Header list of 199d.pdb file
Complete list - 16 20 Bytes
HEADER DNA 01-DEC-94 199D
TITLE SOLUTION STRUCTURE OF THE MONOALKYLATED MITOMYCIN C-DNA COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DNA (5'-D(*(DI)P*CP*AP*CP*GP*TP*CP*(DI)P*T)-3');
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DNA (5'-D(*AP*CP*GP*AP*CP*GP*TP*GP*C)-3');
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: CHEMICALLY SYNTHESIZED;
SOURCE 4 MOL_ID: 2;
SOURCE 5 SYNTHETIC: YES;
SOURCE 6 OTHER_DETAILS: CHEMICALLY SYNTHESIZED
KEYWDS DNA, MITOMYCIN, DOUBLE HELIX
EXPDTA SOLUTION NMR
NUMMDL 3
AUTHOR M.SASTRY,R.FIALA,R.LIPMAN,M.TOMASZ,D.J.PATEL
REVDAT 3 16-FEB-22 199D 1 REMARK LINK
REVDAT 2 24-FEB-09 199D 1 VERSN
REVDAT 1 07-FEB-95 199D 0
JRNL AUTH M.SASTRY,R.FIALA,R.LIPMAN,M.TOMASZ,D.J.PATEL
JRNL TITL SOLUTION STRUCTURE OF THE MONOALKYLATED MITOMYCIN C-DNA
JRNL TITL 2 COMPLEX.
JRNL REF J.MOL.BIOL. V. 247 338 1995
JRNL REFN ISSN 0022-2836
JRNL PMID 7707379
JRNL DOI 10.1006/JMBI.1994.0143
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THREE STARTING STRUCTURES WERE OBTAINED
REMARK 3 BY MANUALLY DOCKING MITOMYCIN C ON A FORM AND B FORM DNA. THESE
REMARK 3 WERE SUBSEQUENTLY REFINED BY DISTANCE-RESTRAINED MOLECULAR
REMARK 3 DYNAMICS USING A SET OF INTER-PROTON DISTANCES DERIVED FROM NMR
REMARK 3 DATA. THE THREE DISTANCE-REFINED STRUCTURES WERE REFINED FURTHER
REMARK 3 USING RELAXATION-MATRIX BASED NOE INTENSITY-RESTRAINED MOLECULAR
REMARK 3 DYNAMICS. THE FINAL THREE STRUCTURES WERE OBTAINED BY TAKING THE
REMARK 3 AVERAGE COORDINATES OF THE LAST 1.5 PS OF THE DYNAMICS DURING
REMARK 3 RELAXATION MATRIX REFINEMENT AND MINIMIZED. THE R(1/6) VALUE WAS
REMARK 3 USED TO REFINE THE STRUCTURE DURING RELAXATION MATRIX
REMARK 3 REFINEMENT. THE SUMMATIONS RUN THROUGH OBSERVED, QUANTIFIABLE
REMARK 3 NOE CROSSPEAKS IN NOESY SPECTRA RECORDED IN D2O AND MIXING TIMES
REMARK 3 OF 30, 60, 90, 120, 200 AND 300 MS. THE R(1/6) FACTOR AND THE
REMARK 3 RMS DEVIATIONS FROM IDEAL GEOMETRY FOR THE THREE FINAL
REMARK 3 STRUCTURES ARE: MDL1 MDL2 MDL3 R(1/6) FACTOR 0.027 0.026 0.026
REMARK 3 BOND (ANG) 0.008 0.008 0.008 ANGLE (DEG) 2.913 2.931 2.949
REMARK 3 IMPROPER (DEG) 0.361 0.393 0.372
REMARK 4
REMARK 4 199D COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000170219.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : MOLECULAR DYNAMICS, MATRIX
REMARK 210 RELAXATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 3
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 3
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
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 1 DT A 6 C5 DT A 6 C7 0.040
REMARK 500 1 DT A 9 C5 DT A 9 C7 0.038
REMARK 500 2 DT A 6 C5 DT A 6 C7 0.042
REMARK 500 2 DT A 9 C5 DT A 9 C7 0.039
REMARK 500 3 DT A 6 C5 DT A 6 C7 0.044
REMARK 500 3 DT A 9 C5 DT A 9 C7 0.042
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 1 DC A 2 O4' - C4' - C3' ANGL. DEV. = 3.6 DEGREES
REMARK 500 1 DC A 2 O4' - C1' - C2' ANGL. DEV. = -5.0 DEGREES
REMARK 500 1 DC A 2 C3' - O3' - P ANGL. DEV. = 10.4 DEGREES
REMARK 500 1 DA A 3 O4' - C1' - N9 ANGL. DEV. = -5.2 DEGREES
REMARK 500 1 DA A 3 C3' - O3' - P ANGL. DEV. = 9.1 DEGREES
REMARK 500 1 DC A 4 C4' - C3' - C2' ANGL. DEV. = -4.5 DEGREES
REMARK 500 1 DC A 4 O4' - C1' - C2' ANGL. DEV. = -5.6 DEGREES
REMARK 500 1 DC A 4 N1 - C2 - O2 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 DG A 5 O4' - C1' - C2' ANGL. DEV. = -5.3 DEGREES
