HEADER SIGNALING PROTEIN 03-DEC-09 2KR3
TITLE SOLUTION STRUCTURE OF SHA-D
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SPECTRIN ALPHA CHAIN, BRAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ALPHA SPECTRIN SH3 DOMAIN;
COMPND 5 SYNONYM: SHA-D, SPECTRIN, NON-ERYTHROID ALPHA CHAIN, FODRIN ALPHA
COMPND 6 CHAIN;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 GENE: SHA-D;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: VECTOR;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PBAT-4
KEYWDS ALPHA SPECTRIN SH3 DOMAIN, BERGERAC, ACTIN CAPPING, ACTIN-BINDING,
KEYWDS 2 CYTOSKELETON, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR V.S.KHRISTOFOROV,D.A.PROKHOROV,M.A.TIMCHENKO,Y.A.KUDREVATYKH,
AUTHOR 2 L.V.GUSHCHINA,V.V.FILIMONOV,V.P.KUTYSHENKO
REVDAT 2 20-OCT-10 2KR3 1 JRNL
REVDAT 1 15-SEP-10 2KR3 0
JRNL AUTH V.S.KHRISTOFOROV,D.A.PROKHOROV,M.A.TIMCHENKO,
JRNL AUTH 2 Y.A.KUDREVATYKH,L.V.GUSHCHINA,V.V.FILIMONOV,V.P.KUTYSHENKO
JRNL TITL CHIMERIC SHA-D DOMAIN "SH3-BERGERAC": 3D STRUCTURE AND
JRNL TITL 2 DYNAMICS STUDIES
JRNL REF RUSS.J.BIOORGANIC CHEM. V. 36 468 2010
JRNL REFN ISSN 1068-1620
JRNL PMID 20823919
JRNL DOI 10.1134/S1068162010040059
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH A.-R.VIGUERA,L.SERRANO
REMARK 1 TITL BERGERAC-SH3: "FRUSTATION" INDUCED BY STABILIZING THE
REMARK 1 TITL 2 FOLDING NUCLEUS
REMARK 1 REF J.MOL.BIOL. V. 311 357 2001
REMARK 1 REFN ISSN 0022-2836
REMARK 1 PMID 11478866
REMARK 1 DOI 10.1006/JMBI.2001.4738
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CYANA 2.1
REMARK 3 AUTHORS : GUNTERT, MUMENTHALER AND WUTHRICH
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2KR3 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-DEC-09.
REMARK 100 THE RCSB ID CODE IS RCSB101468.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 3.5
REMARK 210 IONIC STRENGTH : 20
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5MM [U-98% 13C; U-98% 15N] SHA
REMARK 210 -D; 20MM [U-99% 2H] SODIUM
REMARK 210 ACETATE; 0.03% SODIUM AZIDE; 90%
REMARK 210 H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 3D HNCACB; 3D
REMARK 210 CC(CO)NH; 3D HCCH-TOCSY-ALI; 3D
REMARK 210 HCCH-TOCSY-ARO; 3D 1H-15N TOCSY;
REMARK 210 3D 1H-15N NOESY; 3D 1H-13C NOESY-
REMARK 210 ALI; 3D 1H-13C NOESY-ARO; 3D HNCO
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CYANA 2.1, XWINNMR 3.5, CARA,
REMARK 210 TALOS, MOLMOL
REMARK 210 METHOD USED : TORSION ANGLE 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
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 ALA A 50 137.28 -178.29
REMARK 500 1 LEU A 69 -69.31 -96.02
REMARK 500 2 GLU A 3 56.79 -97.62
REMARK 500 2 ASP A 40 -71.44 -64.00
REMARK 500 2 ASP A 52 22.49 -141.78
REMARK 500 3 GLU A 3 49.88 -94.98
REMARK 500 3 LEU A 34 -53.70 -121.84
REMARK 500 3 ASP A 40 -74.77 -63.95
REMARK 500 3 ALA A 50 135.59 -177.82
REMARK 500 3 LYS A 67 115.11 -161.61
REMARK 500 4 ALA A 50 134.26 -177.59
REMARK 500 4 LYS A 67 117.93 -162.10
REMARK 500 5 THR A 37 39.63 -93.83
REMARK 500 5 ASN A 38 100.54 -166.88
