HEADER PROTEIN BINDING 30-MAR-05 1Z87
TITLE SOLUTION STRUCTURE OF THE SPLIT PH-PDZ SUPRAMODULE OF ALPHA-SYNTROPHIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ALPHA-1-SYNTROPHIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: THE PHN-PDZ-PHC TANDEM;
COMPND 5 SYNONYM: ALPHA-SYNTROPHIN, 59 KDA DYSTROPHIN-ASSOCIATED PROTEIN A1,
COMPND 6 ACIDIC COMPONENT 1, SYNTROPHIN 1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET32A(MODIFIED VERSION)
KEYWDS ALPHA-1-SYNTROPHIN, PROTEIN BINDING
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR J.YAN,W.XU,W.WEN,J.F.LONG,M.E.ADAMS,S.C.FROEHNER,M.ZHANG
REVDAT 3 02-MAR-22 1Z87 1 REMARK
REVDAT 2 24-FEB-09 1Z87 1 VERSN
REVDAT 1 24-JAN-06 1Z87 0
JRNL AUTH J.YAN,W.WEN,W.XU,J.F.LONG,M.E.ADAMS,S.C.FROEHNER,M.ZHANG
JRNL TITL STRUCTURE OF THE SPLIT PH DOMAIN AND DISTINCT LIPID-BINDING
JRNL TITL 2 PROPERTIES OF THE PH-PDZ SUPRAMODULE OF ALPHA-SYNTROPHIN
JRNL REF EMBO J. V. 24 3985 2005
JRNL REFN ISSN 0261-4189
JRNL PMID 16252003
JRNL DOI 10.1038/SJ.EMBOJ.7600858
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUGER, A.T.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 2924 RESTRAINTS, 2600 ARE
REMARK 3 NOE-DERIVED DISTANCE CONSTRAINTS, 184 DIHEDRAL ANGLE RESTRAINTS,
REMARK 3 140 DISTANCE RESTRAINTS FROM HYDROGEN BONDS.
REMARK 3 THIS ENSEMBLE STRUCTURE COULD NOT BE SUPERIMPOSED BECAUSE THIS
REMARK 3 PROTEIN FRAGMENT IS A PH-PDZ TANDEM,
REMARK 3 AND THE LINKER IS VERY FLEXIBLE.
REMARK 4
REMARK 4 1Z87 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-APR-05.
REMARK 100 THE DEPOSITION ID IS D_1000032420.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM PHN-PDZ-PHC TANDEM OF ALPHA1
REMARK 210 -SYNTROPHIN U-15N, 13C; 100MM
REMARK 210 POTASSIUM PHOSPHATE; 90% H2O,10%
REMARK 210 D2O; 1MM PHN-PDZ-PHC TANDEM OF
REMARK 210 ALPHA1-SYNTROPHIN U-15N; 100MM
REMARK 210 POTASSIUM PHOSPHATE; 90% H2O,10%
REMARK 210 D2O; 1MM PHN-PDZ-PHC TANDEM OF
REMARK 210 ALPHA1-SYNTROPHIN U-15N, 13C;
REMARK 210 100MM POTASSIUM PHOSPHATE; 99.9%
REMARK 210 D2O; 1MM PHN-PDZ-PHC TANDEM OF
REMARK 210 ALPHA1-SYNTROPHIN; 100MM
REMARK 210 POTASSIUM PHOSPHATE; 99.9% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCO,HNCA, HN(CO)CA, HNCACB,
REMARK 210 CBCA(CO)NH; 3D_15N-SEPARATED_
REMARK 210 NOESY; 3D_13C-SEPARATED_NOESY;
REMARK 210 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
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 3 110.44 -164.17
REMARK 500 1 ARG A 5 -75.51 66.23
REMARK 500 1 SER A 21 31.93 -164.95
REMARK 500 1 GLU A 26 -178.69 -64.51
REMARK 500 1 ARG A 27 103.30 179.49
REMARK 500 1 ALA A 36 -81.43 -84.29
REMARK 500 1 GLU A 37 -72.47 -144.89
REMARK 500 1 ALA A 56 55.92 -150.56
REMARK 500 1 GLN A 57 171.44 60.17
REMARK 500 1 ASN A 59 96.71 60.58
REMARK 500 1 ALA A 61 -79.81 63.07
REMARK 500 1 PRO A 64 -168.46 -75.18
REMARK 500 1 ALA A 66 37.86 -151.72
REMARK 500 1 ALA A 67 137.47 178.16
REMARK 500 1 PRO A 68 107.80 -59.07
REMARK 500 1 PRO A 69 -173.13 -61.10
REMARK 500 1 GLU A 73 -83.67 -99.25
REMARK 500 1 ALA A 74 -87.72 50.25
REMARK 500 1 ARG A 79 -164.36 43.60
REMARK 500 1 ARG A 81 70.37 -117.91
REMARK 500 1 ALA A 87 31.58 -97.13
REMARK 500 1 ASP A 88 -56.37 -158.34
REMARK 500 1 LYS A 103 29.86 -176.16
REMARK 500 1 LYS A 113 -170.92 46.23
REMARK 500 1 VAL A 125 79.01 -64.48