REMARK 500 1 DG A 5 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES
REMARK 500 1 DT A 6 O4' - C1' - N1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 1 DC A 7 O4' - C1' - N1 ANGL. DEV. = 2.6 DEGREES
REMARK 500 1 DA B 10 C1' - O4' - C4' ANGL. DEV. = -9.1 DEGREES
REMARK 500 1 DA B 10 O4' - C1' - C2' ANGL. DEV. = -6.0 DEGREES
REMARK 500 1 DA B 10 O4' - C1' - N9 ANGL. DEV. = 6.1 DEGREES
REMARK 500 1 DG B 12 C5' - C4' - O4' ANGL. DEV. = 6.7 DEGREES
REMARK 500 1 DG B 12 O4' - C1' - C2' ANGL. DEV. = -5.6 DEGREES
REMARK 500 1 DG B 12 O4' - C1' - N9 ANGL. DEV. = 6.5 DEGREES
REMARK 500 1 DC B 14 O4' - C1' - N1 ANGL. DEV. = -4.3 DEGREES
REMARK 500 1 DC B 14 N1 - C2 - O2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 DG B 15 C5' - C4' - O4' ANGL. DEV. = 7.1 DEGREES
REMARK 500 1 DG B 15 O4' - C1' - C2' ANGL. DEV. = -6.9 DEGREES
REMARK 500 1 DG B 15 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 1 DT B 16 O4' - C1' - C2' ANGL. DEV. = -4.8 DEGREES
REMARK 500 1 DT B 16 O4' - C1' - N1 ANGL. DEV. = 8.7 DEGREES
REMARK 500 1 DG B 17 O4' - C1' - N9 ANGL. DEV. = 5.7 DEGREES
REMARK 500 1 DC B 18 C4' - C3' - C2' ANGL. DEV. = -5.1 DEGREES
REMARK 500 1 DC B 18 O4' - C1' - N1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 2 DC A 2 O4' - C4' - C3' ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 DC A 2 O4' - C1' - C2' ANGL. DEV. = -5.3 DEGREES
REMARK 500 2 DC A 4 O4' - C1' - C2' ANGL. DEV. = -7.9 DEGREES
REMARK 500 2 DC A 4 O4' - C1' - N1 ANGL. DEV. = 4.5 DEGREES
REMARK 500 2 DC A 4 N1 - C2 - O2 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 DG A 5 C4' - C3' - C2' ANGL. DEV. = -4.3 DEGREES
REMARK 500 2 DG A 5 O4' - C1' - C2' ANGL. DEV. = -5.2 DEGREES
REMARK 500 2 DT A 6 O4' - C1' - N1 ANGL. DEV. = 5.0 DEGREES
REMARK 500 2 DC A 7 O4' - C1' - N1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 DA B 10 C1' - O4' - C4' ANGL. DEV. = -9.3 DEGREES
REMARK 500 2 DA B 10 O4' - C1' - C2' ANGL. DEV. = -4.9 DEGREES
REMARK 500 2 DA B 10 O4' - C1' - N9 ANGL. DEV. = 6.4 DEGREES
REMARK 500 2 DA B 10 C3' - O3' - P ANGL. DEV. = 8.8 DEGREES
REMARK 500 2 DG B 12 C5' - C4' - O4' ANGL. DEV. = 8.3 DEGREES
REMARK 500 2 DG B 12 O4' - C1' - C2' ANGL. DEV. = -5.4 DEGREES
REMARK 500 2 DG B 12 C3' - O3' - P ANGL. DEV. = 10.5 DEGREES
REMARK 500 2 DG B 15 O4' - C1' - C2' ANGL. DEV. = -6.2 DEGREES
REMARK 500 2 DG B 15 O4' - C1' - N9 ANGL. DEV. = 2.1 DEGREES
REMARK 500 2 DT B 16 O4' - C1' - N1 ANGL. DEV. = 12.1 DEGREES
REMARK 500 2 DG B 17 O4' - C1' - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 2 DC B 18 O4' - C1' - N1 ANGL. DEV. = 2.1 DEGREES
REMARK 500 3 DI A 1 C3' - O3' - P ANGL. DEV. = 7.2 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 74 ANGLE DEVIATIONS.
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 MOC A 19
DBREF 199D A 1 9 PDB 199D 199D 1 9
DBREF 199D B 10 18 PDB 199D 199D 10 18
SEQRES 1 A 9 DI DC DA DC DG DT DC DI DT
SEQRES 1 B 9 DA DC DG DA DC DG DT DG DC
HET MOC A 19 37
HETNAM MOC CARBAMIC ACID 2,6-DIAMINO-5-METHYL-4,7-DIOXO-2,3,4,7-
HETNAM 2 MOC TETRAHYDRO-1H-3A-AZA-CYCLOPENTA[A]INDEN-8-YLMETHYL
HETNAM 3 MOC ESTER
FORMUL 3 MOC C14 H16 N4 O4
LINK N2 DG A 5 C1 MOC A 19 1555 1555 1.43
SITE 1 AC1 6 DG A 5 DT A 6 DC A 7 DC B 14
SITE 2 AC1 6 DG B 15 DT B 16
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