Header list of 1z86.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING 30-MAR-05 1Z86 TITLE SOLUTION STRUCTURE OF THE PDZ DOMAIN OF ALPHA-SYNTROPHIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: ALPHA-1-SYNTROPHIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: PDZ DOMAIN; 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 TWO ALPHA HELIX, SIX BETA STRANDS, PROTEIN BINDING EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.YAN,W.XU,W.WEN,J.F.LONG,M.E.ADAMS,S.C.FROEHNER,M.ZHANG REVDAT 3 02-MAR-22 1Z86 1 REMARK REVDAT 2 24-FEB-09 1Z86 1 VERSN REVDAT 1 24-JAN-06 1Z86 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: NULL REMARK 4 REMARK 4 1Z86 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_1000032419. 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 PDZ DOMAIN OF ALPHA1 REMARK 210 -SYNTROPHIN U-15N, 13C; 100MM REMARK 210 POTASSIUM PHOSPHATE; 90% H2O,10% REMARK 210 D2O; 1MM PDZ DOMAIN OF ALPHA1- REMARK 210 SYNTROPHIN U-15N; 100MM REMARK 210 POTASSIUM PHOSPHATE; 90% H2O,10% REMARK 210 D2O; 1MM PDZ DOMAIN OF ALPHA1- REMARK 210 SYNTROPHIN U-15N, 13C; 100MM REMARK 210 POTASSIUM PHOSPHATE; 99.9% D2O; REMARK 210 1MM PDZ DOMAIN OF ALPHA1- REMARK 210 SYNTROPHIN; 100MM POTASSIUM REMARK 210 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 : 20 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: 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 O SER A 95 H SER A 109 1.58 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 ALA A 87 -76.88 -137.75 REMARK 500 1 ALA A 89 -64.33 -175.72 REMARK 500 1 LYS A 110 89.74 -172.43 REMARK 500 1 ALA A 122 61.76 -154.95 REMARK 500 1 LEU A 123 97.64 -173.21 REMARK 500 1 SER A 139 59.59 -140.98 REMARK 500 1 THR A 141 160.53 -37.63 REMARK 500 1 LYS A 151 58.16 -102.64 REMARK 500 1 LYS A 154 -138.84 60.29 REMARK 500 2 LEU A 92 -178.04 61.02 REMARK 500 2 LYS A 103 30.46 70.03 REMARK 500 2 LYS A 110 89.86 -171.17 REMARK 500 2 ILE A 129 88.61 -69.98 REMARK 500 2 THR A 141 163.15 -39.73 REMARK 500 2 GLU A 155 144.75 -170.34 REMARK 500 2 LYS A 164 -78.37 65.35 REMARK 500 3 LEU A 92 -75.77 -79.75 REMARK 500 3 LYS A 110 88.28 -165.87 REMARK 500 3 GLU A 121 29.64 46.84 REMARK 500 3 LEU A 123 105.42 -172.17 REMARK 500 3 THR A 141 161.91 -39.44 REMARK 500 3 LYS A 164 -168.59 45.81 REMARK 500 4 ASP A 88 73.56 -161.99 REMARK 500 4 ALA A 89 94.30 59.86 REMARK 500 4 LEU A 92 -172.74 60.84 REMARK 500 4 SER A 109 -12.26 -140.37 REMARK 500 4 LYS A 110 94.07 -176.05 REMARK 500 4 LEU A 123 70.38 -174.36 REMARK 500 4 THR A 141 161.19 -38.58 REMARK 500 4 LYS A 151 79.99 -119.33 REMARK 500 4 LYS A 154 -135.89 60.98 REMARK 500 4 LYS A 164 -81.31 61.34 REMARK 500 5 ALA A 87 -75.67 -86.25 REMARK 500 5 ASP A 88 -56.15 -176.77 REMARK 500 5 LYS A 110 91.34 -173.47 REMARK 500 5 ALA A 122 59.52 -148.43 REMARK 500 5 LEU A 123 98.43 -178.08 REMARK 500 5 THR A 141 163.02 -39.87 REMARK 500 5 LYS A 154 -7.33 77.74 REMARK 500 5 GLU A 155 111.23 -170.45 REMARK 500 5 TYR A 162 85.05 -69.87 REMARK 500 5 LYS A 164 75.39 40.52 REMARK 500 6 LYS A 110 94.02 -175.79 REMARK 500 6 LEU A 123 91.44 -176.58 REMARK 500 6 SER A 139 59.32 -140.31 REMARK 500 6 THR A 141 161.36 -38.66 REMARK 500 6 GLU A 155 117.44 -170.08 REMARK 500 6 LYS A 164 163.20 61.33 REMARK 500 7 LYS A 86 -164.21 -58.18 REMARK 500 7 LYS A 110 90.89 -173.84 REMARK 500 REMARK 500 THIS ENTRY HAS 158 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1Z87 RELATED DB: PDB REMARK 900 SOLUTION STRUCTURE OF THE SPLIT PH-PDZ SUPRAMODULE OF ALPHA- REMARK 900 SYNTROPHIN DBREF 1Z86 A 79 165 UNP Q61234 SNTA1_MOUSE 79 165 SEQRES 1 A 87 ARG ARG ARG VAL THR VAL ARG LYS ALA ASP ALA GLY GLY SEQRES 2 A 87 LEU GLY ILE SER ILE LYS GLY GLY ARG GLU ASN LYS MET SEQRES 3 A 87 PRO ILE LEU ILE SER LYS ILE PHE LYS GLY LEU ALA ALA SEQRES 4 A 87 ASP GLN THR GLU ALA LEU PHE VAL GLY ASP ALA ILE LEU SEQRES 5 A 87 SER VAL ASN GLY GLU ASP LEU SER SER ALA THR HIS ASP SEQRES 6 A 87 GLU ALA VAL GLN ALA LEU LYS LYS THR GLY LYS GLU VAL SEQRES 7 A 87 VAL LEU GLU VAL LYS TYR MET LYS GLU HELIX 1 1 ARG A 100 LYS A 103 5 4 HELIX 2 2 LEU A 115 GLU A 121 1 7 HELIX 3 3 SER A 138 ALA A 140 5 3 HELIX 4 4 THR A 141 LYS A 151 1 11 SHEET 1 A 5 ARG A 80 VAL A 84 0 SHEET 2 A 5 VAL A 156 TYR A 162 -1 O LEU A 158 N VAL A 82 SHEET 3 A 5 ASP A 127 VAL A 132 -1 N ALA A 128 O LYS A 161 SHEET 4 A 5 MET A 104 ILE A 111 -1 N ILE A 108 O ASP A 127 SHEET 5 A 5 ILE A 94 GLY A 99 -1 N SER A 95 O SER A 109 SHEET 1 B 4 ARG A 80 VAL A 84 0 SHEET 2 B 4 VAL A 156 TYR A 162 -1 O LEU A 158 N VAL A 82 SHEET 3 B 4 ASP A 127 VAL A 132 -1 N ALA A 128 O LYS A 161 SHEET 4 B 4 GLU A 135 ASP A 136 -1 O GLU A 135 N VAL A 132 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
Complete list - r 2 2 Bytes