HEADER STRUCTURAL PROTEIN 20-APR-06 2DMC
TITLE SOLUTION STRUCTURE OF THE 18TH FILAMIN DOMAIN FROM HUMAN FILAMIN-B
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FILAMIN-B;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FILAMIN DOMAIN;
COMPND 5 SYNONYM: FLN-B, BETA-FILAMIN, ACTIN-BINDING-LIKE PROTEIN, THYROID
COMPND 6 AUTOANTIGEN, TRUNCATED ACTIN-BINDING PROTEIN, TRUNCATED ABP, ABP- 280
COMPND 7 HOMOLOG, ABP-278, FILAMIN 3, FILAMIN HOMOLOG 1, FH1;
COMPND 8 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: FLNB;
SOURCE 6 EXPRESSION_SYSTEM: CELL FREE SYNTHESIS;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: P051205-16;
SOURCE 9 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS BETA-SANDWICH, IMMUNOGLOBULIN-LIKE FOLD, FILAMIN DOMAIN, STRUCTURAL
KEYWDS 2 GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN STRUCTURAL AND
KEYWDS 3 FUNCTIONAL ANALYSES, RIKEN STRUCTURAL GENOMICS/PROTEOMICS
KEYWDS 4 INITIATIVE, RSGI, STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.TOMIZAWA,S.KOSHIBA,S.WATANABE,T.HARADA,T.KIGAWA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 09-MAR-22 2DMC 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2DMC 1 VERSN
REVDAT 1 20-OCT-06 2DMC 0
JRNL AUTH T.TOMIZAWA,S.KOSHIBA,S.WATANABE,T.HARADA,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE 18TH FILAMIN DOMAIN FROM HUMAN
JRNL TITL 2 FILAMIN-B
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TOPSPIN 1.3, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (TOPSPIN), GUNTERT, P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2DMC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 25-APR-06.
REMARK 100 THE DEPOSITION ID IS D_1000025583.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.14MM FILAMIN DOMAIN U-15N,
REMARK 210 13C; 20MM D-TRIS-HCL (PH 7.0);
REMARK 210 100MM NACL; 1MM D-DTT; 0.02%
REMARK 210 NAN3; 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE II
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20060324, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9742, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS,
REMARK 210 RESTRAINTED MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION, STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY, STRUCTURES
REMARK 210 WITH THE LEAST RESTRAINT
REMARK 210 VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
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 6 53.41 37.99
REMARK 500 1 SER A 11 143.81 -174.79
REMARK 500 1 PRO A 12 -173.29 -69.88
REMARK 500 1 ASP A 19 115.18 -168.13
REMARK 500 1 SER A 21 35.32 -86.90
REMARK 500 1 ARG A 22 169.62 -44.90
REMARK 500 1 ARG A 23 42.67 -84.48
REMARK 500 1 SER A 40 37.74 -83.53
REMARK 500 1 ASP A 43 122.58 -38.49
REMARK 500 1 ALA A 53 169.00 -43.64
REMARK 500 1 PRO A 67 -174.04 -69.80
REMARK 500 1 HIS A 93 141.56 -37.97
REMARK 500 1 SER A 115 174.91 -50.02
REMARK 500 2 PHE A 13 85.81 -57.19
REMARK 500 2 ILE A 17 170.50 -48.53
REMARK 500 2 ASP A 20 87.27 -60.35
REMARK 500 2 SER A 21 78.62 -64.90
REMARK 500 2 ALA A 53 168.45 -43.33
REMARK 500 2 PRO A 60 91.52 -69.84
REMARK 500 2 HIS A 93 143.28 -36.39
REMARK 500 2 SER A 106 120.60 -39.54
REMARK 500 2 ILE A 108 45.44 34.05
REMARK 500 2 SER A 111 134.11 -39.52
REMARK 500 3 ASP A 43 106.77 -43.80
REMARK 500 3 ALA A 53 167.64 -48.39
REMARK 500 3 PRO A 60 93.11 -69.77
