Header list of 1f84.pdb file
Complete list - b 23 2 Bytes
HEADER RNA 28-JUN-00 1F84
TITLE SOLUTION STRUCTURE OF HCV IRES RNA DOMAIN IIID
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HCV-1B IRES RNA DOMAIN IIID;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: HCV IRES RNA DOMAIN IIID (NUCLEOTIDES 252-290 OF GENOMIC
COMPND 5 HEPATITIS C VIRAL RNA);
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SYNTHESIZED ENZYMATICALLY IN-VITRO USING T7 RNA
SOURCE 4 POLYMERASE
KEYWDS RIBONUCLEIC ACID, HEPATITIS C VIRUS INTERNAL RIBOSOME ENTRY SITE,
KEYWDS 2 SARCIN/RICIN LOOP, LOOP E MOTIF, HAIRPIN LOOP, RNA STRUCTURE, RNA
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR P.J.LUKAVSKY,G.A.OTTO,A.M.LANCASTER,P.SARNOW,J.D.PUGLISI
REVDAT 5 23-FEB-22 1F84 1 REMARK
REVDAT 4 24-FEB-09 1F84 1 VERSN
REVDAT 3 08-MAR-05 1F84 3 ATOM HETATM REMARK MASTER
REVDAT 2 01-APR-03 1F84 1 JRNL
REVDAT 1 17-NOV-00 1F84 0
JRNL AUTH P.J.LUKAVSKY,G.A.OTTO,A.M.LANCASTER,P.SARNOW,J.D.PUGLISI
JRNL TITL STRUCTURES OF TWO RNA DOMAINS ESSENTIAL FOR HEPATITIS C
JRNL TITL 2 VIRUS INTERNAL RIBOSOME ENTRY SITE FUNCTION.
JRNL REF NAT.STRUCT.BIOL. V. 7 1105 2000
JRNL REFN ISSN 1072-8368
JRNL PMID 11101890
JRNL DOI 10.1038/81951
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: SEE REFERENCE ABOVE
REMARK 4
REMARK 4 1F84 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUL-00.
REMARK 100 THE DEPOSITION ID IS D_1000011359.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 283; 298
REMARK 210 PH : 6.40; 6.40
REMARK 210 IONIC STRENGTH : 10MM; 10MM
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5MM RNA, NON-ISOTOPICALLY
REMARK 210 LABELLED; 1MM RNA, U-15N,13C
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : P31-DECOUPLED DQF COSY, HP COSY,
REMARK 210 D2O NOESY, H2O NOESY; 3D HCP, 3D
REMARK 210 HMQC-TOCSY, 3D C13-EDITED NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY 3.8
REMARK 210 METHOD USED : SIMULATED ANNEALING AND
REMARK 210 RESTRAINED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 21
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE
REMARK 210 RESONANCE HCN AND HCP EXPERIMENTS ON N15,C13-
REMARK 210 LABELLED RNA
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: 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: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 15 G A 1 O5' G A 1 C5' -0.699
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 15 G A 1 O5' - C5' - C4' ANGL. DEV. = 24.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1F84 A 1 29 PDB 1F84 1F84 1 29
SEQRES 1 A 29 G G C C G A G U A G U G U
SEQRES 2 A 29 U G G G U C G C G A A A G
SEQRES 3 A 29 G C C
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 23 2 Bytes