Header list of 1jxs.pdb file
Complete list - b 23 2 Bytes
HEADER DNA BINDING PROTEIN 08-SEP-01 1JXS
TITLE SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF INTERLEUKIN ENHANCER
TITLE 2 BINDING FACTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERLEUKIN ENHANCER BINDING FACTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DNA-BINDING DOMAIN;
COMPND 5 SYNONYM: ILF-1;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ILF-1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS DNA-BINDING DOMAIN, WINGED HELIX, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR W.J.CHUANG,P.P.LIU,C.LI,Y.H.HSIEH,S.W.CHEN,S.H.CHEN,W.Y.JENG
REVDAT 3 23-FEB-22 1JXS 1 REMARK
REVDAT 2 24-FEB-09 1JXS 1 VERSN
REVDAT 1 11-MAR-03 1JXS 0
JRNL AUTH P.P.LIU,Y.C.CHEN,C.LI,Y.H.HSIEH,S.W.CHEN,S.H.CHEN,W.Y.JENG,
JRNL AUTH 2 W.J.CHUANG
JRNL TITL SOLUTION STRUCTURE OF THE DNA-BINDING DOMAIN OF INTERLEUKIN
JRNL TITL 2 ENHANCER BINDING FACTOR 1 (FOXK1A)
JRNL REF PROTEINS: V. 49 543 2002
JRNL REF 2 STRUCT.,FUNCT.,GENET.
JRNL REFN ISSN 0887-3585
JRNL PMID 12402362
JRNL DOI 10.1002/PROT.10227
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.85
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JXS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-SEP-01.
REMARK 100 THE DEPOSITION ID IS D_1000014308.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 300; 300; 300
REMARK 210 PH : 6; 6; 6; 6
REMARK 210 IONIC STRENGTH : 125; 125; 125; 125
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT;
REMARK 210 AMBIENT
REMARK 210 SAMPLE CONTENTS : 3MM ILF, 25MM PHOSPHATE BUFFER,
REMARK 210 100MM NACL; 3MM ILF, 25MM
REMARK 210 PHOSPHATE BUFFER, 100MM NACL;
REMARK 210 3MM ILF U-15N, 25MM PHOSPHATE
REMARK 210 BUFFER, 100MM NACL; 2MM ILF U-
REMARK 210 15N, 13C, 25MM PHOSPHATE BUFFER,
REMARK 210 100MM NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; DQF-COSY; TOCSY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AURELIA 2.7.10, XWINNMR 2.6
REMARK 210 METHOD USED : HYBRID DISTANCE GEOMETRY
REMARK 210 -DYNAMICAL SIMULATED ANNEALING
REMARK 210 METHOD
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 20
REMARK 210
REMARK 210 REMARK: HNCA, HN(CO)CA, HNCBCA, CBCA(CO)NH, HBHA(CBCA)NH,
REMARK 210 HBHA(CBCACO)NH
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 TYR A 6 -157.97 -122.07
REMARK 500 1 VAL A 13 -70.46 -64.19
REMARK 500 1 GLN A 14 -25.85 -39.10
REMARK 500 1 ASP A 21 -24.77 167.34
