Header list of 1fsh.pdb file
Complete list - b 23 2 Bytes
HEADER SIGNALING PROTEIN 08-SEP-00 1FSH
TITLE STRUCTURAL BASIS OF THE RECOGNITION OF THE DISHEVELLED DEP DOMAIN IN
TITLE 2 THE WNT SIGNALING PATHWAY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DISHEVELLED-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DEP DOMAIN (RESIDUES 391-495);
COMPND 5 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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PQE31
KEYWDS THREE-HELIX BUNDLE, BETA-ARM, DISHEVELLED-1, SEGMENT POLARITY PROTEIN
KEYWDS 2 DISHEVELLED HOMOLOG DVL-1, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.C.WONG,J.ZHENG
REVDAT 4 23-FEB-22 1FSH 1 REMARK
REVDAT 3 24-FEB-09 1FSH 1 VERSN
REVDAT 2 31-DEC-02 1FSH 1 REMARK
REVDAT 1 08-MAR-01 1FSH 0
JRNL AUTH H.C.WONG,J.MAO,J.T.NGUYEN,S.SRINIVAS,W.ZHANG,B.LIU,L.LI,
JRNL AUTH 2 D.WU,J.ZHENG
JRNL TITL STRUCTURAL BASIS OF THE RECOGNITION OF THE DISHEVELLED DEP
JRNL TITL 2 DOMAIN IN THE WNT SIGNALING PATHWAY.
JRNL REF NAT.STRUCT.BIOL. V. 7 1178 2000
JRNL REFN ISSN 1072-8368
JRNL PMID 11101902
JRNL DOI 10.1038/82047
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5
REMARK 3 AUTHORS : GUNTERT, P.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURAL CALCULATIONS ARE BASED
REMARK 3 ON 2009 NOE DISTANCE RESTRAINTS, 54 HYDROGEN-BOND DISTANCE
REMARK 3 RESTRAINTS, AND 40 DIHEDRAL ANGLE RESTRAINTS
REMARK 4
REMARK 4 1FSH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-OCT-00.
REMARK 100 THE DEPOSITION ID IS D_1000011863.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 0.1
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8-1.5MM DEP, 15N AND 13C
REMARK 210 LABELED, 100MM PHOSPHATE BUFFER
REMARK 210 (PH 6.8), 0.1MM NAN3, 3MM DTT;
REMARK 210 0.8-1.5MM DEP, 15N LABELED,
REMARK 210 100MM PHOSPHATE BUFFER (PH 6.8),
REMARK 210 0.1MM NAN3, 3MM DTT; 0.8-1.5MM
REMARK 210 DEP, VALINE SELECTIVE 15N
REMARK 210 LABELED, 100MM PHOSPHATE BUFFER
REMARK 210 (PH 6.8), 0.1MM NAN3, 3MM DTT;
REMARK 210 0.8-1.5MM DEP, 15N LABELED,
REMARK 210 100MM PHOSPHATE BUFFER (PH 6.8),
REMARK 210 0.1MM NAN3, 3MM DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; HNHA;
REMARK 210 3D_15N-SEPARATED_NOESY; 2D NOESY;
REMARK 210 HMQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 98, XEASY 1.3.13, DYANA
REMARK 210 1.5
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1000
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-20
REMARK 465 RES C SSSEQI
REMARK 465 THR A 1
REMARK 465 SER A 2
REMARK 465 SER A 3
REMARK 465 VAL A 4
REMARK 465 PRO A 5
REMARK 465 GLY A 6
REMARK 465 ALA A 7
REMARK 465 PRO A 8
REMARK 465 GLN A 9
REMARK 465 LEU A 10
REMARK 465 GLU A 11
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 HG22 VAL A 17 CE1 PHE A 67 0.73
REMARK 500 HG13 ILE A 24 HH TYR A 76 0.79
REMARK 500 HG22 VAL A 17 HE1 PHE A 67 0.88
REMARK 500 HG11 VAL A 27 HH2 TRP A 59 0.90
REMARK 500 HE1 MET A 28 HG13 VAL A 56 0.91
REMARK 500 HB1 ALA A 13 HG11 VAL A 64 0.98
REMARK 500 HB1 ALA A 13 HG13 VAL A 64 1.00
REMARK 500 HE2 MET A 21 HE1 TYR A 76 1.01
REMARK 500 HB1 ALA A 13 CG1 VAL A 64 1.04
REMARK 500 HG21 VAL A 17 HD1 PHE A 67 1.06
REMARK 500 HE1 MET A 28 CG1 VAL A 56 1.08
REMARK 500 HG21 VAL A 17 CD1 PHE A 67 1.13
REMARK 500 HE1 MET A 28 HG12 VAL A 56 1.16
REMARK 500 HB2 ALA A 13 HG12 VAL A 64 1.18
REMARK 500 HB3 MET A 21 HE2 PHE A 85 1.23
REMARK 500 HE2 GLU A 12 HG2 GLU A 65 1.24
REMARK 500 CB ALA A 13 HG13 VAL A 64 1.32
