Header list of 1idv.pdb file
Complete list - 23 20 Bytes
HEADER RNA 05-APR-01 1IDV
TITLE NMR STRUCTURE OF HCV IRES RNA DOMAIN IIIC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEPATITIS C IRES RNA DOMAIN IIIC;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SYNTHESIZED BY IN VITRO TRANSCRIPTION USING T7 RNA
SOURCE 4 POLYMERASE
KEYWDS HEPATITIS C RNA, IRES, STEM-LOOP, DOMAIN IIIC, RNA
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR K.KALUARACHCHI,R.RIJNBRAND,S.M.LEMON,D.G.GORENSTEIN
REVDAT 4 23-FEB-22 1IDV 1 REMARK
REVDAT 3 24-FEB-09 1IDV 1 VERSN
REVDAT 2 29-MAR-05 1IDV 1 JRNL
REVDAT 1 05-OCT-01 1IDV 0
JRNL AUTH R.RIJNBRAND,V.THIVIYANATHAN,K.KALUARACHCHI,S.M.LEMON,
JRNL AUTH 2 D.G.GORENSTEIN
JRNL TITL MUTATIONAL AND STRUCTURAL ANALYSIS OF STEM-LOOP IIIC OF THE
JRNL TITL 2 HEPATITIS C VIRUS AND GB VIRUS B INTERNAL RIBOSOME ENTRY
JRNL TITL 3 SITES
JRNL REF J.MOL.BIOL. V. 343 805 2004
JRNL REFN ISSN 0022-2836
JRNL PMID 15476802
JRNL DOI 10.1016/J.JMB.2004.08.095
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1, MORASS 2.51
REMARK 3 AUTHORS : BRUNGER (X-PLOR), POST, MEADOWS, LUXON AND
REMARK 3 GORENSTEIN (MORASS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 254 NOE
REMARK 3 RESTRAINTS, 12 SUGAR PUCKER RESTRAINTS AND 9 HYDROGEN BONDS
REMARK 4
REMARK 4 1IDV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-APR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013189.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 283; 298
REMARK 210 PH : 6.8; 6.8
REMARK 210 IONIC STRENGTH : 10 MM KCL; 10 MM KCL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 10 MM SODIUM PHOSPHATE BUFFER,
REMARK 210 10 MM KCL, 0.05 MM EDTA, PH 6.8;
REMARK 210 10 MM SODIUM PHOSPHATE BUFFER,
REMARK 210 10 MM KCL, 0.05 MM EDTA, PH 6.8
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; 2D TOCSY;
REMARK 210 31P HETERO-TOCSY; 1H-13C HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING MOLECULAR
REMARK 210 DYNAMICS RELAXATION MATRIX
REMARK 210 ANALYSIS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : BACK CALCULATED DATA AGREE WITH
REMARK 210 EXPERIMENTAL NOESY SPECTRUM
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 10
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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 O2' G A 5 H5' U A 6 1.32
REMARK 500 O2' G A 2 H5' G A 3 1.48
REMARK 500 O6 G A 1 H41 C A 10 1.57
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 1 G A 1 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 G A 1 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 1 G A 2 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 G A 2 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 1 G A 3 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 G A 3 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 1 G A 5 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 G A 5 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 1 G A 7 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 G A 7 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 2 G A 1 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 G A 1 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 2 G A 2 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 G A 2 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 2 G A 3 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 2 G A 3 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 2 G A 5 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 2 G A 5 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 2 G A 7 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 2 G A 7 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 3 G A 1 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 3 G A 1 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 3 G A 2 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 3 G A 2 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 3 G A 3 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 3 G A 3 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 3 G A 5 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 3 G A 5 C8 - N9 - C4 ANGL. DEV. = -2.8 DEGREES
REMARK 500 3 G A 7 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 3 G A 7 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 4 G A 1 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 4 G A 1 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 4 G A 2 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 4 G A 2 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 4 G A 3 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 4 G A 3 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 4 G A 5 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 4 G A 5 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 4 G A 7 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 4 G A 7 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 5 G A 1 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 5 G A 1 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 5 G A 2 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 5 G A 2 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 5 G A 3 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 5 G A 3 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 5 G A 5 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 5 G A 5 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 5 G A 7 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 5 G A 7 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 100 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1IDV A 1 10 PDB 1IDV 1IDV 1 10
SEQRES 1 A 10 G G G C G U G C C C
CRYST1 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 - 23 20 Bytes