HEADER STRUCTURAL PROTEIN 25-JAN-07 2E9J
TITLE SOLUTION STRUCTURE OF THE 14TH 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_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P060619-05;
SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS BETA-SANDWICH, IMMUNOGLOBULIN-LIKE FOLD, FILAMIN, 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 2E9J 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2E9J 1 VERSN
REVDAT 1 31-JUL-07 2E9J 0
JRNL AUTH T.TOMIZAWA,S.KOSHIBA,S.WATANABE,T.HARADA,T.KIGAWA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE 14TH 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 2E9J COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-JAN-07.
REMARK 100 THE DEPOSITION ID IS D_1000026395.
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 : 1.19MM 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; 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
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 20060524, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.9747, 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 : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY, TARGET
REMARK 210 FUNCTION
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 LYS A 14 42.23 -109.04
REMARK 500 1 ASP A 20 106.67 -168.66
REMARK 500 1 LYS A 23 30.47 -89.76
REMARK 500 1 PRO A 41 97.58 -69.77
REMARK 500 1 LEU A 55 108.41 -47.14
REMARK 500 1 PRO A 86 97.32 -69.71
REMARK 500 1 THR A 89 172.98 -49.12
REMARK 500 1 PRO A 104 1.28 -69.78
REMARK 500 2 PRO A 41 98.48 -69.75
REMARK 500 2 PRO A 104 2.94 -69.74
REMARK 500 2 PRO A 107 -177.39 -69.77
REMARK 500 2 GLN A 114 44.20 -92.90
REMARK 500 3 LYS A 23 33.59 -87.98
REMARK 500 3 PRO A 41 97.17 -69.72
REMARK 500 3 PRO A 86 97.73 -69.81
REMARK 500 3 PRO A 104 3.41 -69.79
REMARK 500 3 PRO A 107 -179.32 -69.75
REMARK 500 3 GLN A 114 46.57 -78.27
REMARK 500 4 SER A 2 142.66 -172.99
REMARK 500 4 PRO A 41 97.81 -69.71
REMARK 500 4 LEU A 55 106.62 -59.25
REMARK 500 4 PRO A 86 91.14 -69.75
REMARK 500 4 ASP A 87 33.33 -93.84
REMARK 500 4 PRO A 104 3.07 -69.74
REMARK 500 5 SER A 9 143.39 -172.73
REMARK 500 5 PRO A 10 -165.74 -69.77
REMARK 500 5 SER A 39 37.76 36.21
REMARK 500 5 PRO A 41 98.01 -69.77
REMARK 500 5 LEU A 55 105.99 -51.55
REMARK 500 5 PRO A 86 88.14 -69.79
REMARK 500 5 PRO A 104 3.01 -69.75
REMARK 500 5 PRO A 107 -176.94 -69.79
REMARK 500 6 SER A 2 118.68 -168.82
REMARK 500 6 ARG A 8 107.13 -172.75
REMARK 500 6 PHE A 11 41.54 38.25
REMARK 500 6 LYS A 12 41.79 -84.10
REMARK 500 6 SER A 39 45.81 38.93
REMARK 500 6 PRO A 41 98.40 -69.77
REMARK 500 6 LEU A 55 99.37 -67.01
REMARK 500 6 PRO A 86 98.44 -69.82
REMARK 500 6 PRO A 104 2.74 -69.72
REMARK 500 6 PRO A 107 -177.25 -69.71
REMARK 500 7 SER A 6 -64.14 -103.50
