Header list of 1fl8.pdb file
Complete list - 23 20 Bytes
HEADER RNA 11-AUG-00 1FL8
TITLE HYPERMODIFIED NUCLEOSIDES IN THE ANTICODON OF TRNALYS STABILIZE A
TITLE 2 CANONICAL U-TURN STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ANTICODON DOMAIN OF TRNA(LYS);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: 17-MER TRNA(LYS) ANTICODON DOMAIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: RESIDUES 30-40 (TRNA NUMBERING) ARE IDENTICAL TO THOSE
COMPND 8 FOUND IN THE ANTICODON DOMAIN OF E. COLI TRNA(LYS) INCLUDING MODIFIED
COMPND 9 NUCLEOSIDES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES
KEYWDS TRNA, ANTICODON, PSEUDOURIDINE, MNM5S2U, T6A, RNA
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.SUNDARAM,P.C.DURANT,D.R.DAVIS
REVDAT 3 23-FEB-22 1FL8 1 REMARK LINK
REVDAT 2 24-FEB-09 1FL8 1 VERSN
REVDAT 1 16-OCT-00 1FL8 0
JRNL AUTH M.SUNDARAM,P.C.DURANT,D.R.DAVIS
JRNL TITL HYPERMODIFIED NUCLEOSIDES IN THE ANTICODON OF TRNALYS
JRNL TITL 2 STABILIZE A CANONICAL U-TURN STRUCTURE.
JRNL REF BIOCHEMISTRY V. 39 12575 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 11027137
JRNL DOI 10.1021/BI0014655
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1B, DISCOVER
REMARK 3 AUTHORS : VARIAN (VNMR), MSI (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 123 NOE-DERIVED RESTRAINTS, 15 HYDROGEN
REMARK 3 BOND RESTRAINTS, 102 LOWER/UPPER BOUND RESTRAINTS, 161 DIHEDRAL
REMARK 3 RESTRAINTS, 68 CHIRAL RESTRAINTS
REMARK 4
REMARK 4 1FL8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-AUG-00.
REMARK 100 THE DEPOSITION ID IS D_1000011684.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 285; 303
REMARK 210 PH : 7; 7
REMARK 210 IONIC STRENGTH : 120MM; 120MM
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5MM NATURAL ABUNDANCE RNA;
REMARK 210 10MM PHOSPHATE BUFFER; 50MM KCL;
REMARK 210 50MM NACL; 10MM MGCL2; 1.5MM
REMARK 210 NATURAL ABUNDANCE RNA; 10MM
REMARK 210 PHOSPHATE BUFFER; 50MM KCL; 50MM
REMARK 210 NACL; 10MM MGCL2
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; 1H-31P-COSY;
REMARK 210 1H-31P-HETERO-TOCSY-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1B, FELIX, DISCOVER
REMARK 210 METHOD USED : USED H5-H6 DISTANCES FOR
REMARK 210 DISTANCE CALCULATIONS THEN
REMARK 210 SIMULATED ANNEALING/MOLECULAR
REMARK 210 DYNAMICS IN VACUO THEN
REMARK 210 RESTRAINED MINIMIZATION IN VACUO
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 35
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 4
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES AND STANDARD 1H-31P 2D CORRELATION
REMARK 210 EXPERIMENTS.
