Header list of 1hji.pdb file
Complete list - n 14 2 Bytes
HEADER BACTERIOPHAGE HK022 15-JAN-01 1HJI
TITLE BACTERIOPHAGE HK022 NUN-PROTEIN-NUTBOXB-RNA COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNA (5-R(P*GP*CP*CP*CP*UP*GP*AP*AP*AP*AP*AP*GP*GP*GP*C)-3);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BACTERIOPHAGE LAMBDA NUTBOXB-RNA;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: NUTBOXB-RNA FROM THE NUTR-SEQUENCE;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: NUN-PROTEIN;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: N-TERMINAL BINDING-DOMAIN, RESIDUES 19-44;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACTERIOPHAGE LAMBDA;
SOURCE 3 ORGANISM_TAXID: 10710;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 MOL_ID: 2;
SOURCE 7 SYNTHETIC: YES;
SOURCE 8 ORGANISM_SCIENTIFIC: BACTERIOPHAGE HK022;
SOURCE 9 ORGANISM_TAXID: 10742
KEYWDS BACTERIOPHAGE HK022, TERMINATION, PEPTIDE-RNA-COMPLEX, PEPTIDE-RNA-
KEYWDS 2 RECOGNITION, PROTEIN/RNA
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR C.FABER,M.SCHAERPF,T.BECKER,H.STICHT,P.ROESCH
REVDAT 4 14-JUN-17 1HJI 1 REMARK
REVDAT 3 24-FEB-09 1HJI 1 VERSN
REVDAT 2 12-JUL-05 1HJI 1 JRNL
REVDAT 1 29-JAN-02 1HJI 0
JRNL AUTH C.FABER,M.SCHAERPF,T.BECKER,H.STICHT,P.ROESCH
JRNL TITL THE STRUCTURE OF THE COLIPHAGE HK022 NUN
JRNL TITL 2 PROTEIN-LAMBDA-PHAGE BOXB RNA COMPLEX. IMPLICATIONS FOR THE
JRNL TITL 3 MECHANISM OF TRANSCRIPTION TERMINATION
JRNL REF J.BIOL.CHEM. V. 276 32064 2001
JRNL REFN ISSN 0021-9258
JRNL PMID 11356847
JRNL DOI 10.1074/JBC.M102975200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.SCHAERPF,H.STICHT,K.SCHWEIMER,M.BOEHM,S.HOFFMANN,P.ROESCH
REMARK 1 TITL ANTITERMINATION IN BACTERIOPHAGE LAMBDA: THE STRUCTURE OF
REMARK 1 TITL 2 THE N36 PEPTIDE-BOXB RNA COMPLEX
REMARK 1 REF EUR.J.BIOCHEM. V. 267 2397 2000
REMARK 1 REFN ISSN 0014-2956
REMARK 1 PMID 10759866
REMARK 1 DOI 10.1046/J.1432-1327.2000.01251.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE
REMARK 4
REMARK 4 1HJI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JAN-01.
