Header list of 2d2w.pdb file
Complete list - r 9 2 Bytes
HEADER DNA BINDING PROTEIN 19-SEP-05 2D2W
TITLE SOLUTION STRUCTURE AND DYNAMICS OF THE DNA-BINDING DOMAIN OF MYOCYTE
TITLE 2 NUCLEAR FACTOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FORKHEAD BOX PROTEIN K1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DNA-BINDING DOMAIN;
COMPND 5 SYNONYM: MYOCYTE NUCLEAR FACTOR, MNF;
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: FOXK1;
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, FORKHEAD, DNA BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR W.-J.CHUANG,C.-H.CHANG,W.-Y.JENG,Y.-P.CHU
REVDAT 3 09-MAR-22 2D2W 1 REMARK
REVDAT 2 24-FEB-09 2D2W 1 VERSN
REVDAT 1 05-SEP-06 2D2W 0
JRNL AUTH C.-H.CHANG,Y.-P.CHU,W.-Y.JENG,W.-J.CHUANG
JRNL TITL SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF THE DNA-BINDING
JRNL TITL 2 DOMAIN OF MYOCYTE NUCLEAR FACTOR (FOXK1)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2D2W COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000024920.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6
REMARK 210 IONIC STRENGTH : 125
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 3MM MNF;25MM PHOSPHATE BUFFER;
REMARK 210 100MM NACL; 3MM MNF;25MM
REMARK 210 PHOSPHATE BUFFER; 100MM NACL;
REMARK 210 3MM MNF U-15N;25MM PHOSPHATE
REMARK 210 BUFFER; 100MM NACL; 3MM MNF U-
REMARK 210 15N,13C;25MM PHOSPHATE BUFFER;
REMARK 210 100MM NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; 3D_15N
REMARK 210 -SEPARATED_NOESY; 3D_13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
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 : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: HNCA, HN(CO)CA, HNCACB, CBCA(CO)NH, HBHA(CACB)NH,
REMARK 210 HBHA(CACBCO)NH, HCCH-TOCSY, HCCH-COSY
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 SER A 2 -162.50 65.67
REMARK 500 1 SER A 7 167.95 -48.59
REMARK 500 1 ALA A 15 -72.66 -67.71
REMARK 500 1 ALA A 19 -156.64 -62.32
REMARK 500 1 GLN A 20 -98.86 -49.84
REMARK 500 1 ARG A 22 28.20 -174.05
REMARK 500 1 SER A 27 47.03 -99.97
REMARK 500 1 HIS A 32 -83.54 -74.06
REMARK 500 1 LYS A 45 48.80 -87.04
REMARK 500 1 ARG A 66 48.31 -163.48
REMARK 500 1 GLN A 68 -72.25 -143.73
REMARK 500 1 PHE A 76 -129.08 -172.76
REMARK 500 1 ARG A 78 -160.83 -160.27
REMARK 500 1 GLN A 97 -72.63 -118.72
REMARK 500 1 ARG A 98 31.78 -177.82
REMARK 500 2 SER A 2 -77.12 -157.67
REMARK 500 2 SER A 7 -178.74 -50.90
REMARK 500 2 ALA A 9 -38.65 -131.34
REMARK 500 2 ALA A 19 -168.03 -60.94
REMARK 500 2 GLN A 20 -90.88 -45.11
REMARK 500 2 ASP A 21 -64.58 -90.38
REMARK 500 2 ARG A 22 38.01 179.85
REMARK 500 2 ARG A 41 -56.35 -164.13
REMARK 500 2 THR A 42 28.53 -157.81
REMARK 500 2 ALA A 43 -82.13 -68.46
REMARK 500 2 LYS A 45 31.03 -90.21
REMARK 500 2 VAL A 64 87.05 -161.64
REMARK 500 2 GLU A 69 -70.10 -88.87
REMARK 500 2 LYS A 73 -73.75 -86.07
REMARK 500 2 SER A 75 -68.62 -124.39
REMARK 500 2 LYS A 94 -79.73 -130.84
REMARK 500 2 ARG A 96 -55.13 -161.61
REMARK 500 3 SER A 7 172.00 -49.14
REMARK 500 3 ARG A 22 -4.19 -59.59
REMARK 500 3 SER A 27 32.24 -99.62
REMARK 500 3 HIS A 32 -70.51 -77.61
REMARK 500 3 TYR A 40 99.40 -60.28
REMARK 500 3 ARG A 41 -50.69 -141.16
REMARK 500 3 THR A 42 40.07 -165.56
REMARK 500 3 ALA A 43 -89.28 -79.13
REMARK 500 3 LYS A 45 43.94 -90.30
