Header list of 1f7i.pdb file
Complete list - 16 20 Bytes
HEADER RNA 27-JUN-00 1F7I
TITLE SOLUTION STRUCTURE OF THE RNASE P RNA (M1 RNA) P4 STEM C70U MUTANT
TITLE 2 OLIGORIBONUCLEOTIDE COMPLEXED WITH COBALT (III) HEXAMINE ,NMR,
TITLE 3 ENSEMBLE OF 12 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RNASE P RNA RIBOZYME, P4 DOMAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: P4 STEM;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SYNTHESIZED FROM DNA OLIGONUCLEOTIDE TEMPLATE BY T7
SOURCE 4 RNA POLYMERASE
KEYWDS RIBONUCLEASE P, RIBOZYME, TRANSFER RNA PROCESSING, P4 STEM, C70U
KEYWDS 2 MUTANT, METAL BINDING SITE, METAL COMPLEX, COBALT (III) HEXAMMINE
KEYWDS 3 COMPLEX, RNA
EXPDTA SOLUTION NMR
NUMMDL 12
AUTHOR M.SCHMITZ,I.TINOCO JR.
REVDAT 3 16-FEB-22 1F7I 1 REMARK
REVDAT 2 24-FEB-09 1F7I 1 VERSN
REVDAT 1 09-OCT-00 1F7I 0
JRNL AUTH M.SCHMITZ,I.TINOCO JR.
JRNL TITL SOLUTION STRUCTURE AND METAL-ION BINDING OF THE P4 ELEMENT
JRNL TITL 2 FROM BACTERIAL RNASE P RNA.
JRNL REF RNA V. 6 1212 2000
JRNL REFN ISSN 1355-8382
JRNL PMID 10999599
JRNL DOI 10.1017/S1355838200000881
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.1, X-PLOR 3.841
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 268 NOE DERIVED DISTANCE CONSTRAINTS, 171 DIHEDRAL RESTRAINTS
REMARK 3 AND 49 DISTANCE RESTRAINTS FROM HYDROGEN BONDS. 12 NOE DERIVED
REMARK 3 INTERMOLECULAR DISTANCE CONSTRAINTS WERE USED TO LOCALIZE THE
REMARK 3 BOUND COBALT(III) HEXAMMINE. THE 12 STRUCTURES WITH LOWEST NOE
REMARK 3 AND DIHEDRAL ANGLE VIOLATION ENERGIES ARE PRESENTED
REMARK 4
REMARK 4 1F7I COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-00.
REMARK 100 THE DEPOSITION ID IS D_1000011338.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 288; 288; 288; 288
REMARK 210 PH : 6.5; 6.5; 6.5; 6.5
REMARK 210 IONIC STRENGTH : 100 MM NA; 100 MM NA; 100 MM NA,
REMARK 210 10 MM MG; 100 MM NA, 3 MM CO(NH3)
REMARK 210 6
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT;
REMARK 210 AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM P4M RNA; 100 MM SODIUM
REMARK 210 CHLORIDE; 10 MM PHOSPHATE BUFFER;
REMARK 210 90% H2O, 10% D2O; 2 MM P4M RNA;
REMARK 210 100 MM SODIUM CHLORIDE; 10 MM
REMARK 210 PHOSPHATE BUFFER; 99.96% D2O; 2
REMARK 210 MM P4M RNA; 100 MM SODIUM
REMARK 210 CHLORIDE; 10 MM MAGNESIUM
REMARK 210 CHLORIDE; 10 MM PHOSPHATE BUFFER;
REMARK 210 90% H2O, 10% D2O; 2 MM P4M RNA;
REMARK 210 100 MM SODIUM CHLORIDE; 3 MM
REMARK 210 HEXAMMINE COBALT CHLORIDE; 10 MM
REMARK 210 PHOSPHATE BUFFER; 90% H2O, 10%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; 31P-1H-COSY;
REMARK 210 13C-1H-HMQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 95, X-PLOR 3.841
REMARK 210 METHOD USED : RESTRAINED MOLECULAR DYNAMICS;
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 12
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 7
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES AND 13C AND 31P HETERONUCLEAR TECHNIQUES
REMARK 210 AT NATURAL ABUNDANCE. DISTANCE CONSTRAINTS DERIVED FROM
REMARK 210 INTERMOLECULAR NOE CROSSPEAKS BETWEEN RNA PROTONS AND COBALT
REMARK 210 (III) HEXAMMINE PROTONS WERE USED TO DETERMINE THE SITE OF
REMARK 210 COBALT (III) HEXAMMINE BINDING IN THE COMPLEX STRUCTURE
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 H41 C A 8 O6 G A 21 1.59
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 NCO A 28
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1F79 RELATED DB: PDB
REMARK 900 CONTAINS THE AVERAGE COMPLEX STRUCTURE CALCULATED FROM THIS ENSEMBLE
DBREF 1F7I A 1 27 PDB 1F7I 1F7I 1 27
SEQRES 1 A 27 G G A A G U U C G G U C U
SEQRES 2 A 27 U C G G A C C G G C U U C
SEQRES 3 A 27 C
HET NCO A 28 25
HETNAM NCO COBALT HEXAMMINE(III)
FORMUL 2 NCO CO H18 N6 3+
SITE 1 AC1 4 G A 5 U A 6 G A 21 G A 22
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