Header list of 1f6v.pdb file
Complete list - b 1 2 Bytes
HEADER DNA BINDING PROTEIN 23-JUN-00 1F6V
TITLE SOLUTION STRUCTURE OF THE C TERMINAL OF MU B TRANSPOSITION PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA TRANSPOSITION PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN;
COMPND 5 SYNONYM: MU B TRANSPOSITION PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE MU;
SOURCE 3 ORGANISM_TAXID: 10677;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PHH05;
SOURCE 8 OTHER_DETAILS: T7 PHAGE
KEYWDS MU PHAGE, RECOMBINATION, TRANSPOSITION, ATPASE, DNA BINDING, HIGH
KEYWDS 2 SALT, SOLUTION STRUCTURE, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR L.-H.HUNG,G.CHACONAS,G.S.SHAW
REVDAT 4 01-FEB-17 1F6V 1 AUTHOR VERSN
REVDAT 3 24-FEB-09 1F6V 1 VERSN
REVDAT 2 01-APR-03 1F6V 1 JRNL
REVDAT 1 08-NOV-00 1F6V 0
JRNL AUTH L.H.HUNG,G.CHACONAS,G.S.SHAW
JRNL TITL THE SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF THE MU B
JRNL TITL 2 TRANSPOSITION PROTEIN.
JRNL REF EMBO J. V. 19 5625 2000
JRNL REFN ISSN 0261-4189
JRNL PMID 11060014
JRNL DOI 10.1093/EMBOJ/19.21.5625
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 1047 NOE DERIVED, AND 55
REMARK 3 DIHEDRAL CONSTRAINTS.
REMARK 3 THERE ARE NO LONG-RANGE NOES OBSERVED FOR THE FIRST 8 RESIDUES
REMARK 3 WHICH ARE DISORDERED.
REMARK 4
REMARK 4 1F6V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUN-00.
REMARK 100 THE RCSB ID CODE IS RCSB011316.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 1.5 M NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.75 MM MU B U-15N,13C; 20 MM
REMARK 210 PHOSPHATE BUFFER; 0.75 MM MU B U-
REMARK 210 15N; 20 MM PHOSPHATE BUFFER; 0.75
REMARK 210 MM MU B NA; 20 MM PHOSPHATE
REMARK 210 BUFFER; MU B U-15N-(COMBINATIONS
REMARK 210 OF LEU, ILE, GLY, SER, GLU, ARG,
REMARK 210 ALA),20 MM PHOSPHATE BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N-
REMARK 210 SEPARATED_NOESY; HNHA; 3D_15N-
REMARK 210 SEPARATED TOCSY; 2D NOESY; 2D
REMARK 210 TOCSY; 15N-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, VNMR
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 LOWEST ENERGY
REMARK 210 AND NO RESTRAINT VIOLATIONS WITH
REMARK 210 PHI PSI ANGLES IN ALLOWED REGIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: HIGH IONIC CONDITIONS PRECLUDED MANY OF THE STANDARD
REMARK 210 TRIPLE RESONANCE EXPERIMENTS.