REMARK 500 1 LEU A 130 -44.48 -166.80
REMARK 500 1 ASN A 133 35.75 36.27
REMARK 500 1 GLU A 135 108.71 -167.98
REMARK 500 1 SER A 139 39.81 -99.38
REMARK 500 1 THR A 141 171.93 -40.69
REMARK 500 1 THR A 152 176.65 -59.31
REMARK 500 1 LYS A 154 -48.25 80.45
REMARK 500 1 GLU A 155 102.40 -161.71
REMARK 500 1 TYR A 162 89.38 -68.69
REMARK 500 1 LYS A 164 -79.21 -151.60
REMARK 500 1 GLU A 165 45.55 -108.77
REMARK 500 1 PHE A 170 155.24 61.16
REMARK 500 1 ASN A 172 32.70 -156.89
REMARK 500 1 ALA A 174 107.75 60.11
REMARK 500 1 VAL A 179 114.06 44.99
REMARK 500 1 ASP A 182 21.91 -140.66
REMARK 500 1 GLN A 190 -43.25 -137.88
REMARK 500 1 SER A 194 170.09 63.74
REMARK 500 1 PRO A 200 73.89 -63.05
REMARK 500 1 SER A 204 -79.12 -108.93
REMARK 500 1 GLU A 205 -37.32 -132.72
REMARK 500 1 LEU A 211 31.72 -98.65
REMARK 500 1 THR A 221 -63.06 -172.97
REMARK 500 1 GLU A 226 -64.00 -169.84
REMARK 500 1 ARG A 228 165.48 67.66
REMARK 500
REMARK 500 THIS ENTRY HAS 771 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1Z86 RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE PDZ DOMAIN OF ALPHA-SYNTROPHIN
DBREF 1Z87 A 2 264 UNP Q61234 SNA1_MOUSE 2 264
SEQRES 1 A 263 ALA SER GLY ARG ARG ALA PRO ARG THR GLY LEU LEU GLU
SEQRES 2 A 263 LEU ARG CYS GLY ALA GLY SER GLY ALA GLY GLY GLU ARG
SEQRES 3 A 263 TRP GLN ARG VAL LEU LEU SER LEU ALA GLU ASP ALA LEU
SEQRES 4 A 263 THR VAL SER PRO ALA ASP GLY GLU PRO GLY PRO GLU PRO
SEQRES 5 A 263 GLU PRO ALA GLN LEU ASN GLY ALA ALA GLU PRO GLY ALA
SEQRES 6 A 263 ALA PRO PRO GLN LEU PRO GLU ALA LEU LEU LEU GLN ARG
SEQRES 7 A 263 ARG ARG VAL THR VAL ARG LYS ALA ASP ALA GLY GLY LEU
SEQRES 8 A 263 GLY ILE SER ILE LYS GLY GLY ARG GLU ASN LYS MET PRO
SEQRES 9 A 263 ILE LEU ILE SER LYS ILE PHE LYS GLY LEU ALA ALA ASP
SEQRES 10 A 263 GLN THR GLU ALA LEU PHE VAL GLY ASP ALA ILE LEU SER
SEQRES 11 A 263 VAL ASN GLY GLU ASP LEU SER SER ALA THR HIS ASP GLU
SEQRES 12 A 263 ALA VAL GLN ALA LEU LYS LYS THR GLY LYS GLU VAL VAL
SEQRES 13 A 263 LEU GLU VAL LYS TYR MET LYS GLU VAL SER PRO TYR PHE
SEQRES 14 A 263 LYS ASN SER ALA GLY GLY THR SER VAL GLY TRP ASP SER
SEQRES 15 A 263 PRO PRO ALA SER PRO LEU GLN ARG GLN PRO SER SER PRO
SEQRES 16 A 263 GLY PRO GLN PRO ARG ASN LEU SER GLU ALA LYS HIS VAL
SEQRES 17 A 263 SER LEU LYS MET ALA TYR VAL SER ARG ARG CYS THR PRO
SEQRES 18 A 263 THR ASP PRO GLU PRO ARG TYR LEU GLU ILE CYS ALA ALA
SEQRES 19 A 263 ASP GLY GLN ASP ALA VAL PHE LEU ARG ALA LYS ASP GLU
SEQRES 20 A 263 ALA SER ALA ARG SER TRP ALA GLY ALA ILE GLN ALA GLN
SEQRES 21 A 263 ILE GLY THR
HELIX 1 1 LEU A 115 THR A 120 1 6
HELIX 2 2 THR A 141 THR A 152 1 12
HELIX 3 3 ASP A 247 GLY A 263 1 17
SHEET 1 A 7 LYS A 207 SER A 210 0
SHEET 2 A 7 ALA A 39 SER A 43 -1 N LEU A 40 O VAL A 209
SHEET 3 A 7 TRP A 28 LEU A 35 -1 N SER A 34 O THR A 41
SHEET 4 A 7 ARG A 9 ARG A 16 -1 N LEU A 15 O GLN A 29
SHEET 5 A 7 ASP A 239 ARG A 244 -1 O ARG A 244 N GLU A 14
SHEET 6 A 7 TYR A 229 ALA A 234 -1 N LEU A 230 O LEU A 243
SHEET 7 A 7 ALA A 214 ARG A 219 -1 N ARG A 219 O TYR A 229
SHEET 1 B 3 ARG A 80 VAL A 82 0
SHEET 2 B 3 LEU A 158 LYS A 161 -1 O VAL A 160 N ARG A 80
SHEET 3 B 3 ALA A 128 VAL A 132 -1 N SER A 131 O GLU A 159
SHEET 1 C 2 SER A 95 GLY A 99 0
SHEET 2 C 2 MET A 104 LYS A 110 -1 O MET A 104 N GLY A 99
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