REMARK 500 7 PRO A 10 92.73 -69.75
REMARK 500 7 PHE A 11 118.64 -174.28
REMARK 500 7 LYS A 23 33.45 -91.24
REMARK 500 7 SER A 39 43.74 38.58
REMARK 500 7 PRO A 41 97.42 -69.79
REMARK 500 7 PRO A 86 93.43 -69.75
REMARK 500 7 PRO A 104 3.20 -69.81
REMARK 500
REMARK 500 THIS ENTRY HAS 134 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: HSK003002600.13 RELATED DB: TARGETDB
DBREF 2E9J A 8 119 UNP O75369 FLNB_HUMAN 1504 1615
SEQADV 2E9J GLY A 1 UNP O75369 CLONING ARTIFACT
SEQADV 2E9J SER A 2 UNP O75369 CLONING ARTIFACT
SEQADV 2E9J SER A 3 UNP O75369 CLONING ARTIFACT
SEQADV 2E9J GLY A 4 UNP O75369 CLONING ARTIFACT
SEQADV 2E9J SER A 5 UNP O75369 CLONING ARTIFACT
SEQADV 2E9J SER A 6 UNP O75369 CLONING ARTIFACT
SEQADV 2E9J GLY A 7 UNP O75369 CLONING ARTIFACT
SEQRES 1 A 119 GLY SER SER GLY SER SER GLY ARG SER PRO PHE LYS VAL
SEQRES 2 A 119 LYS VAL LEU PRO THR TYR ASP ALA SER LYS VAL THR ALA
SEQRES 3 A 119 SER GLY PRO GLY LEU SER SER TYR GLY VAL PRO ALA SER
SEQRES 4 A 119 LEU PRO VAL ASP PHE ALA ILE ASP ALA ARG ASP ALA GLY
SEQRES 5 A 119 GLU GLY LEU LEU ALA VAL GLN ILE THR ASP GLN GLU GLY
SEQRES 6 A 119 LYS PRO LYS ARG ALA ILE VAL HIS ASP ASN LYS ASP GLY
SEQRES 7 A 119 THR TYR ALA VAL THR TYR ILE PRO ASP LYS THR GLY ARG
SEQRES 8 A 119 TYR MET ILE GLY VAL THR TYR GLY GLY ASP ASP ILE PRO
SEQRES 9 A 119 LEU SER PRO TYR ARG ILE ARG ALA THR GLN THR GLY ASP
SEQRES 10 A 119 ALA SER
HELIX 1 1 ASP A 20 SER A 22 5 3
HELIX 2 2 GLY A 28 SER A 32 5 5
SHEET 1 A 4 VAL A 24 SER A 27 0
SHEET 2 A 4 VAL A 42 ALA A 48 -1 O ALA A 45 N SER A 27
SHEET 3 A 4 THR A 79 TYR A 84 -1 O TYR A 84 N VAL A 42
SHEET 4 A 4 ALA A 70 ASP A 74 -1 N HIS A 73 O ALA A 81
SHEET 1 B 4 VAL A 36 PRO A 37 0
SHEET 2 B 4 TYR A 108 THR A 113 1 O THR A 113 N VAL A 36
SHEET 3 B 4 ARG A 91 ILE A 94 -1 N TYR A 92 O ILE A 110
SHEET 4 B 4 ILE A 60 THR A 61 -1 N THR A 61 O MET A 93
SHEET 1 C 2 LEU A 56 ALA A 57 0
SHEET 2 C 2 THR A 97 TYR A 98 -1 O THR A 97 N ALA A 57
CISPEP 1 SER A 106 PRO A 107 1 -0.02
CISPEP 2 SER A 106 PRO A 107 2 0.03
CISPEP 3 SER A 106 PRO A 107 3 -0.05
CISPEP 4 SER A 106 PRO A 107 4 0.03
CISPEP 5 SER A 106 PRO A 107 5 0.06
CISPEP 6 SER A 106 PRO A 107 6 -0.08
CISPEP 7 SER A 106 PRO A 107 7 -0.06
CISPEP 8 SER A 106 PRO A 107 8 0.07
CISPEP 9 SER A 106 PRO A 107 9 0.05
CISPEP 10 SER A 106 PRO A 107 10 -0.09
CISPEP 11 SER A 106 PRO A 107 11 -0.04
CISPEP 12 SER A 106 PRO A 107 12 0.03
CISPEP 13 SER A 106 PRO A 107 13 -0.05
CISPEP 14 SER A 106 PRO A 107 14 -0.06
CISPEP 15 SER A 106 PRO A 107 15 -0.05
CISPEP 16 SER A 106 PRO A 107 16 -0.06
CISPEP 17 SER A 106 PRO A 107 17 -0.05
CISPEP 18 SER A 106 PRO A 107 18 0.01
CISPEP 19 SER A 106 PRO A 107 19 -0.13
CISPEP 20 SER A 106 PRO A 107 20 -0.02
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
