Header list of 1p7a.pdb file
Complete list - 28 20 Bytes
HEADER DNA BINDING PROTEIN 30-APR-03 1P7A
TITLE SOLUTION STRUCTURE OF THE THIRD ZINC FINGER FROM BKLF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KRUPPEL-LIKE FACTOR 3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 9-37;
COMPND 5 SYNONYM: BF3, BKLF;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: BKLF;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS CLASSICAL ZINC FINGER, KRUPPEL-LIKE, TRANSCRIPTION FACTOR, DNA
KEYWDS 2 BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR R.J.Y.SIMPSON,E.D.CRAM,R.CZOLIJ,J.M.MATTHEWS,M.CROSSLEY,J.P.MACKAY
REVDAT 3 28-DEC-16 1P7A 1 TITLE VERSN
REVDAT 2 24-FEB-09 1P7A 1 VERSN
REVDAT 1 30-DEC-03 1P7A 0
JRNL AUTH R.J.SIMPSON,E.D.CRAM,R.CZOLIJ,J.M.MATTHEWS,M.CROSSLEY,
JRNL AUTH 2 J.P.MACKAY
JRNL TITL CCHX ZINC FINGER DERIVATIVES RETAIN THE ABILITY TO BIND
JRNL TITL 2 ZN(II) AND MEDIATE PROTEIN-DNA INTERACTIONS.
JRNL REF J.BIOL.CHEM. V. 278 28011 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12736264
JRNL DOI 10.1074/JBC.M211146200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : ARIA 1.1.2
REMARK 3 AUTHORS : LINGE ET AL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURE CALCULATIONS WERE PERFORMED
REMARK 3 USING THE PACKAGE ARIA 1.1 (AMBIGUOUS RESTRAINTS IN ITERATIVE
REMARK 3 ASSIGNMENT)> FINAL STRUCTURES ARE BASED ON 719 UNAMBIGUOUS NOE-
REMARK 3 DERIVED DISTANCE CONSRAINTS, 6 SETS OF AMBIGUOUS NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS AND 28 ADDITIONAL DIHEDRAL ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1P7A COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-MAY-03.
REMARK 100 THE RCSB ID CODE IS RCSB019096.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 280; 280
REMARK 210 PH : 5.5; 5.5
REMARK 210 IONIC STRENGTH : NULL; NULL
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 3MM BF3; 4.5MM TCEP; 4.5MM
REMARK 210 ZNSO4; 1MM BF3 U-15N; 1.5MM TCEP;
REMARK 210 1.5MM ZNSO4
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY;
REMARK 210 HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.5, DYANA 1.5, XEASY
REMARK 210 1.3.13, ARIA 1.1.2
REMARK 210 METHOD USED : SIMULATED ANNEALING MOLECULAR
REMARK 210 DYNAMICS TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 35
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST ENERGY
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: 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: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 ARG A 4 54.02 -151.09
REMARK 500 1 SER A 6 10.95 -149.10
REMARK 500 1 LYS A 10 146.46 59.24
REMARK 500 1 ASP A 18 49.60 79.93
REMARK 500 1 ARG A 19 -154.83 -83.78
REMARK 500 1 MET A 35 -70.75 -81.00
REMARK 500 1 LEU A 36 53.36 -140.74
REMARK 500 2 SER A 2 -33.79 -143.70