REMARK 500 OE2 GLU A 12 HG2 GLU A 65 1.34
REMARK 500 HG13 ILE A 24 OH TYR A 76 1.36
REMARK 500 CG1 VAL A 27 HH2 TRP A 59 1.40
REMARK 500 CG2 VAL A 17 CE1 PHE A 67 1.45
REMARK 500 CB ALA A 13 HG11 VAL A 64 1.53
REMARK 500 HB2 ALA A 13 CG1 VAL A 64 1.55
REMARK 500 CB ALA A 13 CG1 VAL A 64 1.57
REMARK 500 CG1 ILE A 24 HH TYR A 76 1.59
REMARK 500 O SER A 33 NE2 HIS A 63 1.65
REMARK 500 CG2 VAL A 17 CD1 PHE A 67 1.77
REMARK 500 OE2 GLU A 12 CG GLU A 65 1.91
REMARK 500 CE MET A 28 CG1 VAL A 56 2.11
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 ALA A 13 171.56 -46.10
REMARK 500 1 THR A 16 -48.12 -141.78
REMARK 500 1 VAL A 17 -32.93 167.91
REMARK 500 1 ASP A 20 111.91 -39.39
REMARK 500 1 LEU A 30 135.65 -38.66
REMARK 500 1 GLU A 36 114.17 65.31
REMARK 500 1 ARG A 38 -34.98 178.90
REMARK 500 1 LYS A 44 17.31 83.36
REMARK 500 1 ALA A 48 48.70 -101.76
REMARK 500 1 ASN A 49 93.77 151.58
REMARK 500 1 VAL A 51 -55.36 174.40
REMARK 500 1 ILE A 52 171.94 57.01
REMARK 500 1 ASP A 58 -31.90 -37.71
REMARK 500 1 THR A 62 -72.86 -72.31
REMARK 500 1 VAL A 64 -157.31 -124.48
REMARK 500 1 ARG A 71 -71.16 -71.26
REMARK 500 1 VAL A 90 -168.13 -121.74
REMARK 500 1 LYS A 92 -68.63 -131.18
REMARK 500 1 ILE A 93 -70.35 -149.95
REMARK 500 1 THR A 94 93.66 40.35
REMARK 500 1 PHE A 95 163.40 -41.52
REMARK 500 1 SER A 96 -49.95 -160.72
REMARK 500 1 TYR A 100 121.96 -31.69
REMARK 500 1 PHE A 103 163.82 -39.71
REMARK 500 2 ALA A 13 -51.67 162.37
REMARK 500 2 THR A 16 -43.62 -153.41
REMARK 500 2 VAL A 17 -31.94 167.85
REMARK 500 2 ASP A 20 106.05 56.59
REMARK 500 2 GLU A 36 100.17 71.90
REMARK 500 2 ARG A 38 -36.12 178.98
REMARK 500 2 LYS A 44 17.59 80.99
REMARK 500 2 ALA A 48 47.83 -95.63
REMARK 500 2 ASN A 49 94.85 153.36
REMARK 500 2 VAL A 51 -55.60 174.66
REMARK 500 2 ILE A 52 173.23 54.57
REMARK 500 2 HIS A 63 -75.22 -101.06
REMARK 500 2 VAL A 64 -166.71 -117.26
REMARK 500 2 GLU A 69 -150.63 -159.62
REMARK 500 2 HIS A 88 -98.73 -118.46
REMARK 500 2 THR A 89 -36.05 -156.40
REMARK 500 2 LYS A 92 -111.24 -104.86
REMARK 500 2 ILE A 93 -72.10 -140.54
REMARK 500 2 THR A 94 110.99 55.42
REMARK 500 2 SER A 96 -53.23 -164.28
REMARK 500 2 GLU A 97 41.25 75.71
REMARK 500 2 GLN A 98 -45.19 -132.52
REMARK 500 2 CYS A 99 -144.12 -83.91
REMARK 500 2 PHE A 103 155.60 -35.41
REMARK 500 3 ALA A 13 166.84 -43.28
REMARK 500 3 THR A 16 -49.75 -150.57
REMARK 500
REMARK 500 THIS ENTRY HAS 491 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1FSH A 1 105 UNP P51141 DVL1_MOUSE 391 495
SEQRES 1 A 105 THR SER SER VAL PRO GLY ALA PRO GLN LEU GLU GLU ALA
SEQRES 2 A 105 PRO LEU THR VAL LYS SER ASP MET SER ALA ILE VAL ARG
SEQRES 3 A 105 VAL MET GLN LEU PRO ASP SER GLY LEU GLU ILE ARG ASP
SEQRES 4 A 105 ARG MET TRP LEU LYS ILE THR ILE ALA ASN ALA VAL ILE
SEQRES 5 A 105 GLY ALA ASP VAL VAL ASP TRP LEU TYR THR HIS VAL GLU
SEQRES 6 A 105 GLY PHE LYS GLU ARG ARG GLU ALA ARG LYS TYR ALA SER
SEQRES 7 A 105 SER MET LEU LYS HIS GLY PHE LEU ARG HIS THR VAL ASN
SEQRES 8 A 105 LYS ILE THR PHE SER GLU GLN CYS TYR TYR VAL PHE GLY
SEQRES 9 A 105 ASP
HELIX 1 1 ASP A 20 LEU A 30 1 11
HELIX 2 2 VAL A 51 VAL A 64 1 14
HELIX 3 3 GLU A 69 HIS A 83 1 15
SHEET 1 A 2 ARG A 40 TRP A 42 0
SHEET 2 A 2 ILE A 45 ILE A 47 -1 N ILE A 45 O TRP A 42
SHEET 1 B 2 LEU A 86 ARG A 87 0
SHEET 2 B 2 VAL A 102 PHE A 103 -1 N VAL A 102 O ARG A 87
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 - b 23 2 Bytes