Header list of 8psh.pdb file
Complete list - 16 202 Bytes
HEADER DNA-RNA HYBRID 13-OCT-97 8PSH TITLE HIGH RESOLUTION NMR STRUCTURE OF THE STEREOREGULAR (ALL-RP)- TITLE 2 PHOSPHOROTHIOATE-DNA/RNA HYBRID D TITLE 3 (G*PS*C*PS*G*PS*T*PS*C*PS*A*PS*G*PS*G)R(CCUGACGC), MINIMIZED AVERAGE TITLE 4 STRUCTURE COMPND MOL_ID: 1; COMPND 2 MOLECULE: DNA (5'-D(*DGP*(SC)P*(GS)P*(PST)P*(SC)P*(AS)P*(GS)P*(GS))- COMPND 3 3'); COMPND 4 CHAIN: A; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: RNA (5'-R(*CP*CP*UP*GP*AP*CP*GP*C)-3'); COMPND 8 CHAIN: B; COMPND 9 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 MOL_ID: 2; SOURCE 4 SYNTHETIC: YES KEYWDS OLIGONUCLEOTIDE, DNA-RNA HYBRID, PHOSPHOROTHIOATE, THIONUCLEOTIDE, KEYWDS 2 ANTISENSE EXPDTA SOLUTION NMR AUTHOR M.BACHELIN,G.HESSLER,G.KURZ,J.G.HACIA,P.B.DERVAN,H.KESSLER REVDAT 3 16-MAR-22 8PSH 1 REMARK LINK REVDAT 2 24-FEB-09 8PSH 1 VERSN REVDAT 1 27-MAY-98 8PSH 0 JRNL AUTH M.BACHELIN,G.HESSLER,G.KURZ,J.G.HACIA,P.B.DERVAN,H.KESSLER JRNL TITL STRUCTURE OF A STEREOREGULAR PHOSPHOROTHIOATE DNA/RNA DUPLEX JRNL REF NAT.STRUCT.BIOL. V. 5 271 1998 JRNL REFN ISSN 1072-8368 JRNL PMID 9546216 JRNL DOI 10.1038/NSB0498-271 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.BACHELIN REMARK 1 REF THESIS 1997 REMARK 1 PUBL MUNCHEN : TECHNISCHE UNIVERSITAT MUNCHEN (THESIS) REMARK 1 REFN REMARK 1 REFERENCE 2 REMARK 1 AUTH G.KURZ REMARK 1 REF THESIS 1995 REMARK 1 PUBL MUNCHEN : TECHNISCHE UNIVERSITAT MUNCHEN (THESIS) REMARK 1 REFN REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DISCOVER 2.97 REMARK 3 AUTHORS : MSI REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 8PSH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000180013. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 295 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; P.E.COSY; TOCSY; P-H COSY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : AMX600; DMX600; AMX500 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : BRUKER UXNMR UXNMR, TRIAD SYBYL REMARK 210 SYBYL, MARDIGRAS, MSI INSIGHT II REMARK 210 II REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 50 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : AVERAGE OF ALL STRUCTURES 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: DIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 DG A 1 O4' - C1' - N9 ANGL. DEV. = 2.0 DEGREES 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 A B 13 0.08 SIDE CHAIN REMARK 500 G B 15 0.09 SIDE CHAIN 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 AS A 6 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DG A 1 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GS A 3 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GS A 7 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GS A 8 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PST A 4 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SC A 2 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SC A 5 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 8DRH RELATED DB: PDB REMARK 900 MINIMIZED AVERAGE STRUCTURE DBREF 8PSH A 1 8 PDB 8PSH 8PSH 1 8 DBREF 8PSH B 9 16 PDB 8PSH 8PSH 9 16 SEQRES 1 A 8 DG SC GS PST SC AS GS GS SEQRES 1 B 8 C C U G A C G C MODRES 8PSH SC A 2 DC 2-DEOXY-CYTIDINE-5'-THIOPHOSPHORATE MODRES 8PSH GS A 3 DG GUANOSINE-5'-THIO-MONOPHOSPHATE MODRES 8PSH PST A 4 DT THYMIDINE-5'-THIOPHOSPHATE MODRES 8PSH SC A 5 DC 2-DEOXY-CYTIDINE-5'-THIOPHOSPHORATE MODRES 8PSH AS A 6 DA MODRES 8PSH GS A 7 DG GUANOSINE-5'-THIO-MONOPHOSPHATE MODRES 8PSH GS A 8 DG GUANOSINE-5'-THIO-MONOPHOSPHATE HET SC A 2 30 HET GS A 3 33 HET PST A 4 32 HET SC A 5 30 HET AS A 6 32 HET GS A 7 33 HET GS A 8 34 HETNAM SC 2-DEOXY-CYTIDINE-5'-THIOPHOSPHORATE HETNAM GS GUANOSINE-5'-THIO-MONOPHOSPHATE HETNAM PST THYMIDINE-5'-THIOPHOSPHATE HETNAM AS 2-DEOXY-ADENOSINE -5'-THIO-MONOPHOSPHATE FORMUL 1 SC 2(C9 H14 N3 O6 P S) FORMUL 1 GS 3(C10 H14 N5 O6 P S) FORMUL 1 PST C10 H15 N2 O7 P S FORMUL 1 AS C10 H14 N5 O5 P S LINK O3' DG A 1 P SC A 2 1555 1555 1.62 LINK O3' SC A 2 P GS A 3 1555 1555 1.62 LINK O3' GS A 3 P PST A 4 1555 1555 1.62 LINK O3' PST A 4 P SC A 5 1555 1555 1.62 LINK O3' SC A 5 P AS A 6 1555 1555 1.62 LINK O3' AS A 6 P GS A 7 1555 1555 1.63 LINK O3' GS A 7 P GS A 8 1555 1555 1.62 SITE 1 AC1 4 SC A 5 GS A 7 U B 11 G B 12 SITE 1 AC2 2 SC A 2 C B 16 SITE 1 AC3 5 SC A 2 PST A 4 A B 13 C B 14 SITE 2 AC3 5 G B 15 SITE 1 AC4 4 AS A 6 GS A 8 C B 10 U B 11 SITE 1 AC5 3 GS A 7 C B 9 C B 10 SITE 1 AC6 3 GS A 3 SC A 5 A B 13 SITE 1 AC7 3 DG A 1 GS A 3 G B 15 SITE 1 AC8 4 PST A 4 AS A 6 G B 12 A B 13 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
Complete list - 16 202 Bytes