REMARK 500 1 ASN A 36 -70.27 -94.91
REMARK 500 1 TYR A 39 -72.32 -108.53
REMARK 500 1 ARG A 41 -45.97 -157.94
REMARK 500 1 ALA A 43 -33.78 178.53
REMARK 500 1 GLN A 48 -82.13 -52.83
REMARK 500 1 PRO A 65 -85.88 -78.71
REMARK 500 1 SER A 67 -149.55 -167.21
REMARK 500 1 GLU A 69 28.26 39.84
REMARK 500 1 SER A 75 141.91 -175.06
REMARK 500 1 ARG A 78 -163.95 -106.52
REMARK 500 1 ALA A 82 34.95 -94.39
REMARK 500 1 SER A 83 -57.17 -131.64
REMARK 500 1 GLU A 84 -81.71 -43.04
REMARK 500 1 SER A 85 -30.40 -31.97
REMARK 500 1 ALA A 91 -62.30 -98.63
REMARK 500 1 ARG A 93 -153.28 -77.42
REMARK 500 1 ARG A 96 94.93 -164.30
REMARK 500 2 LYS A 3 94.29 -33.65
REMARK 500 2 TYR A 6 -160.75 -112.07
REMARK 500 2 ASP A 21 -20.81 161.92
REMARK 500 2 PRO A 38 -72.35 -72.75
REMARK 500 2 TYR A 39 -70.84 -114.18
REMARK 500 2 TYR A 40 25.98 44.10
REMARK 500 2 ARG A 41 63.93 -167.89
REMARK 500 2 THR A 42 -35.97 -172.44
REMARK 500 2 GLN A 48 -82.61 -48.20
REMARK 500 2 PRO A 65 -165.46 -75.32
REMARK 500 2 ARG A 66 42.36 -86.36
REMARK 500 2 GLN A 68 71.23 -105.60
REMARK 500 2 GLU A 69 88.00 41.43
REMARK 500 2 ARG A 78 -163.51 -109.23
REMARK 500 2 SER A 83 -51.27 -146.53
REMARK 500 2 SER A 85 -28.41 -37.72
REMARK 500 2 ARG A 93 -156.42 -101.55
REMARK 500 2 LYS A 94 -168.76 -126.32
REMARK 500 2 ARG A 95 68.71 -119.18
REMARK 500 3 ASP A 21 -19.83 159.58
REMARK 500 3 THR A 31 -6.71 -55.32
REMARK 500 3 HIS A 32 -70.78 -100.84
REMARK 500 3 ASN A 36 -87.97 -99.23
REMARK 500 3 TYR A 37 165.78 -44.42
REMARK 500 3 PRO A 38 -87.12 -72.97
REMARK 500 3 TYR A 40 -50.48 164.25
REMARK 500 3 ARG A 41 50.22 -93.93
REMARK 500 3 THR A 42 -43.26 -150.02
REMARK 500 3 GLN A 48 -87.37 -49.62
REMARK 500
REMARK 500 THIS ENTRY HAS 373 RAMACHANDRAN OUTLIERS.
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 1 ARG A 41 0.21 SIDE CHAIN
REMARK 500 1 ARG A 59 0.30 SIDE CHAIN
REMARK 500 1 ARG A 66 0.26 SIDE CHAIN
REMARK 500 1 ARG A 78 0.15 SIDE CHAIN
REMARK 500 1 ARG A 93 0.21 SIDE CHAIN
REMARK 500 1 ARG A 95 0.27 SIDE CHAIN
REMARK 500 1 ARG A 96 0.30 SIDE CHAIN
REMARK 500 1 ARG A 98 0.25 SIDE CHAIN
REMARK 500 2 ARG A 41 0.17 SIDE CHAIN
REMARK 500 2 ARG A 52 0.28 SIDE CHAIN
REMARK 500 2 ARG A 59 0.31 SIDE CHAIN
REMARK 500 2 ARG A 66 0.23 SIDE CHAIN
REMARK 500 2 ARG A 78 0.32 SIDE CHAIN
REMARK 500 2 ARG A 93 0.31 SIDE CHAIN
REMARK 500 2 ARG A 95 0.30 SIDE CHAIN
REMARK 500 2 ARG A 98 0.19 SIDE CHAIN
REMARK 500 3 ARG A 41 0.17 SIDE CHAIN
