HEADER GENE REGULATION 12-OCT-99 1D5V
TITLE SOLUTION STRUCTURE OF THE FORKHEAD DOMAIN OF THE ADIPOCYTE-
TITLE 2 TRANSCRIPTION FACTOR FREAC-11 (S12)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: S12 TRANSCRIPTION FACTOR (FKH-14);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DNA-BINDING DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 TISSUE: ADIPOSE TISSUE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-11A
KEYWDS WINGED HELIX, DNA-RECOGNITION HELIX, GENE REGULATION
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR M.J.P.VAN DONGEN,A.CEDERBERG,P.CARLSSON,S.ENERBACK,M.WIKSTROM
REVDAT 4 16-FEB-22 1D5V 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1D5V 1 VERSN
REVDAT 2 01-APR-03 1D5V 1 JRNL
REVDAT 1 11-OCT-00 1D5V 0
JRNL AUTH M.J.VAN DONGEN,A.CEDERBERG,P.CARLSSON,S.ENERBACK,M.WIKSTROM
JRNL TITL SOLUTION STRUCTURE AND DYNAMICS OF THE DNA-BINDING DOMAIN OF
JRNL TITL 2 THE ADIPOCYTE-TRANSCRIPTION FACTOR FREAC-11.
JRNL REF J.MOL.BIOL. V. 296 351 2000
JRNL REFN ISSN 0022-2836
JRNL PMID 10669593
JRNL DOI 10.1006/JMBI.1999.3476
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 1, ANSIG 3.3
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), KRAULIS (ANSIG)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE WAS DETERMINED FROM 1042
REMARK 3 DISTANCE RESTRAINTS, COMPLEMENTED WITH 145 RESTRAINTS ON
REMARK 3 DIHEDRAL ANGLES AND 36 RESTRAINTS ON HYDROGEN BOND LENGTHS.
REMARK 4
REMARK 4 1D5V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-OCT-99.
REMARK 100 THE DEPOSITION ID IS D_1000009821.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.1
REMARK 210 IONIC STRENGTH : 15 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM S12 DBD, 10 MM NACL, 5 MM
REMARK 210 MGCL2, 0.02% NAN3, 5 MM DTT; 1
REMARK 210 MM S12 DBD, 10 MM NACL, 5 MM
REMARK 210 MGCL2, 0.02% NAN3, 5 MM DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNHA; CROSS
REMARK 210 RELAXATION BETWEEN 13CA-1HA
REMARK 210 DIPOLAR AND 13C' CHEMICAL SHIFT
REMARK 210 ANISOTROPY; CROSS RELAXATION
REMARK 210 BETWEEN 13CA-1HA AND 15N-1HN
REMARK 210 DIPOLAR INTERACTIONS
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ; 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.1
REMARK 210 METHOD USED : COMBINED DISTANCE
REMARK 210 GEOMETRY/SIMULATING ANNEALING
REMARK 210 PROCEDURE
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 125
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 8
REMARK 210
REMARK 210 REMARK: HNCA, HN(CO)CA, HNCACB, CACB(CO)NH AND HNCO EXPERIMENTS
REMARK 210 WERE USED TO OBTAIN SEQUENTIAL ASSIGNMENTS FOR THE BACKBONE.
REMARK 210 SIDE-CHAIN RESONANCES WERE ASSIGNED USING TOCSY-15N-HSQC, C(CO)
REMARK 210 NH, H(CCO)NH AND HC(C)H-TOCSY EXPERIMENTS.
