Header list of 1eht.pdb file
Complete list - 16 20 Bytes
HEADER RNA 20-MAR-97 1EHT
TITLE THEOPHYLLINE-BINDING RNA IN COMPLEX WITH THEOPHYLLINE, NMR, 10
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THEOPHYLLINE-BINDING RNA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BINDING FRAGMENT, RESIDUES 1 - 33;
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: CONSENSUS SEQUENCE OF THE THEOPHYLLINE BINDING RNA
COMPND 7 APTAMER FLANKED BY A FOUR BASE-PAIR STEM, A THREE BASE-PAIR STEM, AND
COMPND 8 CAPPED BY A GAAA TETRALOOP
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES
KEYWDS RIBONUCLEIC ACID, RNA
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR G.R.ZIMMERMANN,A.PARDI
REVDAT 3 16-FEB-22 1EHT 1 REMARK
REVDAT 2 24-FEB-09 1EHT 1 VERSN
REVDAT 1 24-DEC-97 1EHT 0
JRNL AUTH G.R.ZIMMERMANN,R.D.JENISON,C.L.WICK,J.P.SIMORRE,A.PARDI
JRNL TITL INTERLOCKING STRUCTURAL MOTIFS MEDIATE MOLECULAR
JRNL TITL 2 DISCRIMINATION BY A THEOPHYLLINE-BINDING RNA.
JRNL REF NAT.STRUCT.BIOL. V. 4 644 1997
JRNL REFN ISSN 1072-8368
JRNL PMID 9253414
JRNL DOI 10.1038/NSB0897-644
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH R.D.JENISON,S.C.GILL,A.PARDI,B.POLISKY
REMARK 1 TITL HIGH-RESOLUTION MOLECULAR DISCRIMINATION BY RNA
REMARK 1 REF SCIENCE V. 263 1425 1994
REMARK 1 REFN ISSN 0036-8075
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1EHT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000173054.
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 : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST TOTAL ENERGY
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: 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 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. = -2.6 DEGREES
REMARK 500 1 G A 2 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 G A 2 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 1 G A 4 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 G A 4 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 1 A A 5 N7 - C8 - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 A A 7 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 A A 10 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 G A 11 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 G A 11 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 1 G A 14 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 G A 14 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 1 A A 15 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 A A 16 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 A A 17 N7 - C8 - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 G A 18 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 G A 18 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 1 G A 19 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 G A 19 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 1 G A 25 N7 - C8 - N9 ANGL. DEV. = 4.7 DEGREES
REMARK 500 1 G A 25 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 1 G A 26 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 G A 26 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 1 A A 28 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 G A 29 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 1 G A 29 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 1 G A 31 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 1 G A 31 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 2 G A 1 N7 - C8 - N9 ANGL. DEV. = 4.6 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 4 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 2 G A 4 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 2 A A 5 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 A A 7 N7 - C8 - N9 ANGL. DEV. = 3.6 DEGREES
REMARK 500 2 A A 10 N7 - C8 - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 G A 11 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 G A 11 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 2 G A 14 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 G A 14 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 2 A A 15 N7 - C8 - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 A A 16 N7 - C8 - N9 ANGL. DEV. = 3.6 DEGREES
REMARK 500 2 A A 17 N7 - C8 - N9 ANGL. DEV. = 3.9 DEGREES
REMARK 500 2 G A 18 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 2 G A 18 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 2 G A 19 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 G A 19 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 2 G A 25 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 292 ANGLE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TEP A 34
DBREF 1EHT A 1 33 PDB 1EHT 1EHT 1 33
SEQRES 1 A 33 G G C G A U A C C A G C C
SEQRES 2 A 33 G A A A G G C C C U U G G
SEQRES 3 A 33 C A G C G U C
HET TEP A 34 21
HETNAM TEP THEOPHYLLINE
FORMUL 2 TEP C7 H8 N4 O2
SITE 1 AC1 6 U A 6 A A 7 C A 8 C A 22
SITE 2 AC1 6 U A 24 A A 28
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 - 16 20 Bytes