HEADER STRUCTURAL PROTEIN 24-NOV-05 2D7Q
TITLE SOLUTION STRUCTURE OF THE 23TH FILAMIN DOMAIN FROM HUMAN
TITLE 2 FILAMIN C
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FILAMIN-C;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: FILAMIN DOMAIN;
COMPND 5 SYNONYM: GAMMA-FILAMIN, FILAMIN-2, PROTEIN FLNC, ACTIN-
COMPND 6 BINDING-LIKE PROTEIN, ABP-L, ABP-280-LIKE PROTEIN;
COMPND 7 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: FLNC;
SOURCE 6 EXPRESSION_SYSTEM: SYNTHETIC CONSTRUCT;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 32630;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: P050404-09;
SOURCE 10 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS
KEYWDS BETA-SANDWICH, IMMUNOGLOBULIN-LIKE FOLD, FILAMIN DOMAIN,
KEYWDS 2 STRUCTURAL GENOMICS, NPPSFA, NATIONAL PROJECT ON PROTEIN
KEYWDS 3 STRUCTURAL AND FUNCTIONAL ANALYSES, RIKEN STRUCTURAL
KEYWDS 4 GENOMICS/PROTEOMICS INITIATIVE, RSGI, STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 2 24-FEB-09 2D7Q 1 VERSN
REVDAT 1 24-NOV-06 2D7Q 0
JRNL AUTH T.TOMIZAWA,T.KIGAWA,S.KOSHIBA,M.INOUE,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE 23TH FILAMIN DOMAIN FROM
JRNL TITL 2 HUMAN FILAMIN C
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.0.17
REMARK 3 AUTHORS : GUNTERT, P.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2D7Q COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-NOV-05.
REMARK 100 THE RCSB ID CODE IS RCSB025091.
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 : 1.13MM 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_
REMARK 210 13C-SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.5, NMRPIPE
REMARK 210 20030801, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.932, 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
REMARK 210 WITH THE LOWEST ENERGY,
REMARK 210 STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT 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 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 2 155.09 -45.43
REMARK 500 1 SER A 29 107.89 -45.38
REMARK 500 1 LYS A 53 149.48 -39.38
REMARK 500 1 PRO A 62 1.25 -69.81
REMARK 500 2 SER A 29 103.08 -43.62
REMARK 500 2 SER A 52 116.80 -165.57
REMARK 500 2 LYS A 53 149.12 -34.42
REMARK 500 2 PRO A 62 1.47 -69.75
REMARK 500 2 TYR A 83 114.84 -171.68
REMARK 500 2 ARG A 102 93.56 -59.29
REMARK 500 2 LEU A 103 53.70 -93.60
REMARK 500 2 SER A 109 -56.89 -123.85
REMARK 500 3 ASP A 10 104.96 -162.41
REMARK 500 3 SER A 29 106.51 -53.31
REMARK 500 3 PRO A 62 0.09 -69.76
REMARK 500 3 ARG A 102 90.36 -68.18
REMARK 500 4 LYS A 53 145.29 -34.48
REMARK 500 4 VAL A 90 108.91 -59.33
REMARK 500 4 ARG A 102 106.91 -57.03
REMARK 500 5 VAL A 90 104.38 -51.49
REMARK 500 6 ASP A 10 114.34 -166.23
REMARK 500 6 SER A 41 142.67 -174.45
REMARK 500 6 ARG A 102 100.64 -50.20
REMARK 500 6 PRO A 108 92.98 -69.74
REMARK 500 7 PRO A 93 -177.67 -69.75
REMARK 500 8 SER A 29 102.92 -55.05
REMARK 500 8 LYS A 53 133.36 -37.74
REMARK 500 8 PRO A 62 0.96 -69.76
REMARK 500 8 VAL A 90 107.97 -48.88
REMARK 500 8 ARG A 102 130.71 -36.61
REMARK 500 8 SER A 110 73.75 -101.01
REMARK 500 9 SER A 5 118.84 -163.75
REMARK 500 9 ASP A 10 116.26 -170.35
REMARK 500 9 VAL A 90 100.16 -49.13
REMARK 500 9 ARG A 102 101.69 -36.70
REMARK 500 9 PRO A 108 1.25 -69.72
REMARK 500 10 SER A 5 131.27 -173.13
REMARK 500 10 SER A 29 104.00 -46.98
REMARK 500 10 ASN A 35 98.67 -69.54
REMARK 500 10 PRO A 62 0.74 -69.79
REMARK 500 11 SER A 5 130.31 -173.28
REMARK 500 11 LYS A 53 146.79 -34.59
REMARK 500 11 PRO A 62 1.19 -69.73
REMARK 500 11 ARG A 102 79.31 -69.23
REMARK 500 12 LYS A 53 139.95 -34.44
REMARK 500 12 PRO A 62 1.26 -69.74
REMARK 500 12 ARG A 102 108.26 -35.25