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 PRO A 6 -8.03 -48.41
REMARK 500 1 LEU A 56 59.00 -69.59
REMARK 500 1 SER A 57 -55.64 -172.55
REMARK 500 1 ARG A 67 -168.58 -72.23
REMARK 500 1 PRO A 72 -157.78 -82.18
REMARK 500 1 SER A 84 49.03 -83.54
REMARK 500 1 MET A 87 6.15 -69.05
REMARK 500 2 PRO A 5 155.57 -42.66
REMARK 500 2 PRO A 82 -137.16 -50.86
REMARK 500 3 PRO A 5 160.57 -45.58
REMARK 500 3 PRO A 39 -7.25 -49.75
REMARK 500 3 GLN A 46 -168.89 -59.91
REMARK 500 3 LYS A 74 -105.99 -82.94
REMARK 500 3 PRO A 82 -141.86 -55.12
REMARK 500 3 ASP A 83 45.38 -81.96
REMARK 500 3 PHE A 93 -13.76 -46.46
REMARK 500 4 PRO A 6 28.79 -73.27
REMARK 500 4 ARG A 67 -161.38 -79.07
REMARK 500 5 PRO A 6 -12.11 -42.25
REMARK 500 5 PRO A 39 -6.07 -50.31
REMARK 500 5 LEU A 56 59.21 -65.29
REMARK 500 5 SER A 57 -54.87 -159.97
REMARK 500 5 PRO A 66 -168.84 -71.12
REMARK 500 5 PRO A 82 -79.72 -53.25
REMARK 500 5 ASP A 83 42.62 -162.08
REMARK 500 5 SER A 84 110.00 -45.37
REMARK 500 5 TYR A 85 -76.67 -89.95
REMARK 500 5 ASN A 90 44.68 -80.96
REMARK 500 6 PRO A 6 27.66 -74.67
REMARK 500 6 PRO A 82 -135.99 -49.69
REMARK 500 6 SER A 84 44.30 -179.97
REMARK 500 6 PHE A 88 35.87 -89.49
REMARK 500 6 ASN A 90 1.50 -65.96
REMARK 500 6 SER A 92 120.36 -173.47
REMARK 500 7 PRO A 5 154.26 -40.93
REMARK 500 7 PRO A 6 30.22 -75.72
REMARK 500 7 PRO A 21 -73.94 -37.33
REMARK 500 7 GLU A 22 -79.97 -90.10
REMARK 500 7 LYS A 23 -34.65 -165.50
REMARK 500 7 LYS A 45 -66.39 -95.55
REMARK 500 7 PRO A 66 162.67 -35.52
REMARK 500 7 ARG A 67 -172.36 -59.79
REMARK 500 7 PRO A 72 -131.68 -47.89
REMARK 500 8 PRO A 6 26.61 -73.40
REMARK 500 8 PRO A 82 -153.69 -74.55
REMARK 500 8 SER A 84 85.83 -59.30
REMARK 500 8 PHE A 88 -107.82 -59.15
REMARK 500 8 ASN A 90 31.35 -90.89
REMARK 500 9 PRO A 6 -12.17 -42.03
REMARK 500 9 LYS A 70 -15.21 -49.82
REMARK 500
REMARK 500 THIS ENTRY HAS 155 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1D5V A 1 94 UNP Q99958 FOXC2_HUMAN 69 162
SEQADV 1D5V MET A 1 UNP Q99958 ASP 69 CONFLICT
SEQRES 1 A 94 MET LEU VAL LYS PRO PRO TYR SER TYR ILE ALA LEU ILE
SEQRES 2 A 94 THR MET ALA ILE GLN ASN ALA PRO GLU LYS LYS ILE THR
SEQRES 3 A 94 LEU ASN GLY ILE TYR GLN PHE ILE MET ASP ARG PHE PRO
SEQRES 4 A 94 PHE TYR ARG GLU ASN LYS GLN GLY TRP GLN ASN SER ILE
SEQRES 5 A 94 ARG HIS ASN LEU SER LEU ASN GLU CYS PHE VAL LYS VAL
SEQRES 6 A 94 PRO ARG ASP ASP LYS LYS PRO GLY LYS GLY SER TYR TRP
SEQRES 7 A 94 THR LEU ASP PRO ASP SER TYR ASN MET PHE GLU ASN GLY
SEQRES 8 A 94 SER PHE LEU
HELIX 1 1 SER A 8 ASN A 19 1 12
HELIX 2 2 THR A 26 PHE A 38 1 13
HELIX 3 3 PRO A 39 ASN A 44 1 6
HELIX 4 4 GLY A 47 ASN A 59 1 13
SHEET 1 A 2 PHE A 62 LYS A 64 0
SHEET 2 A 2 TRP A 78 LEU A 80 -1 O THR A 79 N VAL A 63
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
(ATOM LINES ARE NOT SHOWN.)
END
