Header list of 1xrw.pdb file
Complete list - 20 201 Bytes
HEADER DNA 16-OCT-04 1XRW
TITLE SOLUTION STRUCTURE OF A PLATINUM-ACRIDINE MODIFIED OCTAMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-D(*CP*CP*TP*CP*GP*TP*CP*C)-3';
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: 5'-D(*GP*GP*AP*CP*GP*AP*GP*G)-3';
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 SYNTHETIC: YES
KEYWDS PLATINUM, ACRIDINE, DUAL BINDING MODE, MAJOR GROOVE, UNWINDING, DNA
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR H.BARUAH,M.W.WRIGHT,U.BIERBACH
REVDAT 3 20-APR-16 1XRW 1 FORMUL HETATM VERSN
REVDAT 2 24-FEB-09 1XRW 1 VERSN
REVDAT 1 03-MAY-05 1XRW 0
JRNL AUTH H.BARUAH,M.W.WRIGHT,U.BIERBACH
JRNL TITL SOLUTION STRUCTURAL STUDY OF A DNA DUPLEX CONTAINING THE
JRNL TITL 2 GUANINE-N7 ADDUCT FORMED BY A CYTOTOXIC PLATINUM-ACRIDINE
JRNL TITL 3 HYBRID AGENT
JRNL REF BIOCHEMISTRY V. 44 6059 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 15835895
JRNL DOI 10.1021/BI050021B
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISCOVER 2000
REMARK 3 AUTHORS : ACCELRYS
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1XRW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-OCT-04.
REMARK 100 THE RCSB ID CODE IS RCSB030695.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 10 MM NAH2PO4, 10 MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 3.5MM MODIFIED DUPLEX, 10 MM
REMARK 210 PHOSPHATE BUFFER, 10MM NACL, 100%
REMARK 210 D2O OR 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY; 2D TOCSY; 2D NOESY; 1H
REMARK 210 -31P COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, FELIX 2000,
REMARK 210 MARDIGRAS 3.2, CORMA 5.2
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS,
REMARK 210 MATRIX RELAXATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
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 LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 DG A 5 N1 DG A 5 C2 0.090
REMARK 500 DG A 5 C6 DG A 5 N1 -0.050
REMARK 500 DG A 5 C5 DG A 5 N7 0.057
REMARK 500 DG A 5 N7 DG A 5 C8 0.132
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 DC A 1 O4' - C1' - N1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 DC A 2 O4' - C1' - N1 ANGL. DEV. = 2.9 DEGREES
REMARK 500 DT A 3 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DG A 5 O4' - C1' - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 DG A 5 C6 - N1 - C2 ANGL. DEV. = -4.3 DEGREES
REMARK 500 DG A 5 C5 - C6 - N1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 DG A 5 C4 - C5 - N7 ANGL. DEV. = 4.6 DEGREES
REMARK 500 DG A 5 C5 - N7 - C8 ANGL. DEV. = -6.2 DEGREES
REMARK 500 DG A 5 C8 - N9 - C4 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DG A 5 C6 - C5 - N7 ANGL. DEV. = -4.9 DEGREES
REMARK 500 DT A 6 O4' - C1' - N1 ANGL. DEV. = 4.8 DEGREES
REMARK 500 DG A 5 C3' - O3' - P ANGL. DEV. = -8.4 DEGREES
REMARK 500 DC A 8 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 DG B 1 O4' - C1' - N9 ANGL. DEV. = 3.4 DEGREES
REMARK 500 DG B 2 O4' - C1' - N9 ANGL. DEV. = 2.8 DEGREES
REMARK 500 DG B 5 O4' - C1' - N9 ANGL. DEV. = 3.2 DEGREES
REMARK 500 DA B 6 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DG B 7 O4' - C1' - N9 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DG B 8 O4' - C1' - N9 ANGL. DEV. = 2.2 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 DG A 5 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 2PT B 20 PT
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 DG A 5 N7
REMARK 620 2 2PT B 20 S 82.5
REMARK 620 3 2PT B 20 N5 93.1 175.7
REMARK 620 4 2PT B 20 N4 174.4 100.7 83.6
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2PT B 20
DBREF 1XRW A 1 8 PDB 1XRW 1XRW 1 8
DBREF 1XRW B 1 8 PDB 1XRW 1XRW 1 8
SEQRES 1 A 8 DC DC DT DC DG DT DC DC
SEQRES 1 B 8 DG DG DA DC DG DA DG DG
HET 2PT B 20 57
HETNAM 2PT 1-[2-(ACRIDIN-9-YLAMINO)ETHYL]-1,3-DIMETHYLTHIOUREA-
HETNAM 2 2PT PLATINUM(II)-ETHANE-1,2-DIAMINE
FORMUL 3 2PT C20 H29 N6 PT S 3+
LINK N7 DG A 5 PT 2PT B 20 1555 1555 2.04
SITE 1 AC1 5 DC A 4 DG A 5 DT A 6 DC B 4
SITE 2 AC1 5 DG B 5
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 - 20 201 Bytes