REMARK 500 13 SER A 3 41.79 -107.09
REMARK 500 13 ALA A 8 138.06 -172.48
REMARK 500 13 SER A 29 101.95 -41.04
REMARK 500 13 ASN A 35 97.76 -69.42
REMARK 500 13 LYS A 53 141.51 -37.65
REMARK 500 13 ARG A 102 105.92 -42.96
REMARK 500 13 SER A 109 122.74 -174.67
REMARK 500 14 ASP A 10 116.64 -171.29
REMARK 500 14 LYS A 53 139.49 -35.30
REMARK 500 14 TYR A 83 131.51 -170.29
REMARK 500 14 VAL A 90 102.35 -54.02
REMARK 500 15 SER A 29 101.53 -50.65
REMARK 500 15 TYR A 83 105.01 -170.96
REMARK 500 15 VAL A 90 99.21 -53.87
REMARK 500 15 SER A 109 109.26 -56.09
REMARK 500 15 SER A 110 45.24 39.66
REMARK 500 16 ASP A 10 116.06 -170.01
REMARK 500 16 ASN A 35 98.78 -69.78
REMARK 500 16 LYS A 53 150.04 -45.34
REMARK 500 16 PRO A 93 -178.71 -69.76
REMARK 500 16 LEU A 103 52.64 -103.54
REMARK 500 17 ARG A 102 88.87 -48.52
REMARK 500 17 LEU A 103 48.08 -86.19
REMARK 500 18 ASP A 10 117.61 -173.66
REMARK 500 18 SER A 29 106.05 -51.75
REMARK 500 18 SER A 110 86.33 -69.15
REMARK 500 19 SER A 6 109.56 -161.26
REMARK 500 19 PRO A 62 0.98 -69.80
REMARK 500 19 PRO A 86 2.09 -69.82
REMARK 500 19 LEU A 103 46.74 -82.86
REMARK 500 19 SER A 106 137.64 -37.92
REMARK 500 20 SER A 3 161.97 -44.66
REMARK 500 20 PRO A 62 0.12 -69.81
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2D7Q A 8 105 UNP Q14315 FLNC_HUMAN 2500 2599
SEQADV 2D7Q GLY A 1 UNP Q14315 CLONING ARTIFACT
SEQADV 2D7Q SER A 2 UNP Q14315 CLONING ARTIFACT
SEQADV 2D7Q SER A 3 UNP Q14315 CLONING ARTIFACT
SEQADV 2D7Q GLY A 4 UNP Q14315 CLONING ARTIFACT
SEQADV 2D7Q SER A 5 UNP Q14315 CLONING ARTIFACT
SEQADV 2D7Q SER A 6 UNP Q14315 CLONING ARTIFACT
SEQADV 2D7Q GLY A 7 UNP Q14315 CLONING ARTIFACT
SEQADV 2D7Q SER A 106 UNP Q14315 CLONING ARTIFACT
SEQADV 2D7Q GLY A 107 UNP Q14315 CLONING ARTIFACT
SEQADV 2D7Q PRO A 108 UNP Q14315 CLONING ARTIFACT
SEQADV 2D7Q SER A 109 UNP Q14315 CLONING ARTIFACT
SEQADV 2D7Q SER A 110 UNP Q14315 CLONING ARTIFACT
SEQADV 2D7Q GLY A 111 UNP Q14315 CLONING ARTIFACT
SEQRES 1 A 111 GLY SER SER GLY SER SER GLY ALA GLY ASP PRO GLY LEU
SEQRES 2 A 111 VAL SER ALA TYR GLY PRO GLY LEU GLU GLY GLY THR THR
SEQRES 3 A 111 GLY VAL SER SER GLU PHE ILE VAL ASN THR LEU ASN ALA
SEQRES 4 A 111 GLY SER GLY ALA LEU SER VAL THR ILE ASP GLY PRO SER
SEQRES 5 A 111 LYS VAL GLN LEU ASP CYS ARG GLU CYS PRO GLU GLY HIS
SEQRES 6 A 111 VAL VAL THR TYR THR PRO MET ALA PRO GLY ASN TYR LEU
SEQRES 7 A 111 ILE ALA ILE LYS TYR GLY GLY PRO GLN HIS ILE VAL GLY
SEQRES 8 A 111 SER PRO PHE LYS ALA LYS VAL THR GLY PRO ARG LEU SER
SEQRES 9 A 111 GLY SER GLY PRO SER SER GLY
HELIX 1 1 ASP A 10 VAL A 14 5 5
HELIX 2 2 GLY A 18 GLY A 23 1 6
SHEET 1 A 4 SER A 15 TYR A 17 0
SHEET 2 A 4 SER A 30 ASN A 35 -1 O ILE A 33 N TYR A 17
SHEET 3 A 4 GLY A 64 THR A 70 -1 O TYR A 69 N SER A 30
SHEET 4 A 4 GLN A 55 CYS A 61 -1 N ARG A 59 O VAL A 66
SHEET 1 B 3 LEU A 44 THR A 47 0
SHEET 2 B 3 GLY A 75 TYR A 83 -1 O LYS A 82 N SER A 45
SHEET 3 B 3 PHE A 94 VAL A 98 -1 O PHE A 94 N ILE A 79
CISPEP 1 SER A 92 PRO A 93 1 -0.03
CISPEP 2 SER A 92 PRO A 93 2 0.00
CISPEP 3 SER A 92 PRO A 93 3 -0.04
CISPEP 4 SER A 92 PRO A 93 4 -0.10
CISPEP 5 SER A 92 PRO A 93 5 0.05
CISPEP 6 SER A 92 PRO A 93 6 0.00
CISPEP 7 SER A 92 PRO A 93 7 -0.02
CISPEP 8 SER A 92 PRO A 93 8 0.00
CISPEP 9 SER A 92 PRO A 93 9 -0.07
CISPEP 10 SER A 92 PRO A 93 10 0.02
CISPEP 11 SER A 92 PRO A 93 11 0.00
CISPEP 12 SER A 92 PRO A 93 12 0.00
CISPEP 13 SER A 92 PRO A 93 13 0.00
CISPEP 14 SER A 92 PRO A 93 14 0.00
CISPEP 15 SER A 92 PRO A 93 15 0.03
CISPEP 16 SER A 92 PRO A 93 16 -0.03
CISPEP 17 SER A 92 PRO A 93 17 0.02
CISPEP 18 SER A 92 PRO A 93 18 -0.09
CISPEP 19 SER A 92 PRO A 93 19 -0.06
CISPEP 20 SER A 92 PRO A 93 20 -0.04
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