REMARK 500 3 TYR A 60 50.17 -151.33
REMARK 500 3 GLU A 69 -76.12 -169.42
REMARK 500 3 ARG A 96 155.50 179.87
REMARK 500 4 SER A 2 -125.36 72.29
REMARK 500 4 SER A 7 169.32 -48.56
REMARK 500 4 ALA A 19 -162.57 -65.86
REMARK 500 4 GLN A 20 -76.84 -66.54
REMARK 500 4 ASP A 21 -73.56 -91.42
REMARK 500 4 ARG A 22 31.94 178.75
REMARK 500
REMARK 500 THIS ENTRY HAS 287 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 22 0.28 SIDE CHAIN
REMARK 500 1 ARG A 41 0.28 SIDE CHAIN
REMARK 500 1 ARG A 52 0.22 SIDE CHAIN
REMARK 500 1 ARG A 59 0.31 SIDE CHAIN
REMARK 500 1 ARG A 66 0.09 SIDE CHAIN
REMARK 500 1 ARG A 78 0.18 SIDE CHAIN
REMARK 500 1 ARG A 93 0.09 SIDE CHAIN
REMARK 500 1 ARG A 95 0.11 SIDE CHAIN
REMARK 500 1 ARG A 96 0.31 SIDE CHAIN
REMARK 500 1 ARG A 98 0.32 SIDE CHAIN
REMARK 500 2 ARG A 22 0.31 SIDE CHAIN
REMARK 500 2 ARG A 41 0.15 SIDE CHAIN
REMARK 500 2 ARG A 52 0.29 SIDE CHAIN
REMARK 500 2 ARG A 59 0.30 SIDE CHAIN
REMARK 500 2 ARG A 66 0.19 SIDE CHAIN
REMARK 500 2 ARG A 78 0.10 SIDE CHAIN
REMARK 500 2 ARG A 93 0.28 SIDE CHAIN
REMARK 500 2 ARG A 95 0.25 SIDE CHAIN
REMARK 500 2 ARG A 96 0.29 SIDE CHAIN
REMARK 500 2 ARG A 98 0.27 SIDE CHAIN
REMARK 500 3 ARG A 22 0.28 SIDE CHAIN
REMARK 500 3 ARG A 41 0.12 SIDE CHAIN
REMARK 500 3 ARG A 52 0.32 SIDE CHAIN
REMARK 500 3 ARG A 59 0.27 SIDE CHAIN
REMARK 500 3 ARG A 66 0.15 SIDE CHAIN
REMARK 500 3 ARG A 78 0.31 SIDE CHAIN
REMARK 500 3 ARG A 93 0.20 SIDE CHAIN
REMARK 500 3 ARG A 95 0.20 SIDE CHAIN
REMARK 500 3 ARG A 98 0.23 SIDE CHAIN
REMARK 500 4 ARG A 22 0.23 SIDE CHAIN
REMARK 500 4 ARG A 41 0.32 SIDE CHAIN
REMARK 500 4 ARG A 52 0.32 SIDE CHAIN
REMARK 500 4 ARG A 59 0.28 SIDE CHAIN
REMARK 500 4 ARG A 66 0.21 SIDE CHAIN
REMARK 500 4 ARG A 78 0.14 SIDE CHAIN
REMARK 500 4 ARG A 93 0.25 SIDE CHAIN
REMARK 500 4 ARG A 95 0.29 SIDE CHAIN
REMARK 500 4 ARG A 96 0.28 SIDE CHAIN
REMARK 500 4 ARG A 98 0.29 SIDE CHAIN
REMARK 500 5 ARG A 22 0.31 SIDE CHAIN
REMARK 500 5 ARG A 41 0.10 SIDE CHAIN
REMARK 500 5 ARG A 52 0.24 SIDE CHAIN
REMARK 500 5 ARG A 59 0.32 SIDE CHAIN
REMARK 500 5 ARG A 66 0.31 SIDE CHAIN
REMARK 500 5 ARG A 93 0.30 SIDE CHAIN
REMARK 500 5 ARG A 95 0.19 SIDE CHAIN
REMARK 500 5 ARG A 96 0.28 SIDE CHAIN
REMARK 500 6 ARG A 22 0.32 SIDE CHAIN
REMARK 500 6 ARG A 41 0.24 SIDE CHAIN
REMARK 500 6 ARG A 52 0.20 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 190 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2D2W A 1 101 UNP P42128 FOXK1_MOUSE 287 387
SEQRES 1 A 101 GLU SER LYS PRO PRO TYR SER TYR ALA GLN LEU ILE VAL
SEQRES 2 A 101 GLN ALA ILE SER SER ALA GLN ASP ARG GLN LEU THR LEU
SEQRES 3 A 101 SER GLY ILE TYR ALA HIS ILE THR LYS HIS TYR PRO TYR
SEQRES 4 A 101 TYR ARG THR ALA ASP LYS GLY TRP GLN ASN SER ILE ARG
SEQRES 5 A 101 HIS ASN LEU SER LEU ASN ARG TYR PHE ILE LYS VAL PRO
SEQRES 6 A 101 ARG SER GLN GLU GLU PRO GLY LYS GLY SER PHE TRP ARG
SEQRES 7 A 101 ILE ASP PRO ALA SER GLU ALA LYS LEU VAL GLU GLN ALA
SEQRES 8 A 101 PHE ARG LYS ARG ARG GLN ARG GLY VAL SER
HELIX 1 1 ALA A 9 ALA A 19 1 11
HELIX 2 2 GLY A 28 TYR A 37 1 10
HELIX 3 3 GLY A 46 ASN A 58 1 13
HELIX 4 4 LYS A 86 PHE A 92 1 7
SHEET 1 A 3 GLN A 23 LEU A 24 0
SHEET 2 A 3 TRP A 77 ARG A 78 -1 O TRP A 77 N LEU A 24
SHEET 3 A 3 ILE A 62 LYS A 63 -1 N ILE A 62 O ARG A 78
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 - r 9 2 Bytes