Header list of 1mxk.pdb file
Complete list - 23 20 Bytes
HEADER DNA 02-OCT-02 1MXK
TITLE NMR STRUCTURE OF HO2-CO(III)BLEOMYCIN A(2) BOUND TO D(GGAAGCTTCC)(2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-D(*GP*GP*AP*AP*GP*CP*TP*TP*CP*C)-3';
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES
KEYWDS DRUG-DNA COMPLEX, COBALT(III), DNA
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR C.ZHAO,C.XIA,Q.MAO,H.FORSTERLING,E.DEROSE,W.E.ANTHOLINE,
AUTHOR 2 W.K.SUBCZYNSKI,D.H.PETERING
REVDAT 3 23-FEB-22 1MXK 1 REMARK LINK
REVDAT 2 24-FEB-09 1MXK 1 VERSN
REVDAT 1 16-OCT-02 1MXK 0
JRNL AUTH C.ZHAO,C.XIA,Q.MAO,H.FORSTERLING,E.DEROSE,W.E.ANTHOLINE,
JRNL AUTH 2 W.K.SUBCZYNSKI,D.H.PETERING
JRNL TITL STRUCTURES OF HO(2)-CO(III)BLEOMYCIN A(2) BOUND TO
JRNL TITL 2 D(GAGCTC)(2) AND D(GGAAGCTTCC)(2): STRUCTURE-REACTIVITY
JRNL TITL 3 RELATIONSHIPS OF CO AND FE BLEOMYCINS
JRNL REF J.INORG.BIOCHEM. V. 91 259 2002
JRNL REFN ISSN 0162-0134
JRNL PMID 12121784
JRNL DOI 10.1016/S0162-0134(02)00420-8
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 1.3, X-PLOR 3.1
REMARK 3 AUTHORS : BRUKER INSTR. (XWINNMR), AXEL BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE IS BASED ON 424 DISTANCE
REMARK 3 RESTRAINTS (333 INTRAMOLECULAR DNA, 66 INTRAMOLECULAR BLEOMYCIN
REMARK 3 AND 25 INTERMOLECULAR).
REMARK 4
REMARK 4 1MXK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-OCT-02.
REMARK 100 THE DEPOSITION ID IS D_1000017282.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 0.1 M NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2MM BLEOMYCIN/DNA COMPLEX; 20 MM
REMARK 210 PHOSPHATE BUFFER; 0.1 M NACL;
REMARK 210 2MM BLEOMYCIN/DNA COMPLEX; 20 MM
REMARK 210 PHOSPHATE BUFFER; 0.1 M NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY;
REMARK 210 31P/1H-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 : FELIX 2.3
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS
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: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES
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: 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 O1 PEO A 23 HNK BLM B 21 1.39
REMARK 500 O2 DC A 9 H21 DG B 12 1.51
REMARK 500 H21 DG A 1 O2 DC B 20 1.56
REMARK 500 O2 DC A 10 H21 DG B 11 1.57
REMARK 500 H21 DG A 2 O2 DC B 19 1.58
REMARK 500 H41 DC A 6 O6 DG B 15 1.59
REMARK 500 O6 DG A 5 H41 DC B 16 1.60
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 DG A 1 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 DG A 1 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 DG A 1 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 DG A 2 O4' - C1' - N9 ANGL. DEV. = 3.1 DEGREES
REMARK 500 DG A 2 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 DG A 2 C8 - N9 - C4 ANGL. DEV. = -2.5 DEGREES
REMARK 500 DA A 3 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 DA A 3 N7 - C8 - N9 ANGL. DEV. = 3.8 DEGREES
REMARK 500 DA A 4 O4' - C1' - N9 ANGL. DEV. = 2.8 DEGREES
REMARK 500 DA A 4 N7 - C8 - N9 ANGL. DEV. = 3.9 DEGREES
REMARK 500 DG A 5 O4' - C1' - N9 ANGL. DEV. = 4.2 DEGREES
REMARK 500 DG A 5 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 DG A 5 C8 - N9 - C4 ANGL. DEV. = -2.5 DEGREES
