Header list of 1wgu.pdb file
Complete list - r 2 2 Bytes
HEADER PROTEIN BINDING 28-MAY-04 1WGU TITLE SOLUTION STRUCTURE OF THE C-TERMINAL PHOSPHOTYROSINE INTERACTION TITLE 2 DOMAIN OF APBB2 FROM MOUSE COMPND MOL_ID: 1; COMPND 2 MOLECULE: AMYLOID BETA (A4) PRECURSOR PROTEIN-BINDING, FAMILY B, COMPND 3 MEMBER 2; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: PHOSPHOTYROSINE-INTERACTION DOMAIN; COMPND 6 SYNONYM: APBB2; 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 GENE: RIKEN CDNA 1200015I07; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P031020-58; SOURCE 8 OTHER_DETAILS: CELL-FREE PROTEIN SYNTHESIS KEYWDS PHOSPHOTYROSINE-INTERACTION DOMAIN, AMYLOID DISEASE, STRUCTURAL KEYWDS 2 GENOMICS, RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, KEYWDS 3 PROTEIN BINDING EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR H.LI,F.HAYASHI,S.KOSHIBA,M.INOUE,T.KIGAWA,S.YOKOYAMA,RIKEN STRUCTURAL AUTHOR 2 GENOMICS/PROTEOMICS INITIATIVE (RSGI) REVDAT 4 02-MAR-22 1WGU 1 REMARK SEQADV REVDAT 3 04-NOV-08 1WGU 1 JRNL REVDAT 2 02-SEP-08 1WGU 1 VERSN REVDAT 1 28-NOV-04 1WGU 0 JRNL AUTH H.LI,S.KOSHIBA,F.HAYASHI,N.TOCHIO,T.TOMIZAWA,T.KASAI, JRNL AUTH 2 T.YABUKI,Y.MOTODA,T.HARADA,S.WATANABE,M.INOUE,Y.HAYASHIZAKI, JRNL AUTH 3 A.TANAKA,T.KIGAWA,S.YOKOYAMA JRNL TITL STRUCTURE OF THE C-TERMINAL PHOSPHOTYROSINE INTERACTION JRNL TITL 2 DOMAIN OF FE65L1 COMPLEXED WITH THE CYTOPLASMIC TAIL OF JRNL TITL 3 AMYLOID PRECURSOR PROTEIN REVEALS A NOVEL PEPTIDE BINDING JRNL TITL 4 MODE JRNL REF J.BIOL.CHEM. V. 283 27165 2008 JRNL REFN ISSN 0021-9258 JRNL PMID 18650440 JRNL DOI 10.1074/JBC.M803892200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : VNMR 6.1C, CYANA 1.0.7 REMARK 3 AUTHORS : VARIAN (VNMR), GUENTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1WGU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 03-JUN-04. REMARK 100 THE DEPOSITION ID IS D_1000023564. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 7.0 REMARK 210 IONIC STRENGTH : 120MM REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 0.84MM PHOSPHOTYROSINE REMARK 210 -INTERACTION DOMAIN U-13C, 15N; REMARK 210 20MM D-TRIS-HCL (PH7.0); 100MM REMARK 210 NACL; 2MM D-DTT; 0.02% NAN3; 10% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 900 MHZ REMARK 210 SPECTROMETER MODEL : INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRPIPE 20020425, NMRVIEW 5.0.4, REMARK 210 KUJIRA 0.897, CYANA 1.0.7 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, TARGET