Header list of 1r2p.pdb file
Complete list - 2 20 Bytes
HEADER RNA 29-SEP-03 1R2P
TITLE SOLUTION STRUCTURE OF DOMAIN 5 FROM THE AI5(GAMMA) GROUP II INTRON
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 34-MER;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DOMAIN 5 OF THE AI5(GAMMA) GROUP II INTRON;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SEQUENCE OCCURS NATURALLY IN SACCHAROMYCES CEREVISIAE
SOURCE 4 (BAKER'S YEAST) AND WAS SYNTHESIZED IN VITRO USING T7 RNA POLYMERASE
SOURCE 5 AND SYNTHETIC DNA OLIGONUCLEOTIDES.
KEYWDS RNA HAIRPIN, TETRALOOP, BULGE, METAL ION, MAGNESIUM, RNA
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR R.K.O.SIGEL,D.G.SASHITAL,D.L.ABRAMOVITZ,A.G.PALMER III,S.E.BUTCHER,
AUTHOR 2 A.M.PYLE
REVDAT 3 02-MAR-22 1R2P 1 REMARK
REVDAT 2 24-FEB-09 1R2P 1 VERSN
REVDAT 1 03-FEB-04 1R2P 0
JRNL AUTH R.K.SIGEL,D.G.SASHITAL,D.L.ABRAMOVITZ,A.G.PALMER,
JRNL AUTH 2 S.E.BUTCHER,A.M.PYLE
JRNL TITL SOLUTION STRUCTURE OF DOMAIN 5 OF A GROUP II INTRON RIBOZYME
JRNL TITL 2 REVEALS A NEW RNA MOTIF.
JRNL REF NAT.STRUCT.MOL.BIOL. V. 11 187 2004
JRNL REFN ISSN 1545-9993
JRNL PMID 14745440
JRNL DOI 10.1038/NSMB717
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1, CNS 1.1
REMARK 3 AUTHORS : BRUNGER ET. AL. (CNS), BRUNGER ET. AL. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES BASED ON 678 NOE-DERIVED
REMARK 3 DISTANCE RESTRAINTS, 261 DIHEDRAL RESTRAINTS, 72 HYDROGEN BOND
REMARK 3 RESTRAINTS, AND 24 RESIDUAL DIPOLAR COUPLING RESTRAINTS
REMARK 4
REMARK 4 1R2P COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-OCT-03.
REMARK 100 THE DEPOSITION ID IS D_1000020362.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 278; 298; 308; 291; 303
REMARK 210 PH : 6.5; 6.5; 6.5; 6.5; 6.5
REMARK 210 IONIC STRENGTH : 100MM KCL; 100MM KCL; 100MM KCL;
REMARK 210 100MM KCL; 100MM KCL
REMARK 210 PRESSURE : NULL; NULL; NULL; NULL; NULL
REMARK 210 SAMPLE CONTENTS : 0.5 - 0.7 MM D5 RNA; 0 - 200MM
REMARK 210 KCL, 0 - 20 MM MGCL2, 0.01 MM
REMARK 210 EDTA, 90% H2O, 10% D2O; 0.5 -
REMARK 210 0.7 MM D5 RNA; 0 - 200MM KCL, 0 -
REMARK 210 20 MM MGCL2, 0.01 MM EDTA,
REMARK 210 99.999% D2O; 0.5 - 0.7 MM D5 RNA,
REMARK 210 13C-15N LABELED; 100MM KCL,
REMARK 210 0.01 MM EDTA, 90% H2O, 10% D2O;
REMARK 210 0.5 - 0.7 MM D5 RNA, 13C-15N
REMARK 210 LABELED; 100MM KCL, 0.01 MM EDTA,
REMARK 210 99.999% D2O; 0.5 - 0.7 MM D5
REMARK 210 RNA, 13C-15N LABELED; 100MM KCL,
REMARK 210 0.01 MM EDTA, 17 MG/ML PF1
REMARK 210 FILAMENTOUS BACTERIOPHAGE, 90%
REMARK 210 H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 2D 1H-13C HSQC;
REMARK 210 2D 1H-1H TOCSY; 3D 1H-13C-1H
REMARK 210 HCCH TOCSY; 3D 1H-13C-1H HCCH
REMARK 210 COSY; 2D 2JHN HNN-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA, SPARKY 3, XWINNMR 2.6
REMARK 210 METHOD USED : TORSION ANGLE MOLECULAR DYNAMICS
REMARK 210 CARTESIAN SPACE SIMULATED
REMARK 210 ANNEALING AND MOLECULAR DYNAMICS
REMARK 210 RESIDUAL DIPOLAR COUPLINGS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: RESIDUAL DIPOLAR COUPLINGS WERE MEASURED USING 1H-13C HSQC
REMARK 210 COUPLED IN EITHER THE PROTON OR THE CARBON DIMENSION
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: 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 8 G A 15 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5962 RELATED DB: BMRB
REMARK 900 NMR DATA: CHEMICAL SHIFTS OF DOMAIN 5
REMARK 900 RELATED ID: 1KXK RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF A DOMAIN5 / DOMAIN 6 CONSTRUCT FROM AI5GAMMA
DBREF 1R2P A 1 34 PDB 1R2P 1R2P 1 34
SEQRES 1 A 34 G A G C C G U A U G C G A
SEQRES 2 A 34 U G A A A G U C G C A C G
SEQRES 3 A 34 U A C G G U U 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 - 2 20 Bytes