHAIN
REMARK 500 10 ARG A 58 0.29 SIDE CHAIN
REMARK 500 10 ARG A 74 0.30 SIDE CHAIN
REMARK 500 10 ARG A 76 0.29 SIDE CHAIN
REMARK 500 10 ARG A 110 0.20 SIDE CHAIN
REMARK 500 11 ARG A 26 0.25 SIDE CHAIN
REMARK 500 11 ARG A 58 0.20 SIDE CHAIN
REMARK 500 11 ARG A 74 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 146 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2TBD A 3 132 UNP P03070 TALA_SV40 131 260
SEQRES 1 A 134 GLY SER LYS VAL GLU ASP PRO LYS ASP PHE PRO SER GLU
SEQRES 2 A 134 LEU LEU SER PHE LEU SER HIS ALA VAL PHE SER ASN ARG
SEQRES 3 A 134 THR LEU ALA CYS PHE ALA ILE TYR THR THR LYS GLU LYS
SEQRES 4 A 134 ALA ALA LEU LEU TYR LYS LYS ILE MET GLU LYS TYR SER
SEQRES 5 A 134 VAL THR PHE ILE SER ARG HIS ASN SER TYR ASN HIS ASN
SEQRES 6 A 134 ILE LEU PHE PHE LEU THR PRO HIS ARG HIS ARG VAL SER
SEQRES 7 A 134 ALA ILE ASN ASN TYR ALA GLN LYS LEU CYS THR PHE SER
SEQRES 8 A 134 PHE LEU ILE CYS LYS GLY VAL ASN LYS GLU TYR LEU MET
SEQRES 9 A 134 TYR SER ALA LEU THR ARG ASP PRO PHE SER VAL ILE GLU
SEQRES 10 A 134 GLU SER LEU PRO GLY GLY LEU LYS GLU HIS ASP PHE ASN
SEQRES 11 A 134 PRO GLU SER SER
HELIX 1 1 SER A 12 LEU A 15 5 4
HELIX 2 2 LYS A 37 GLU A 49 1 13
HELIX 3 3 SER A 78 LYS A 86 1 9
HELIX 4 4 TYR A 102 THR A 109 1 8
SHEET 1 A 5 ILE A 94 GLY A 97 0
SHEET 2 A 5 CYS A 30 THR A 35 -1 N TYR A 34 O ILE A 94
SHEET 3 A 5 ASN A 65 LEU A 70 -1 N PHE A 69 O PHE A 31
SHEET 4 A 5 PHE A 55 ASN A 60 -1 N HIS A 59 O ILE A 66
SHEET 5 A 5 SER A 114 GLU A 118 -1 N GLU A 117 O ARG A 58
SHEET 1 B 5 ILE A 94 GLY A 97 0
SHEET 2 B 5 CYS A 30 THR A 35 -1 N TYR A 34 O ILE A 94
SHEET 3 B 5 ASN A 65 LEU A 70 -1 N PHE A 69 O PHE A 31
SHEET 4 B 5 PHE A 55 ASN A 60 -1 N HIS A 59 O ILE A 66
SHEET 5 B 5 SER A 114 GLU A 118 -1 N GLU A 117 O ARG A 58
CISPEP 1 ASP A 111 PRO A 112 1 -0.42
CISPEP 2 ASP A 111 PRO A 112 2 -0.05
CISPEP 3 ASP A 111 PRO A 112 3 -0.01
CISPEP 4 ASP A 111 PRO A 112 4 -0.03
CISPEP 5 ASP A 111 PRO A 112 5 -0.43
CISPEP 6 ASP A 111 PRO A 112 6 -0.05
CISPEP 7 ASP A 111 PRO A 112 7 -0.12
CISPEP 8 ASP A 111 PRO A 112 8 0.00
CISPEP 9 ASP A 111 PRO A 112 9 -0.01
CISPEP 10 ASP A 111 PRO A 112 10 -0.20
CISPEP 11 ASP A 111 PRO A 112 11 -0.23
CISPEP 12 ASP A 111 PRO A 112 12 -0.03
CISPEP 13 ASP A 111 PRO A 112 13 -0.03
CISPEP 14 ASP A 111 PRO A 112 14 -0.32
CISPEP 15 ASP A 111 PRO A 112 15 -0.21
CISPEP 16 ASP A 111 PRO A 112 16 -0.09
CISPEP 17 ASP A 111 PRO A 112 17 0.24
CISPEP 18 ASP A 111 PRO A 112 18 -0.09
CISPEP 19 ASP A 111 PRO A 112 19 0.05
CISPEP 20 ASP A 111 PRO A 112 20 -0.31
CISPEP 21 ASP A 111 PRO A 112 21 -0.05
CISPEP 22 ASP A 111 PRO A 112 22 -0.23
CISPEP 23 ASP A 111 PRO A 112 23 -0.24
CISPEP 24 ASP A 111 PRO A 112 24 -0.12
CISPEP 25 ASP A 111 PRO A 112 25 -0.07
CISPEP 26 ASP A 111 PRO A 112 26 -0.25
CISPEP 27 ASP A 111 PRO A 112 27 -0.05
CISPEP 28 ASP A 111 PRO A 112 28 0.00
CISPEP 29 ASP A 111 PRO A 112 29 0.20
CISPEP 30 ASP A 111 PRO A 112 30 -0.05
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 16 2 Bytes