REMARK 500 DC A 6 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
REMARK 500 DT A 7 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DT A 7 C6 - C5 - C7 ANGL. DEV. = -3.8 DEGREES
REMARK 500 DT A 8 O4' - C1' - N1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 DC A 9 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES
REMARK 500 DC A 10 O4' - C1' - N1 ANGL. DEV. = 2.2 DEGREES
REMARK 500 DG B 11 O4' - C1' - N9 ANGL. DEV. = 2.9 DEGREES
REMARK 500 DG B 11 N7 - C8 - N9 ANGL. DEV. = 4.5 DEGREES
REMARK 500 DG B 11 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 DG B 12 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DG B 12 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 DG B 12 C8 - N9 - C4 ANGL. DEV. = -2.6 DEGREES
REMARK 500 DA B 13 O4' - C1' - N9 ANGL. DEV. = 2.6 DEGREES
REMARK 500 DA B 13 N7 - C8 - N9 ANGL. DEV. = 3.9 DEGREES
REMARK 500 DA B 14 O4' - C1' - N9 ANGL. DEV. = 3.4 DEGREES
REMARK 500 DA B 14 N7 - C8 - N9 ANGL. DEV. = 3.7 DEGREES
REMARK 500 DG B 15 O4' - C1' - N9 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DG B 15 N7 - C8 - N9 ANGL. DEV. = 4.6 DEGREES
REMARK 500 DG B 15 C8 - N9 - C4 ANGL. DEV. = -2.7 DEGREES
REMARK 500 DC B 16 O4' - C1' - N1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 DT B 17 O4' - C1' - N1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 DT B 18 O4' - C1' - N1 ANGL. DEV. = 2.5 DEGREES
REMARK 500 DC B 19 O4' - C1' - N1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 DC B 20 O4' - C1' - N1 ANGL. DEV. = 2.7 DEGREES
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 3CO A 22 CO
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 PEO A 23 O1
REMARK 620 2 PEO A 23 O2 27.3
REMARK 620 3 BLM B 21 NG 89.7 72.8
REMARK 620 4 BLM B 21 NC 90.7 68.1 83.8
REMARK 620 5 BLM B 21 NB 177.3 150.7 90.5 86.6
REMARK 620 6 BLM B 21 NH 92.2 110.9 84.3 167.7 90.5
REMARK 620 7 BLM B 21 NJ 85.4 104.2 173.4 100.7 94.6 91.5
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3CO A 22
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BLM B 21
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEO A 23
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MTG RELATED DB: PDB
REMARK 900 1MTG IS HO2-CO(III)BLEOMYCIN-A(2) BOUND TO D(GAGCTC)(2)
DBREF 1MXK A 1 10 PDB 1MXK 1MXK 1 10
DBREF 1MXK B 11 20 PDB 1MXK 1MXK 11 20
SEQRES 1 A 10 DG DG DA DA DG DC DT DT DC DC
SEQRES 1 B 10 DG DG DA DA DG DC DT DT DC DC
HET 3CO A 22 1
HET PEO A 23 3
HET BLM B 21 179
HETNAM 3CO COBALT (III) ION
HETNAM PEO HYDROGEN PEROXIDE
HETNAM BLM BLEOMYCIN A2
HETSYN BLM N1-[3-(DIMETHYLSULFONIO)-PROPYL]BLEOMYCINAMIDE
FORMUL 3 3CO CO 3+
FORMUL 4 PEO H2 O2
FORMUL 5 BLM C55 H85 N17 O21 S3
LINK CO 3CO A 22 O1 PEO A 23 1555 1555 1.84
LINK CO 3CO A 22 O2 PEO A 23 1555 1555 2.75
LINK CO 3CO A 22 NG BLM B 21 1555 1555 1.84
LINK CO 3CO A 22 NC BLM B 21 1555 1555 2.06
LINK CO 3CO A 22 NB BLM B 21 1555 1555 2.15
LINK CO 3CO A 22 NH BLM B 21 1555 1555 1.93
LINK CO 3CO A 22 NJ BLM B 21 1555 1555 2.00
SITE 1 AC1 2 PEO A 23 BLM B 21
SITE 1 AC2 12 DG A 5 DC A 6 DT A 7 3CO A 22
SITE 2 AC2 12 PEO A 23 DA B 13 DA B 14 DG B 15
SITE 3 AC2 12 DC B 16 DT B 17 DT B 18 DC B 19
SITE 1 AC3 2 3CO A 22 BLM B 21
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 - 23 20 Bytes