REMARK 500 5 ALA A 50 131.57 -176.17
REMARK 500 6 GLU A 3 41.04 -94.14
REMARK 500 6 LYS A 6 146.57 -174.12
REMARK 500 6 ASP A 52 22.10 -154.45
REMARK 500 7 ASP A 2 65.80 66.21
REMARK 500 7 LYS A 6 144.48 -170.06
REMARK 500 7 ASP A 40 -73.72 -64.83
REMARK 500 7 ALA A 50 139.14 -173.94
REMARK 500 7 LEU A 69 -63.26 -95.03
REMARK 500 8 ASP A 2 76.05 63.54
REMARK 500 8 LYS A 6 88.12 -67.56
REMARK 500 8 GLU A 17 81.18 -69.41
REMARK 500 8 THR A 37 40.90 -93.33
REMARK 500 8 ASN A 38 97.80 -170.57
REMARK 500 8 ALA A 50 136.87 -175.22
REMARK 500 8 LYS A 67 114.07 -161.03
REMARK 500 8 LEU A 69 -66.43 -103.30
REMARK 500 9 GLU A 3 63.03 -115.89
REMARK 500 9 THR A 37 33.33 -94.54
REMARK 500 9 ASP A 40 -71.55 -65.53
REMARK 500 9 ALA A 50 138.55 -178.18
REMARK 500 9 LYS A 67 113.94 -162.00
REMARK 500 9 LEU A 69 -61.85 -93.91
REMARK 500 10 ASP A 2 138.94 -172.92
REMARK 500 10 LYS A 6 146.53 -173.94
REMARK 500 10 GLU A 17 81.46 -69.93
REMARK 500 10 ASP A 52 22.22 -154.64
REMARK 500 11 LYS A 27 105.26 -51.57
REMARK 500 11 ASP A 40 -73.87 -66.37
REMARK 500 11 ASP A 52 21.99 -143.17
REMARK 500 12 ASP A 2 66.41 66.37
REMARK 500 12 LYS A 27 109.38 -52.04
REMARK 500 12 ALA A 50 135.14 -174.10
REMARK 500 13 THR A 37 41.84 -94.95
REMARK 500 13 ASN A 38 98.35 -169.58
REMARK 500 13 ASP A 40 -70.39 -67.03
REMARK 500
REMARK 500 THIS ENTRY HAS 77 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2RMO RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF ALPHA-SPECTRIN_SH3-BERGERAC FROM
REMARK 900 CHICKEN
REMARK 900 RELATED ID: 16622 RELATED DB: BMRB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THIS IS ANALOGUE OF SHA PROTEIN. THERE IS INSERTION OF BETA SHEET
REMARK 999 INCLUDING 47-56 RESIDUES (KATANDKTYE) BETWEEN 46-49 OF SH3-PWT
REMARK 999 (1SHG).
DBREF 2KR3 A 2 70 UNP P07751 SPTA2_CHICK 965 1025
SEQADV 2KR3 MET A 1 UNP P07751 INITIATING METHIONINE
SEQADV 2KR3 LYS A 47 UNP P07751 SEE REMARK 999
SEQADV 2KR3 ALA A 48 UNP P07751 SEE REMARK 999
SEQADV 2KR3 THR A 49 UNP P07751 SEE REMARK 999
SEQADV 2KR3 ALA A 50 UNP P07751 SEE REMARK 999
SEQADV 2KR3 ASN A 51 UNP P07751 SEE REMARK 999
SEQADV 2KR3 ASP A 52 UNP P07751 SEE REMARK 999
SEQADV 2KR3 LYS A 53 UNP P07751 SEE REMARK 999
SEQADV 2KR3 THR A 54 UNP P07751 SEE REMARK 999
SEQADV 2KR3 TYR A 55 UNP P07751 SEE REMARK 999
SEQADV 2KR3 GLU A 56 UNP P07751 SEE REMARK 999
SEQRES 1 A 70 MET ASP GLU THR GLY LYS GLU LEU VAL LEU ALA LEU TYR
SEQRES 2 A 70 ASP TYR GLN GLU LYS SER PRO ARG GLU VAL THR MET LYS
SEQRES 3 A 70 LYS GLY ASP ILE LEU THR LEU LEU ASN SER THR ASN LYS
SEQRES 4 A 70 ASP TRP TRP LYS VAL GLU VAL LYS ALA THR ALA ASN ASP
SEQRES 5 A 70 LYS THR TYR GLU ARG GLN GLY PHE VAL PRO ALA ALA TYR
SEQRES 6 A 70 VAL LYS LYS LEU ASP
SHEET 1 A 5 GLU A 56 PRO A 62 0
SHEET 2 A 5 TRP A 41 LYS A 47 -1 N TRP A 42 O VAL A 61
SHEET 3 A 5 ILE A 30 ASN A 35 -1 N LEU A 34 O LYS A 43
SHEET 4 A 5 LEU A 8 ALA A 11 -1 N VAL A 9 O LEU A 31
SHEET 5 A 5 VAL A 66 LYS A 68 -1 O LYS A 67 N LEU A 10
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
