HEADER CYTOSKELETON 07-JUN-01 1H67
TITLE NMR STRUCTURE OF THE CH DOMAIN OF CALPONIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALPONIN ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CALPONIN HOMOLOGY DOMAIN, RESIDUES 28-134;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 ORGAN: GIZZARD;
SOURCE 6 TISSUE: SMOOTH MUSCLE;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET PSJW1
KEYWDS CYTOSKELETON, CALPONIN HOMOLOGY DOMAIN, ACTIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR J.BRAMHAM,B.O.SMITH,D.UHRIN,P.N.BARLOW,S.J.WINDER
REVDAT 3 15-JAN-20 1H67 1 REMARK
REVDAT 2 24-FEB-09 1H67 1 VERSN
REVDAT 1 14-FEB-02 1H67 0
JRNL AUTH J.BRAMHAM,J.L.HODGKINSON,B.O.SMITH,D.UHRIN,P.N.BARLOW,
JRNL AUTH 2 S.J.WINDER
JRNL TITL SOLUTION STRUCTURE OF THE CALPONIN CH DOMAIN AND FITTING TO
JRNL TITL 2 THE 3D-HELICAL RECONSTRUCTION OF F-ACTIN:CALPONIN.
JRNL REF STRUCTURE V. 10 249 2002
JRNL REFN ISSN 0969-2126
JRNL PMID 11839310
JRNL DOI 10.1016/S0969-2126(02)00703-7
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : A.T.BRUNGER,P.D.ADAMS, G.M.CLORE,W.L.DELANO,
REMARK 3 P.GROS, R.W.GROSSE-KUNSTLEVE,J.-S.JIANG,
REMARK 3 J.KUSZEWSKI,M.NILGES,N.S.PANNU, R.J.READ, L.M.RICE,
REMARK 3 T.SIMONSON,G.L.WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE
REMARK 4
REMARK 4 1H67 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-JUN-01.
REMARK 100 THE DEPOSITION ID IS D_1290008139.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 291
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 0
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 1MM CALPONIN CH DOMAIN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 13C; 15N HSQC-NOESY-CH3NH; 13C
REMARK 210 -EDITTED NOESY-HSQC
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 : AZARA, ANSIG, CNS
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 9
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED PROTEIN.
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: 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
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 GLN A 29 -125.46 -171.09
REMARK 500 1 THR A 30 -42.37 -161.96
REMARK 500 1 GLU A 31 -31.53 -168.79
REMARK 500 1 TRP A 37 -76.12 -60.42
REMARK 500 1 ARG A 45 38.62 -94.91
REMARK 500 1 ILE A 46 72.94 39.41
REMARK 500 1 ASP A 48 -147.79 -176.92
REMARK 500 1 VAL A 58 -60.19 -156.00
REMARK 500 1 VAL A 72 48.38 -144.49
REMARK 500 1 LYS A 74 43.19 -80.54
REMARK 500 1 PRO A 78 43.27 -69.26
REMARK 500 1 GLN A 80 -124.84 -75.08
REMARK 500 1 ASN A 81 -46.89 -142.83
REMARK 500 2 THR A 30 -43.91 -161.57
REMARK 500 2 GLU A 31 -34.93 177.12
REMARK 500 2 TRP A 37 -73.22 -59.39
REMARK 500 2 ASN A 49 -133.18 -71.95
REMARK 500 2 PHE A 50 -51.18 -168.63
REMARK 500 2 VAL A 58 -56.95 -145.62
REMARK 500 2 LYS A 74 135.59 -174.06
REMARK 500 2 PRO A 78 44.57 -70.13
REMARK 500 2 GLN A 80 -123.41 -77.86
REMARK 500 2 ASN A 81 -47.11 -145.26
REMARK 500 2 ALA A 131 39.84 -83.61
REMARK 500 2 THR A 133 46.43 179.60
REMARK 500 3 THR A 30 -37.09 -174.65
REMARK 500 3 GLU A 31 -40.14 -142.43
REMARK 500 3 GLN A 33 -33.07 76.45
REMARK 500 3 ARG A 45 31.46 -80.80
REMARK 500 3 ILE A 46 -76.71 58.03
REMARK 500 3 ASP A 48 -123.60 -67.55
REMARK 500 3 LYS A 74 121.86 -172.15
REMARK 500 3 PRO A 78 39.48 -76.48
REMARK 500 3 GLN A 80 -130.98 -76.32
REMARK 500 3 ASN A 81 -46.13 -138.12
REMARK 500 3 PHE A 106 -150.10 -73.15
REMARK 500 4 THR A 30 23.66 -155.73
REMARK 500 4 ARG A 32 -43.67 -168.74
REMARK 500 4 ARG A 35 36.34 -77.48
REMARK 500 4 VAL A 36 -37.82 -154.00
REMARK 500 4 ASN A 49 -125.84 -74.83
REMARK 500 4 PHE A 50 -45.21 -169.24
REMARK 500 4 VAL A 58 -58.38 -159.20
REMARK 500 4 SER A 71 -80.23 -75.58
REMARK 500 4 GLN A 73 -140.61 -69.68
REMARK 500 4 VAL A 79 -57.22 -154.36
REMARK 500 4 GLN A 80 -125.24 -79.66
REMARK 500 4 ASN A 81 -46.86 -132.45
REMARK 500 4 PHE A 106 -154.88 -72.94
REMARK 500 4 HIS A 117 -43.75 -132.13
REMARK 500
REMARK 500 THIS ENTRY HAS 258 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4880 RELATED DB: BMRB
DBREF 1H67 A 27 134 UNP Q9PSG0 Q9PSG0 27 134
SEQADV 1H67 MET A 27 UNP Q9PSG0 ASP 27 CLONING ARTIFACT
SEQRES 1 A 108 MET PRO GLN THR GLU ARG GLN LEU ARG VAL TRP ILE GLU
SEQRES 2 A 108 GLY ALA THR GLY ARG ARG ILE GLY ASP ASN PHE MET ASP
SEQRES 3 A 108 GLY LEU LYS ASP GLY VAL ILE LEU CYS GLU LEU ILE ASN
SEQRES 4 A 108 LYS LEU GLN PRO GLY SER VAL GLN LYS VAL ASN ASP PRO
SEQRES 5 A 108 VAL GLN ASN TRP HIS LYS LEU GLU ASN ILE GLY ASN PHE
SEQRES 6 A 108 LEU ARG ALA ILE LYS HIS TYR GLY VAL LYS PRO HIS ASP
SEQRES 7 A 108 ILE PHE GLU ALA ASN ASP LEU PHE GLU ASN THR ASN HIS
SEQRES 8 A 108 THR GLN VAL GLN SER THR LEU ILE ALA LEU ALA SER GLN
SEQRES 9 A 108 ALA LYS THR LYS
HELIX 1 1 ARG A 32 THR A 42 1 11
HELIX 2 2 PHE A 50 LYS A 55 1 6
HELIX 3 3 VAL A 58 GLN A 68 1 11
HELIX 4 4 ASN A 81 GLY A 99 1 19
HELIX 5 5 LYS A 101 ILE A 105 5 5
HELIX 6 6 GLU A 107 GLU A 113 1 7
HELIX 7 7 HIS A 117 THR A 133 1 17
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