REMARK 100 THE DEPOSITION ID IS D_1290005795.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 301.0
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 90
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : COSY; TOCSY; NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NDEE, X-PLOR
REMARK 210 METHOD USED : MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 120
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST 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 O ILE B 30 H TRP B 33 1.56
REMARK 500 O ARG B 32 H ARG B 36 1.59
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 ASP B 26 -74.58 -54.47
REMARK 500 7 THR B 23 -169.27 -107.89
REMARK 500 8 ASP B 26 -70.06 -66.72
REMARK 500 11 THR B 23 35.64 -87.42
REMARK 500 11 SER B 24 -58.59 67.23
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 B 20 0.31 SIDE CHAIN
REMARK 500 1 ARG B 25 0.29 SIDE CHAIN
REMARK 500 1 ARG B 27 0.27 SIDE CHAIN
REMARK 500 1 ARG B 29 0.32 SIDE CHAIN
REMARK 500 1 ARG B 32 0.14 SIDE CHAIN
REMARK 500 1 ARG B 36 0.19 SIDE CHAIN
REMARK 500 2 ARG B 20 0.28 SIDE CHAIN
REMARK 500 2 ARG B 27 0.21 SIDE CHAIN
REMARK 500 2 ARG B 28 0.27 SIDE CHAIN
REMARK 500 2 ARG B 32 0.15 SIDE CHAIN
REMARK 500 2 ARG B 36 0.28 SIDE CHAIN
REMARK 500 3 ARG B 20 0.31 SIDE CHAIN
REMARK 500 3 ARG B 25 0.11 SIDE CHAIN
REMARK 500 3 ARG B 27 0.26 SIDE CHAIN
REMARK 500 3 ARG B 28 0.30 SIDE CHAIN
REMARK 500 3 ARG B 29 0.31 SIDE CHAIN
REMARK 500 3 ARG B 32 0.14 SIDE CHAIN
REMARK 500 3 ARG B 36 0.32 SIDE CHAIN
REMARK 500 4 ARG B 20 0.29 SIDE CHAIN
REMARK 500 4 ARG B 25 0.14 SIDE CHAIN
REMARK 500 4 ARG B 27 0.25 SIDE CHAIN
REMARK 500 4 ARG B 28 0.32 SIDE CHAIN
REMARK 500 4 ARG B 29 0.27 SIDE CHAIN
REMARK 500 4 ARG B 36 0.30 SIDE CHAIN
REMARK 500 5 ARG B 25 0.24 SIDE CHAIN
REMARK 500 5 ARG B 27 0.30 SIDE CHAIN
REMARK 500 5 ARG B 28 0.25 SIDE CHAIN
REMARK 500 5 ARG B 29 0.27 SIDE CHAIN
REMARK 500 5 ARG B 36 0.28 SIDE CHAIN
REMARK 500 6 ARG B 20 0.31 SIDE CHAIN
REMARK 500 6 ARG B 25 0.26 SIDE CHAIN
REMARK 500 6 ARG B 27 0.25 SIDE CHAIN
REMARK 500 6 ARG B 28 0.28 SIDE CHAIN
REMARK 500 6 ARG B 29 0.19 SIDE CHAIN
REMARK 500 6 ARG B 32 0.21 SIDE CHAIN
REMARK 500 6 ARG B 36 0.15 SIDE CHAIN
REMARK 500 7 ARG B 20 0.31 SIDE CHAIN
REMARK 500 7 ARG B 25 0.08 SIDE CHAIN
REMARK 500 7 ARG B 27 0.31 SIDE CHAIN
REMARK 500 7 ARG B 28 0.19 SIDE CHAIN
REMARK 500 7 ARG B 29 0.09 SIDE CHAIN
REMARK 500 7 ARG B 32 0.32 SIDE CHAIN
REMARK 500 7 ARG B 36 0.09 SIDE CHAIN
REMARK 500 8 ARG B 20 0.30 SIDE CHAIN
REMARK 500 8 ARG B 25 0.26 SIDE CHAIN
REMARK 500 8 ARG B 27 0.19 SIDE CHAIN
REMARK 500 8 ARG B 28 0.20 SIDE CHAIN
REMARK 500 8 ARG B 29 0.25 SIDE CHAIN
REMARK 500 8 ARG B 32 0.32 SIDE CHAIN
REMARK 500 8 ARG B 36 0.14 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 128 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1E4Z RELATED DB: PDB
REMARK 900 BACTERIOPHAGE HK022 NUN-PROTEIN-NUTBOXB-RNA COMPLEX
DBREF 1HJI A 1 15 PDB 1HJI 1HJI 1 15
DBREF 1HJI B 19 44 UNP P18683 VNUN_BPHK0 22 47
SEQRES 1 A 15 G C C C U G A A A A A G G
SEQRES 2 A 15 G C
SEQRES 1 B 26 ASP ARG GLY LEU THR SER ARG ASP ARG ARG ARG ILE ALA
SEQRES 2 B 26 ARG TRP GLU LYS ARG ILE ALA TYR ALA LEU LYS ASN GLY
HELIX 1 1 THR B 23 ASN B 43 1 21
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 - n 14 2 Bytes