REMARK 210 FUNCTION 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 ASN A 121 H ALA A 125 1.50 REMARK 500 O ILE A 41 H MET A 45 1.52 REMARK 500 H ASN A 57 O ILE A 68 1.53 REMARK 500 O GLU A 124 H ALA A 128 1.53 REMARK 500 H VAL A 65 O CYS A 80 1.57 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 LYS A 11 126.22 -176.23 REMARK 500 1 SER A 48 129.26 62.06 REMARK 500 1 LYS A 71 47.05 -95.89 REMARK 500 1 ASN A 72 111.39 172.43 REMARK 500 1 MET A 88 -158.40 -172.24 REMARK 500 1 HIS A 95 36.93 -99.34 REMARK 500 1 GLN A 106 49.56 37.34 REMARK 500 1 SER A 131 90.38 39.76 REMARK 500 2 SER A 6 -41.41 -177.17 REMARK 500 2 ARG A 19 99.84 -65.16 REMARK 500 2 GLU A 42 -37.69 -38.85 REMARK 500 2 SER A 47 -61.88 -154.61 REMARK 500 2 GLU A 74 -44.04 -158.00 REMARK 500 2 MET A 88 -158.75 -169.56 REMARK 500 2 LYS A 92 -72.68 -40.78 REMARK 500 2 GLN A 106 56.87 38.19 REMARK 500 3 THR A 9 88.66 38.76 REMARK 500 3 GLU A 13 143.53 62.77 REMARK 500 3 THR A 46 60.03 -69.39 REMARK 500 3 SER A 47 -65.36 -169.10 REMARK 500 3 LYS A 71 -90.18 -85.73 REMARK 500 3 ASN A 72 156.90 -47.24 REMARK 500 3 MET A 88 -158.99 -170.65 REMARK 500 3 LYS A 92 -73.74 -40.10 REMARK 500 3 ASN A 105 -160.90 80.48 REMARK 500 3 ALA A 119 33.17 -91.78 REMARK 500 3 SER A 135 79.42 -155.19 REMARK 500 4 SER A 2 166.79 56.62 REMARK 500 4 THR A 12 140.06 -170.25 REMARK 500 4 LEU A 14 154.86 59.85 REMARK 500 4 ARG A 19 99.34 -65.48 REMARK 500 4 SER A 48 128.77 62.12 REMARK 500 4 SER A 49 -179.18 -61.59 REMARK 500 4 LYS A 71 45.92 -89.16 REMARK 500 4 GLU A 73 -51.60 -126.08 REMARK 500 4 MET A 88 -149.03 -164.01 REMARK 500 4 ASN A 105 -164.97 75.97 REMARK 500 4 ALA A 119 37.59 -91.55 REMARK 500 4 SER A 131 84.93 39.87 REMARK 500 5 SER A 2 166.83 57.37 REMARK 500 5 SER A 3 -58.08 -141.06 REMARK 500 5 SER A 5 100.27 66.42 REMARK 500 5 LEU A 14 128.46 62.34 REMARK 500 5 ARG A 19 99.47 -65.43 REMARK 500 5 GLU A 42 -39.68 -38.45 REMARK 500 5 SER A 48 127.78 61.66 REMARK 500 5 SER A 49 -178.94 -59.05 REMARK 500 5 MET A 88 -161.08 -170.23 REMARK 500 5 ASN A 105 -170.59 73.19 REMARK 500 5 GLN A 106 46.52 -84.66 REMARK 500 REMARK 500 THIS ENTRY HAS 232 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 650 REMARK 650 HELIX REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED REMARK 700 REMARK 700 SHEET REMARK 700 DETERMINATION METHOD: AUTHOR DETERMINED REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: MMT007006815.1 RELATED DB: TARGETDB DBREF 1WGU A 8 130 