REMARK 500 2 ARG A 4 -105.24 56.83
REMARK 500 2 LYS A 10 147.42 55.43
REMARK 500 2 ASP A 18 43.58 81.10
REMARK 500 2 ARG A 19 -158.38 -81.01
REMARK 500 2 SER A 20 125.67 -170.09
REMARK 500 2 LEU A 36 54.82 -109.65
REMARK 500 3 LYS A 10 148.45 56.89
REMARK 500 3 ASP A 18 39.18 77.89
REMARK 500 3 ARG A 19 -160.58 -78.49
REMARK 500 4 ARG A 4 52.28 -144.73
REMARK 500 4 LYS A 10 147.16 60.20
REMARK 500 4 ASP A 18 52.21 77.62
REMARK 500 4 ARG A 19 -146.52 -85.96
REMARK 500 5 THR A 3 -141.86 57.41
REMARK 500 5 LYS A 10 147.34 63.16
REMARK 500 5 ASP A 18 48.38 77.94
REMARK 500 5 ARG A 19 -155.62 -78.17
REMARK 500 6 SER A 2 -112.43 49.92
REMARK 500 6 LYS A 10 149.55 64.02
REMARK 500 7 SER A 2 -152.60 59.80
REMARK 500 7 THR A 7 74.61 -114.37
REMARK 500 7 LYS A 10 147.35 62.53
REMARK 500 7 ASP A 18 48.65 78.56
REMARK 500 8 THR A 3 -159.47 -129.32
REMARK 500 8 LYS A 10 147.52 63.05
REMARK 500 8 ASP A 18 18.85 83.76
REMARK 500 9 THR A 3 97.01 80.24
REMARK 500 9 SER A 6 -127.86 -93.48
REMARK 500 9 LYS A 10 147.43 69.18
REMARK 500 9 ASP A 18 50.99 70.28
REMARK 500 9 ARG A 19 -155.11 -85.40
REMARK 500 9 LEU A 36 53.27 -108.19
REMARK 500 10 THR A 3 138.91 -39.83
REMARK 500 10 ARG A 4 44.04 -143.28
REMARK 500 10 LYS A 10 146.06 67.61
REMARK 500 10 ASP A 18 34.03 81.32
REMARK 500 10 LEU A 36 52.42 -143.98
REMARK 500 11 LYS A 10 147.13 71.40
REMARK 500 11 ASP A 18 49.12 75.47
REMARK 500 11 ARG A 19 -148.02 -84.59
REMARK 500 12 LYS A 10 148.13 69.03
REMARK 500 12 ASP A 18 24.43 84.23
REMARK 500
REMARK 500 THIS ENTRY HAS 78 RAMACHANDRAN OUTLIERS.
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 1 ZN A 38 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 30 NE2
REMARK 620 2 HIS A 34 NE2 102.5
REMARK 620 3 CYS A 14 SG 110.7 109.4
REMARK 620 4 CYS A 17 SG 112.1 110.5 111.3
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 ZN A 38
DBREF 1P7A A 7 37 UNP Q60980 KLF3_MOUSE 314 344
SEQADV 1P7A GLY A 1 UNP Q60980 CLONING ARTIFACT
SEQADV 1P7A SER A 2 UNP Q60980 CLONING ARTIFACT
SEQADV 1P7A THR A 3 UNP Q60980 CLONING ARTIFACT
SEQADV 1P7A ARG A 4 UNP Q60980 CLONING ARTIFACT
SEQADV 1P7A GLY A 5 UNP Q60980 CLONING ARTIFACT
SEQADV 1P7A SER A 6 UNP Q60980 CLONING ARTIFACT
SEQRES 1 A 37 GLY SER THR ARG GLY SER THR GLY ILE LYS PRO PHE GLN
SEQRES 2 A 37 CYS PRO ASP CYS ASP ARG SER PHE SER ARG SER ASP HIS
SEQRES 3 A 37 LEU ALA LEU HIS ARG LYS ARG HIS MET LEU VAL
HET ZN A 38 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 ARG A 23 LYS A 32 1 10
HELIX 2 2 ARG A 33 MET A 35 5 3
LINK ZN ZN A 38 NE2 HIS A 30 1555 1555 1.99
LINK ZN ZN A 38 NE2 HIS A 34 1555 1555 1.97
LINK ZN ZN A 38 SG CYS A 14 1555 1555 2.33
LINK ZN ZN A 38 SG CYS A 17 1555 1555 2.32
SITE 1 AC1 4 CYS A 14 CYS A 17 HIS A 30 HIS A 34
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 - 28 20 Bytes