Header list of 1u86.pdb file
Complete list - 2 20 Bytes
HEADER DNA BINDING PROTEIN 05-AUG-04 1U86
TITLE 321-TW-322 INSERTION MUTANT OF THE THIRD ZINC FINGER OF BKLF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KRUPPEL-LIKE FACTOR 3;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: THIRD ZINC FINGER;
COMPND 5 SYNONYM: BASIC KRUPPEL-LIKE FACTOR, KLF3, CACCC-BOX BINDING PROTEIN
COMPND 6 BKLF, TEF-2;
COMPND 7 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 ZINC FINGER, KRUPPEL-LIKE, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR E.D.CRAM,J.P.MACKAY,J.M.MATTHEWS
REVDAT 3 02-MAR-22 1U86 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1U86 1 VERSN
REVDAT 1 23-AUG-05 1U86 0
JRNL AUTH E.D.CRAM,J.P.MACKAY,J.M.MATTHEWS
JRNL TITL SOLUTION STRUCTURES OF TRYPTOPHAN-CONTAINING CCHH ZINC
JRNL TITL 2 FINGER MUTANTS
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.5, ARIA 1.1.2
REMARK 3 AUTHORS : BRUKER (XWINNMR), LINGE ET AL (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURE CALCULATIONS WERE PERFORMED
REMARK 3 IN ARIA. THE STRUCTURES ARE BASED ON 638 NOE-DERIVED DISTANCE
REMARK 3 CONSTRAINTS AND 20 DIHEDRAL ANGLE RESTRAINTS
REMARK 4
REMARK 4 1U86 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-AUG-04.
REMARK 100 THE DEPOSITION ID IS D_1000023366.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 280
REMARK 210 PH : 5.7
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.6MM B3F+TW, 2MM TCEP, 2MM
REMARK 210 ZNSO4; 0.5MM 15N-B3F+TW, 2MM
REMARK 210 TCEP, 2MM 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 : XEASY 1.3.13, CYANA 1.0.6
REMARK 210 METHOD USED : SIMULATED ANNEALING MOLECULAR
REMARK 210 DYNAMICS, TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
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: 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
REMARK 500 REMARK: NULL
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 PHE A 8 50.29 -91.86
REMARK 500 2 PHE A 8 47.17 -92.16
REMARK 500 3 THR A 11 31.55 -83.41
REMARK 500 3 CYS A 15 -68.92 -101.16
REMARK 500 4 THR A 3 42.73 -105.75
REMARK 500 4 PHE A 8 49.81 -106.14
REMARK 500 4 CYS A 15 -68.69 -94.83
REMARK 500 4 LEU A 34 61.84 -103.09
REMARK 500 5 THR A 3 74.08 -119.27
REMARK 500 5 CYS A 15 -66.79 -93.42
REMARK 500 6 PHE A 8 44.91 -94.91
REMARK 500 6 CYS A 15 -73.11 -63.56
REMARK 500 6 ASP A 16 63.59 63.50
REMARK 500 6 LEU A 34 71.79 -112.54
REMARK 500 7 PHE A 8 56.16 -97.83
REMARK 500 7 THR A 11 32.64 -91.33
REMARK 500 7 CYS A 15 -73.07 -75.75
REMARK 500 7 LEU A 34 55.80 -116.38
REMARK 500 8 PHE A 8 54.16 -99.78
REMARK 500 8 CYS A 15 -73.54 -101.31
REMARK 500 9 PHE A 8 47.72 -101.33
REMARK 500 10 PHE A 8 53.54 -97.00
REMARK 500 10 CYS A 15 -74.07 -92.69
REMARK 500 10 ASP A 16 64.75 61.13
REMARK 500 11 THR A 3 48.75 -100.26
REMARK 500 11 PHE A 8 47.54 -92.38
REMARK 500 11 CYS A 15 -73.73 -100.15
REMARK 500 12 PHE A 8 57.78 -93.74
REMARK 500 12 THR A 11 30.56 -96.34
REMARK 500 12 LEU A 34 55.10 -111.20
REMARK 500 13 PHE A 8 47.30 -96.11
REMARK 500 13 CYS A 15 -73.35 -93.13
REMARK 500 14 PHE A 8 55.09 -103.24
REMARK 500 15 PHE A 8 50.06 -93.30
REMARK 500 15 CYS A 15 -67.66 -100.04
REMARK 500 15 ASP A 16 63.28 63.92
REMARK 500 16 PHE A 8 47.88 -101.46
REMARK 500 16 THR A 11 32.44 -82.12
REMARK 500 16 CYS A 15 -66.46 -100.29
REMARK 500 16 LEU A 34 67.90 -110.57
REMARK 500 17 THR A 3 33.83 -83.11
REMARK 500 17 PHE A 8 46.60 -92.85
REMARK 500 17 THR A 11 34.25 -84.29
REMARK 500 17 CYS A 15 -74.95 -81.25
REMARK 500 18 PHE A 8 46.96 -96.10
REMARK 500 18 CYS A 15 -71.74 -99.10
REMARK 500 19 THR A 3 44.95 -99.48
REMARK 500 19 PHE A 8 54.99 -92.79
REMARK 500 19 CYS A 15 -68.78 -97.44
REMARK 500 20 SER A 2 45.76 -98.07
REMARK 500
REMARK 500 THIS ENTRY HAS 53 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 ZN A 36 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 10 SG
REMARK 620 2 CYS A 15 SG 110.4
REMARK 620 3 HIS A 28 NE2 112.3 112.3
REMARK 620 4 HIS A 32 NE2 109.7 110.4 101.4
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 36
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1P7A RELATED DB: PDB
REMARK 900 WILD-TYPE BKLF F3 STRUCTURE
REMARK 900 RELATED ID: 1U85 RELATED DB: PDB
REMARK 900 R326W MUTANT OF BKLF F3
DBREF 1U86 A 3 35 UNP Q60980 KLF3_MOUSE 314 344
SEQADV 1U86 GLY A 1 UNP Q60980 CLONING ARTIFACT
SEQADV 1U86 SER A 2 UNP Q60980 CLONING ARTIFACT
SEQADV 1U86 THR A 11 UNP Q60980 INSERTION
SEQADV 1U86 TRP A 12 UNP Q60980 INSERTION
SEQRES 1 A 35 GLY SER THR GLY ILE LYS PRO PHE GLN CYS THR TRP PRO
SEQRES 2 A 35 ASP CYS ASP ARG SER PHE SER ARG SER ASP HIS LEU ALA
SEQRES 3 A 35 LEU HIS ARG LYS ARG HIS MET LEU VAL
HET ZN A 36 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
HELIX 1 1 ARG A 21 ARG A 31 1 11
SHEET 1 A 2 PHE A 8 GLN A 9 0
SHEET 2 A 2 SER A 18 PHE A 19 -1 O PHE A 19 N PHE A 8
LINK SG CYS A 10 ZN ZN A 36 1555 1555 2.31
LINK SG CYS A 15 ZN ZN A 36 1555 1555 2.30
LINK NE2 HIS A 28 ZN ZN A 36 1555 1555 1.98
LINK NE2 HIS A 32 ZN ZN A 36 1555 1555 1.96
SITE 1 AC1 4 CYS A 10 CYS A 15 HIS A 28 HIS A 32
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 - 2 20 Bytes