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-20
REMARK 470 RES CSSEQI ATOMS
REMARK 470 ASN A 91 O
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 ALA A 9 -171.21 -55.04
REMARK 500 1 LYS A 12 15.18 53.14
REMARK 500 1 THR A 13 -168.16 43.10
REMARK 500 1 TRP A 25 -143.61 -99.39
REMARK 500 1 GLN A 26 81.61 -65.99
REMARK 500 1 ASN A 28 -49.60 -152.86
REMARK 500 1 GLN A 38 20.95 -146.01
REMARK 500 1 PRO A 43 -79.86 -73.22
REMARK 500 1 ALA A 45 -0.71 -152.55
REMARK 500 1 LEU A 46 -82.07 -46.40
REMARK 500 1 ARG A 47 -75.73 8.97
REMARK 500 1 ALA A 56 -35.75 -32.01
REMARK 500 1 MET A 58 94.16 -67.33
REMARK 500 1 HIS A 61 90.02 -32.75
REMARK 500 1 LYS A 63 -41.26 175.23
REMARK 500 1 ARG A 66 -153.12 -76.42
REMARK 500 1 VAL A 67 70.97 -151.71
REMARK 500 1 ASN A 68 -166.32 163.44
REMARK 500 1 TYR A 71 -51.90 -29.25
REMARK 500 1 ARG A 77 -43.37 -150.27
REMARK 500 1 LEU A 79 -73.02 -94.16
REMARK 500 1 ASP A 80 -44.02 169.09
REMARK 500 1 LEU A 81 59.73 83.08
REMARK 500 1 ASP A 82 -30.48 -168.45
REMARK 500 1 VAL A 83 -40.87 -155.51
REMARK 500 1 SER A 86 -147.39 -69.43
REMARK 500 1 LEU A 89 -67.39 -144.89
REMARK 500 1 ARG A 90 -169.41 -53.64
REMARK 500 2 SER A 2 -88.32 -101.55
REMARK 500 2 ARG A 3 61.87 -101.58
REMARK 500 2 THR A 8 -88.37 -78.39
REMARK 500 2 ILE A 10 79.84 -108.24
REMARK 500 2 LYS A 12 94.70 -38.88
REMARK 500 2 THR A 13 162.87 -48.73
REMARK 500 2 TRP A 25 -148.82 65.80
REMARK 500 2 ASN A 28 -43.33 -161.92
REMARK 500 2 GLN A 38 22.31 -145.13
REMARK 500 2 PRO A 43 -84.81 -73.73
REMARK 500 2 ALA A 45 -7.35 -147.65
REMARK 500 2 LEU A 46 -77.72 -45.91
REMARK 500 2 ARG A 47 -73.52 4.99
REMARK 500 2 ALA A 56 -37.18 -30.56
REMARK 500 2 MET A 58 97.08 -63.70
REMARK 500 2 ARG A 66 -102.82 -106.04
REMARK 500 2 VAL A 67 130.84 177.92
REMARK 500 2 ASN A 68 -150.06 76.63
REMARK 500 2 TYR A 71 -48.14 -29.42
REMARK 500 2 ARG A 77 -34.12 -153.28
REMARK 500 2 LEU A 79 -70.77 -103.76
REMARK 500 2 ASP A 80 -46.77 171.84
REMARK 500
REMARK 500 THIS ENTRY HAS 536 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 3 0.29 SIDE CHAIN
REMARK 500 1 ARG A 7 0.26 SIDE CHAIN
REMARK 500 1 ARG A 47 0.16 SIDE CHAIN
REMARK 500 1 ARG A 54 0.25 SIDE CHAIN
REMARK 500 1 ARG A 66 0.09 SIDE CHAIN
REMARK 500 1 ARG A 73 0.24 SIDE CHAIN
REMARK 500 1 ARG A 77 0.28 SIDE CHAIN
REMARK 500 1 ARG A 90 0.27 SIDE CHAIN
REMARK 500 2 ARG A 3 0.27 SIDE CHAIN
REMARK 500 2 ARG A 7 0.32 SIDE CHAIN