REMARK 500 3 ARG A 52 0.22 SIDE CHAIN
REMARK 500 3 ARG A 59 0.29 SIDE CHAIN
REMARK 500 3 ARG A 66 0.20 SIDE CHAIN
REMARK 500 3 ARG A 78 0.32 SIDE CHAIN
REMARK 500 3 ARG A 93 0.20 SIDE CHAIN
REMARK 500 3 ARG A 95 0.23 SIDE CHAIN
REMARK 500 3 ARG A 96 0.20 SIDE CHAIN
REMARK 500 3 ARG A 98 0.12 SIDE CHAIN
REMARK 500 4 ARG A 41 0.29 SIDE CHAIN
REMARK 500 4 ARG A 52 0.23 SIDE CHAIN
REMARK 500 4 ARG A 59 0.31 SIDE CHAIN
REMARK 500 4 ARG A 66 0.23 SIDE CHAIN
REMARK 500 4 ARG A 78 0.25 SIDE CHAIN
REMARK 500 4 ARG A 95 0.32 SIDE CHAIN
REMARK 500 4 ARG A 96 0.27 SIDE CHAIN
REMARK 500 4 ARG A 98 0.31 SIDE CHAIN
REMARK 500 5 ARG A 41 0.18 SIDE CHAIN
REMARK 500 5 ARG A 52 0.09 SIDE CHAIN
REMARK 500 5 ARG A 59 0.13 SIDE CHAIN
REMARK 500 5 ARG A 66 0.32 SIDE CHAIN
REMARK 500 5 ARG A 78 0.26 SIDE CHAIN
REMARK 500 5 ARG A 93 0.22 SIDE CHAIN
REMARK 500 5 ARG A 95 0.32 SIDE CHAIN
REMARK 500 5 ARG A 96 0.31 SIDE CHAIN
REMARK 500 5 ARG A 98 0.25 SIDE CHAIN
REMARK 500 6 ARG A 41 0.31 SIDE CHAIN
REMARK 500 6 ARG A 52 0.16 SIDE CHAIN
REMARK 500 6 ARG A 59 0.13 SIDE CHAIN
REMARK 500 6 ARG A 66 0.27 SIDE CHAIN
REMARK 500 6 ARG A 78 0.27 SIDE CHAIN
REMARK 500 6 ARG A 93 0.24 SIDE CHAIN
REMARK 500 6 ARG A 95 0.28 SIDE CHAIN
REMARK 500 6 ARG A 96 0.22 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 169 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4829 RELATED DB: BMRB
REMARK 900 1H, 15N AND 13C RESONANCE ASSIGNMENTS FOR THE DNA-BINDING DOMAIN OF
REMARK 900 INTERLEUKIN ENHANCER BINDING FACTOR
DBREF 1JXS A 1 98 UNP Q01167 FOXK2_HUMAN 251 348
SEQRES 1 A 98 ASP SER LYS PRO PRO TYR SER TYR ALA GLN LEU ILE VAL
SEQRES 2 A 98 GLN ALA ILE THR MET ALA PRO ASP LYS GLN LEU THR LEU
SEQRES 3 A 98 ASN GLY ILE TYR THR HIS ILE THR LYS ASN TYR PRO TYR
SEQRES 4 A 98 TYR ARG THR ALA ASP LYS GLY TRP GLN ASN SER ILE ARG
SEQRES 5 A 98 HIS ASN LEU SER LEU ASN ARG TYR PHE ILE LYS VAL PRO
SEQRES 6 A 98 ARG SER GLN GLU GLU PRO GLY LYS GLY SER PHE TRP ARG
SEQRES 7 A 98 ILE ASP PRO ALA SER GLU SER LYS LEU ILE GLU GLN ALA
SEQRES 8 A 98 PHE ARG LYS ARG ARG PRO ARG
HELIX 1 1 ALA A 9 MET A 18 1 10
HELIX 2 2 THR A 25 TYR A 37 1 13
HELIX 3 3 TRP A 47 ASN A 58 1 12
HELIX 4 4 SER A 83 ARG A 93 1 11
SHEET 1 A 3 GLN A 23 LEU A 24 0
SHEET 2 A 3 PHE A 76 ILE A 79 -1 O TRP A 77 N LEU A 24
SHEET 3 A 3 PHE A 61 VAL A 64 -1 N VAL A 64 O PHE A 76
CRYST1 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 - b 23 2 Bytes