Header list of 1tns.pdb file
Complete list - 2 20 Bytes
HEADER DNA BINDING PROTEIN 10-OCT-94 1TNS
TITLE A NOVEL CLASS OF WINGED HELIX-TURN-HELIX PROTEIN: THE DNA-BINDING
TITLE 2 DOMAIN OF MU TRANSPOSASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MU-TRANSPOSASE;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTEROBACTERIA PHAGE MU;
SOURCE 3 ORGANISM_TAXID: 10677
KEYWDS DNA-BINDING PROTEIN, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR G.M.CLORE,R.T.CLUBB,J.G.OMICHINSKI,A.M.GRONENBORN
REVDAT 3 02-MAR-22 1TNS 1 KEYWDS REMARK SEQADV
REVDAT 2 24-FEB-09 1TNS 1 VERSN
REVDAT 1 14-FEB-95 1TNS 0
JRNL AUTH R.T.CLUBB,J.G.OMICHINSKI,H.SAVILAHTI,K.MIZUUCHI,
JRNL AUTH 2 A.M.GRONENBORN,G.M.CLORE
JRNL TITL A NOVEL CLASS OF WINGED HELIX-TURN-HELIX PROTEIN: THE
JRNL TITL 2 DNA-BINDING DOMAIN OF MU TRANSPOSASE.
JRNL REF STRUCTURE V. 2 1041 1994
JRNL REFN ISSN 0969-2126
JRNL PMID 7881904
JRNL DOI 10.1016/S0969-2126(94)00107-3
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE 3D SOLUTION STRUCTURE OF THE DNA BINDING DOMAIN OF MU
REMARK 3 TRANSPOSASE (MUA76, RESIDUES 1 - 76) WAS SOLVED BY
REMARK 3 MULTIDIMENSIONAL HETERONUCLEAR-EDITED NMR EXPERIMENTS AND
REMARK 3 IS BASED ON 1320 EXPERIMENTAL RESTRAINTS COMPRISING THE
REMARK 3 FOLLOWING: (A) 1192 APPROXIMATE INTERPROTON DISTANCE
REMARK 3 RESTRAINTS (308 SEQUENTIAL, 266 SHORT RANGE 1 , |I-J| <=5,
REMARK 3 323 LONG RANGE |I-J|>5, AND 295 INTRARESIDUE (B) 18
REMARK 3 DISTANCE RESTRAINTS FOR 9 BACKBONE HYDROGEN BONDS (C) 36
REMARK 3 HN-CAH COUPLING CONSTANT RESTRAINTS (D) 74 TORSION ANGLE
REMARK 3 RESTRAINTS (40 PHI, 23 CHI1 AND 11 CHI2).
REMARK 3
REMARK 3 A COMPLETE LIST OF EXPERIMENTAL RESTRAINTS HAVE BEEN
REMARK 3 DEPOSITED WITH THE BROOKHAVEN DATA BANK.
REMARK 3
REMARK 3 THE STRUCTURES ARE CALCULATED USING THE HYBRID METRIC
REMARK 3 MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED ANNEALING
REMARK 3 METHOD DESCRIBED BY: NILGES, M., CLORE, G.M. &
REMARK 3 GRONENBORN, A.M. (1988) FEBS LETT 229, 317 - 324 ALL
REMARK 3 STRUCTURAL STATISTICS ARE GIVEN IN REF. 1.
REMARK 3
REMARK 3 THIS STRUCTURE IS THE RESTRAINED MINIMIZED AVERAGE
REMARK 3 STRUCTURE: (SA)R. THIS IS OBTAINED BY FIRST AVERAGING
REMARK 3 THE COORDINATES OF THE INDIVIDUAL 33 DYNAMICAL SIMULATED
REMARK 3 ANNEALING (SA) STRUCTURES BEST FITTED TO RESIDUES 3 - 36
REMARK 3 AND 45 - 65 AND SUBJECTING THE RESULTING COORDINATES TO
REMARK 3 RESTRAINED MINIMIZATION. THE LAST NUMBER COLUMN IN THIS
REMARK 3 SET OF COORDINATES (THE B-FACTOR COLUMN IN X-RAY
REMARK 3 STRUCTURES) GIVES THE AVERAGE RMS DIFFERENCE BETWEEN THE
REMARK 3 INDIVIDUAL SA STRUCTURES AND THE MEAN STRUCTURE. THE
REMARK 3 NUMBERS IN THE LAST COLUMN OF THE INDIVIDUAL STRUCTURES
REMARK 3 HAVE NO MEANING. RESIDUES 1 - 2, 66 - 76, AND 37 - 44 ARE
REMARK 3 DISORDERED IN SOLUTION. THE 33 INDIVIDUAL STRUCTURES CAN
REMARK 3 BE FOUND IN PDB ENTRY 1TNT.
REMARK 4
REMARK 4 1TNS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176761.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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: 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 LEU A 3 74.35 -161.65
REMARK 500 ALA A 11 29.24 -64.14
REMARK 500 ASN A 12 -8.49 -146.05
REMARK 500 PRO A 17 177.69 -55.06
REMARK 500 GLN A 30 -61.74 -150.16
REMARK 500 GLN A 33 98.07 -47.88
REMARK 500 VAL A 40 -83.13 -93.08
REMARK 500 LYS A 41 -74.06 -80.52
REMARK 500 LYS A 44 97.32 52.05
REMARK 500 PRO A 54 -165.06 -57.25
REMARK 500 GLU A 67 93.37 55.99
REMARK 500 ILE A 68 -77.92 -85.14
REMARK 500 GLU A 69 -133.64 -136.18
REMARK 500 THR A 70 -139.27 -80.73
REMARK 500 SER A 71 -74.16 73.33
REMARK 500 PHE A 75 23.60 40.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1TNT RELATED DB: PDB
DBREF 1TNS A 1 76 UNP P07636 TRA_BPMU 1 76
SEQADV 1TNS LEU A 10 UNP P07636 CYS 10 CONFLICT
SEQRES 1 A 76 MET GLU LEU TRP VAL SER PRO LYS GLU LEU ALA ASN LEU
SEQRES 2 A 76 PRO GLY LEU PRO LYS THR SER ALA GLY VAL ILE TYR VAL
SEQRES 3 A 76 ALA LYS LYS GLN GLY TRP GLN ASN ARG THR ARG ALA GLY
SEQRES 4 A 76 VAL LYS GLY GLY LYS ALA ILE GLU TYR ASN ALA ASN SER
SEQRES 5 A 76 LEU PRO VAL GLU ALA LYS ALA ALA LEU LEU LEU ARG GLN
SEQRES 6 A 76 GLY GLU ILE GLU THR SER LEU GLY TYR PHE GLU
HELIX 1 1 SER A 6 ALA A 11 1 6
HELIX 2 2 THR A 19 LYS A 29 1 11
HELIX 3 3 PRO A 54 GLN A 65 1 12
SHEET 1 A 2 TRP A 4 VAL A 5 0
SHEET 2 A 2 TYR A 48 ASN A 49 -1 O TYR A 48 N VAL A 5
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 - 2 20 Bytes