REMARK 500 3 ASN A 69 42.74 34.16
REMARK 500 3 HIS A 93 145.55 -35.22
REMARK 500 3 GLN A 105 98.15 -65.17
REMARK 500 4 SER A 2 127.50 -171.31
REMARK 500 4 LYS A 16 109.24 -40.22
REMARK 500 4 SER A 40 34.37 -84.24
REMARK 500 4 ALA A 53 169.31 -43.84
REMARK 500 4 HIS A 93 141.24 -35.55
REMARK 500 4 SER A 106 100.32 -56.68
REMARK 500 4 SER A 114 107.88 -34.69
REMARK 500 5 SER A 40 44.28 -81.71
REMARK 500 5 THR A 42 -69.57 -109.73
REMARK 500 5 ASP A 43 123.93 -35.37
REMARK 500 5 ALA A 53 169.37 -44.45
REMARK 500 5 PRO A 60 90.34 -69.73
REMARK 500 5 HIS A 93 147.06 -35.64
REMARK 500 6 PRO A 12 -172.44 -69.70
REMARK 500 6 SER A 21 41.53 -98.25
REMARK 500 6 ASP A 43 109.94 -34.89
REMARK 500 6 ALA A 53 169.60 -43.76
REMARK 500 6 PRO A 60 87.69 -69.77
REMARK 500 6 HIS A 93 141.12 -34.47
REMARK 500 7 SER A 40 44.54 -80.05
REMARK 500 7 LEU A 44 -74.96 -43.91
REMARK 500
REMARK 500 THIS ENTRY HAS 158 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK003002600.9 RELATED DB: TARGETDB
DBREF 2DMC A 8 110 UNP O75369 FLNB_HUMAN 1899 2001
SEQADV 2DMC GLY A 1 UNP O75369 CLONING ARTIFACT
SEQADV 2DMC SER A 2 UNP O75369 CLONING ARTIFACT
SEQADV 2DMC SER A 3 UNP O75369 CLONING ARTIFACT
SEQADV 2DMC GLY A 4 UNP O75369 CLONING ARTIFACT
SEQADV 2DMC SER A 5 UNP O75369 CLONING ARTIFACT
SEQADV 2DMC SER A 6 UNP O75369 CLONING ARTIFACT
SEQADV 2DMC GLY A 7 UNP O75369 CLONING ARTIFACT
SEQADV 2DMC SER A 111 UNP O75369 CLONING ARTIFACT
SEQADV 2DMC GLY A 112 UNP O75369 CLONING ARTIFACT
SEQADV 2DMC PRO A 113 UNP O75369 CLONING ARTIFACT
SEQADV 2DMC SER A 114 UNP O75369 CLONING ARTIFACT
SEQADV 2DMC SER A 115 UNP O75369 CLONING ARTIFACT
SEQADV 2DMC GLY A 116 UNP O75369 CLONING ARTIFACT
SEQRES 1 A 116 GLY SER SER GLY SER SER GLY ILE PRO GLY SER PRO PHE
SEQRES 2 A 116 THR ALA LYS ILE THR ASP ASP SER ARG ARG CYS SER GLN
SEQRES 3 A 116 VAL LYS LEU GLY SER ALA ALA ASP PHE LEU LEU ASP ILE
SEQRES 4 A 116 SER GLU THR ASP LEU SER SER LEU THR ALA SER ILE LYS
SEQRES 5 A 116 ALA PRO SER GLY ARG ASP GLU PRO CYS LEU LEU LYS ARG
SEQRES 6 A 116 LEU PRO ASN ASN HIS ILE GLY ILE SER PHE ILE PRO ARG
SEQRES 7 A 116 GLU VAL GLY GLU HIS LEU VAL SER ILE LYS LYS ASN GLY
SEQRES 8 A 116 ASN HIS VAL ALA ASN SER PRO VAL SER ILE MET VAL VAL
SEQRES 9 A 116 GLN SER GLU ILE GLY ASP SER GLY PRO SER SER GLY
SHEET 1 A 3 ALA A 33 LEU A 36 0
SHEET 2 A 3 HIS A 70 PHE A 75 -1 O PHE A 75 N ALA A 33
SHEET 3 A 3 CYS A 61 LEU A 66 -1 N LEU A 62 O SER A 74
SHEET 1 B 3 SER A 50 LYS A 52 0
SHEET 2 B 3 GLY A 81 SER A 86 -1 O SER A 86 N SER A 50
SHEET 3 B 3 VAL A 99 VAL A 103 -1 O VAL A 99 N VAL A 85
CISPEP 1 SER A 97 PRO A 98 1 -0.07
CISPEP 2 SER A 97 PRO A 98 2 0.08
CISPEP 3 SER A 97 PRO A 98 3 -0.01
CISPEP 4 SER A 97 PRO A 98 4 -0.05
CISPEP 5 SER A 97 PRO A 98 5 0.05
CISPEP 6 SER A 97 PRO A 98 6 -0.03
CISPEP 7 SER A 97 PRO A 98 7 -0.03
CISPEP 8 SER A 97 PRO A 98 8 0.06
CISPEP 9 SER A 97 PRO A 98 9 0.02
CISPEP 10 SER A 97 PRO A 98 10 -0.04
CISPEP 11 SER A 97 PRO A 98 11 0.05
CISPEP 12 SER A 97 PRO A 98 12 0.02
CISPEP 13 SER A 97 PRO A 98 13 -0.13
CISPEP 14 SER A 97 PRO A 98 14 0.02
CISPEP 15 SER A 97 PRO A 98 15 -0.03
CISPEP 16 SER A 97 PRO A 98 16 0.00
CISPEP 17 SER A 97 PRO A 98 17 -0.02
CISPEP 18 SER A 97 PRO A 98 18 0.07
CISPEP 19 SER A 97 PRO A 98 19 -0.11
CISPEP 20 SER A 97 PRO A 98 20 0.05
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