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: 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 C A 32 O4' - C1' - N1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 1 U8U A 34 C3' - O3' - P ANGL. DEV. = -7.5 DEGREES
REMARK 500 2 U8U A 34 C3' - O3' - P ANGL. DEV. = -7.6 DEGREES
REMARK 500 3 U8U A 34 C3' - O3' - P ANGL. DEV. = -7.5 DEGREES
REMARK 500 4 U8U A 34 C3' - O3' - P ANGL. DEV. = -7.5 DEGREES
REMARK 500 5 U8U A 34 C3' - O3' - P ANGL. DEV. = -7.3 DEGREES
REMARK 500 6 U8U A 34 C3' - O3' - P ANGL. DEV. = -7.5 DEGREES
REMARK 500 7 C A 32 O4' - C1' - N1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 7 U8U A 34 C3' - O3' - P ANGL. DEV. = -7.3 DEGREES
REMARK 500 8 U8U A 34 C3' - O3' - P ANGL. DEV. = -7.4 DEGREES
REMARK 500 9 U8U A 34 C3' - O3' - P ANGL. DEV. = -7.5 DEGREES
REMARK 500 10 C A 32 O4' - C1' - N1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 10 U8U A 34 C3' - O3' - P ANGL. DEV. = -7.4 DEGREES
REMARK 500 10 PSU A 39 C3' - O3' - P ANGL. DEV. = -7.2 DEGREES
REMARK 500 11 C A 32 O4' - C1' - N1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 11 U8U A 34 C3' - O3' - P ANGL. DEV. = -7.7 DEGREES
REMARK 500 12 U8U A 34 C3' - O3' - P ANGL. DEV. = -7.4 DEGREES
REMARK 500 13 U8U A 34 C3' - O3' - P ANGL. DEV. = -7.6 DEGREES
REMARK 500 14 U8U A 34 C3' - O3' - P ANGL. DEV. = -7.6 DEGREES
REMARK 500 15 U A 33 O4' - C1' - N1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 16 U8U A 34 C3' - O3' - P ANGL. DEV. = -7.5 DEGREES
REMARK 500 17 U8U A 34 C3' - O3' - P ANGL. DEV. = -7.5 DEGREES
REMARK 500 18 U8U A 34 C3' - O3' - P ANGL. DEV. = -7.4 DEGREES
REMARK 500 19 U8U A 34 C3' - O3' - P ANGL. DEV. = -7.5 DEGREES
REMARK 500 20 U8U A 34 C3' - O3' - P ANGL. DEV. = -7.5 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BZU RELATED DB: PDB
REMARK 900 THE SAME ANTICODON LOOP SEQUENCE BUT WITHOUT MODIFIED NUCLEOSIDES
REMARK 900 AT POSITION 34 AND 37. PSEUDOURIDINE IS PRESENT AT POSTION 39
REMARK 900 RELATED ID: 1BZ2 RELATED DB: PDB
REMARK 900 THE SAME ANTICODON LOOP SEQUENCE BUT WITHOUT MODIFIED NUCLEOSIDES
REMARK 900 AT POSITION 34, 37 OR 39
DBREF 1FL8 A 27 43 PDB 1FL8 1FL8 27 43
SEQRES 1 A 17 U C A G A C U U8U U U T6A A PSU
SEQRES 2 A 17 C U G A
MODRES 1FL8 U8U A 34 U
MODRES 1FL8 T6A A 37 A
MODRES 1FL8 PSU A 39 U PSEUDOURIDINE-5'-MONOPHOSPHATE
HET U8U A 34 39
HET T6A A 37 49
HET PSU A 39 30
HETNAM U8U 5-METHYLAMINOMETHYL-2-THIOURIDINE-5'-MONOPHOSPHATE
HETNAM T6A N-[N-(9-B-D-RIBOFURANOSYLPURIN-6-YL)
HETNAM 2 T6A CARBAMOYL]THREONINE-5'-MONOPHOSPHATE
HETNAM PSU PSEUDOURIDINE-5'-MONOPHOSPHATE
HETSYN T6A N-(NEBULARIN-6-YLCARBAMOYL)-L-THREONINE-5'-
HETSYN 2 T6A MONOPHOSPHATE
FORMUL 1 U8U C11 H18 N3 O8 P S
FORMUL 1 T6A C15 H21 N6 O11 P
FORMUL 1 PSU C9 H13 N2 O9 P
LINK O3' U A 33 P U8U A 34 1555 1555 1.61
LINK O3' U8U A 34 P U A 35 1555 1555 1.62
LINK O3' U A 36 P T6A A 37 1555 1555 1.62
LINK O3' T6A A 37 P A A 38 1555 1555 1.62
LINK O3' A A 38 P PSU A 39 1555 1555 1.62
LINK O3' PSU A 39 P C A 40 1555 1555 1.62
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 - 23 20 Bytes