REMARK 500 2 ARG A 47 0.32 SIDE CHAIN
REMARK 500 2 ARG A 54 0.32 SIDE CHAIN
REMARK 500 2 ARG A 66 0.31 SIDE CHAIN
REMARK 500 2 ARG A 73 0.29 SIDE CHAIN
REMARK 500 2 ARG A 77 0.08 SIDE CHAIN
REMARK 500 2 ARG A 90 0.27 SIDE CHAIN
REMARK 500 3 ARG A 3 0.24 SIDE CHAIN
REMARK 500 3 ARG A 7 0.30 SIDE CHAIN
REMARK 500 3 ARG A 47 0.31 SIDE CHAIN
REMARK 500 3 ARG A 54 0.19 SIDE CHAIN
REMARK 500 3 ARG A 73 0.29 SIDE CHAIN
REMARK 500 3 ARG A 77 0.17 SIDE CHAIN
REMARK 500 3 ARG A 90 0.29 SIDE CHAIN
REMARK 500 4 ARG A 3 0.30 SIDE CHAIN
REMARK 500 4 ARG A 7 0.31 SIDE CHAIN
REMARK 500 4 ARG A 47 0.28 SIDE CHAIN
REMARK 500 4 ARG A 54 0.24 SIDE CHAIN
REMARK 500 4 ARG A 66 0.27 SIDE CHAIN
REMARK 500 4 ARG A 73 0.25 SIDE CHAIN
REMARK 500 4 ARG A 77 0.28 SIDE CHAIN
REMARK 500 4 ARG A 90 0.20 SIDE CHAIN
REMARK 500 5 ARG A 3 0.17 SIDE CHAIN
REMARK 500 5 ARG A 7 0.18 SIDE CHAIN
REMARK 500 5 ARG A 47 0.31 SIDE CHAIN
REMARK 500 5 ARG A 54 0.31 SIDE CHAIN
REMARK 500 5 ARG A 73 0.26 SIDE CHAIN
REMARK 500 5 ARG A 77 0.31 SIDE CHAIN
REMARK 500 5 ARG A 90 0.25 SIDE CHAIN
REMARK 500 6 ARG A 3 0.27 SIDE CHAIN
REMARK 500 6 ARG A 7 0.29 SIDE CHAIN
REMARK 500 6 ARG A 47 0.30 SIDE CHAIN
REMARK 500 6 ARG A 54 0.21 SIDE CHAIN
REMARK 500 6 ARG A 66 0.19 SIDE CHAIN
REMARK 500 6 ARG A 73 0.27 SIDE CHAIN
REMARK 500 6 ARG A 77 0.29 SIDE CHAIN
REMARK 500 6 ARG A 90 0.25 SIDE CHAIN
REMARK 500 7 ARG A 3 0.26 SIDE CHAIN
REMARK 500 7 ARG A 7 0.27 SIDE CHAIN
REMARK 500 7 ARG A 47 0.32 SIDE CHAIN
REMARK 500 7 ARG A 54 0.15 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 155 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1F6V A 2 91 UNP P03763 VPB_BPMU 223 312
SEQADV 1F6V GLY A 1 UNP P03763 CLONING ARTIFACT
SEQRES 1 A 91 GLY SER ARG ILE ALA LYS ARG THR ALA ILE ASN LYS THR
SEQRES 2 A 91 LYS LYS ALA ASP VAL LYS ALA ILE ALA ASP ALA TRP GLN
SEQRES 3 A 91 ILE ASN GLY GLU LYS GLU LEU GLU LEU LEU GLN GLN ILE
SEQRES 4 A 91 ALA GLN LYS PRO GLY ALA LEU ARG ILE LEU ASN HIS SER
SEQRES 5 A 91 LEU ARG LEU ALA ALA MET THR ALA HIS GLY LYS GLY GLU
SEQRES 6 A 91 ARG VAL ASN GLU ASP TYR LEU ARG GLN ALA PHE ARG GLU
SEQRES 7 A 91 LEU ASP LEU ASP VAL ASP ILE SER THR LEU LEU ARG ASN
HELIX 1 1 LYS A 14 VAL A 18 5 5
HELIX 2 2 LYS A 19 ALA A 24 1 6
HELIX 3 3 GLU A 30 GLN A 38 1 9
HELIX 4 4 ALA A 45 ARG A 54 1 10
HELIX 5 5 LEU A 55 ALA A 57 5 3
HELIX 6 6 ASN A 68 ARG A 77 1 10
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 - b 1 2 Bytes