UNP Q9DBR4 APBB2_MOUSE 582 704 SEQADV 1WGU GLY A 1 UNP Q9DBR4 EXPRESSION TAG SEQADV 1WGU SER A 2 UNP Q9DBR4 EXPRESSION TAG SEQADV 1WGU SER A 3 UNP Q9DBR4 EXPRESSION TAG SEQADV 1WGU GLY A 4 UNP Q9DBR4 EXPRESSION TAG SEQADV 1WGU SER A 5 UNP Q9DBR4 EXPRESSION TAG SEQADV 1WGU SER A 6 UNP Q9DBR4 EXPRESSION TAG SEQADV 1WGU GLY A 7 UNP Q9DBR4 EXPRESSION TAG SEQADV 1WGU SER A 131 UNP Q9DBR4 EXPRESSION TAG SEQADV 1WGU GLY A 132 UNP Q9DBR4 EXPRESSION TAG SEQADV 1WGU PRO A 133 UNP Q9DBR4 EXPRESSION TAG SEQADV 1WGU SER A 134 UNP Q9DBR4 EXPRESSION TAG SEQADV 1WGU SER A 135 UNP Q9DBR4 EXPRESSION TAG SEQADV 1WGU GLY A 136 UNP Q9DBR4 EXPRESSION TAG SEQRES 1 A 136 GLY SER SER GLY SER SER GLY PRO THR PRO LYS THR GLU SEQRES 2 A 136 LEU VAL GLN LYS PHE ARG VAL GLN TYR LEU GLY MET LEU SEQRES 3 A 136 PRO VAL ASP ARG PRO VAL GLY MET ASP THR LEU ASN SER SEQRES 4 A 136 ALA ILE GLU ASN LEU MET THR SER SER SER LYS GLU ASP SEQRES 5 A 136 TRP PRO SER VAL ASN MET ASN VAL ALA ASP ALA THR VAL SEQRES 6 A 136 THR VAL ILE SER GLU LYS ASN GLU GLU GLU VAL LEU VAL SEQRES 7 A 136 GLU CYS ARG VAL ARG PHE LEU SER PHE MET GLY VAL GLY SEQRES 8 A 136 LYS ASP VAL HIS THR PHE ALA PHE ILE MET ASP THR GLY SEQRES 9 A 136 ASN GLN ARG PHE GLU CYS HIS VAL PHE TRP CYS GLU PRO SEQRES 10 A 136 ASN ALA ALA ASN VAL SER GLU ALA VAL GLN ALA ALA CYS SEQRES 11 A 136 SER GLY PRO SER SER GLY HELIX 1 1 MET A 34 MET A 45 1 12 HELIX 2 2 ALA A 120 CYS A 130 1 11 SHEET 1 A 7 VAL A 76 ARG A 81 0 SHEET 2 A 7 THR A 64 ILE A 68 -1 N VAL A 65 O CYS A 80 SHEET 3 A 7 SER A 55 ALA A 61 -1 N ASN A 57 O ILE A 68 SHEET 4 A 7 PHE A 18 PRO A 27 -1 N VAL A 20 O VAL A 56 SHEET 5 A 7 PHE A 108 TRP A 114 -1 O CYS A 110 N LEU A 26 SHEET 6 A 7 PHE A 97 ASP A 102 -1 N PHE A 97 O PHE A 113 SHEET 7 A 7 LEU A 85 GLY A 89 -1 N PHE A 87 O ILE A 100 CISPEP 1 GLU A 116 PRO A 117 1 0.00 CISPEP 2 GLU A 116 PRO A 117 2 0.04 CISPEP 3 GLU A 116 PRO A 117 3 -0.03 CISPEP 4 GLU A 116 PRO A 117 4 -0.02 CISPEP 5 GLU A 116 PRO A 117 5 0.00 CISPEP 6 GLU A 116 PRO A 117 6 0.00 CISPEP 7 GLU A 116 PRO A 117 7 -0.12 CISPEP 8 GLU A 116 PRO A 117 8 -0.04 CISPEP 9 GLU A 116 PRO A 117 9 -0.03 CISPEP 10 GLU A 116 PRO A 117 10 0.03 CISPEP 11 GLU A 116 PRO A 117 11 -0.01 CISPEP 12 GLU A 116 PRO A 117 12 -0.04 CISPEP 13 GLU A 116 PRO A 117 13 0.04 CISPEP 14 GLU A 116 PRO A 117 14 -0.05 CISPEP 15 GLU A 116 PRO A 117 15 0.04 CISPEP 16 GLU A 116 PRO A 117 16 -0.02 CISPEP 17 GLU A 116 PRO A 117 17 0.01 CISPEP 18 GLU A 116 PRO A 117 18 0.01 CISPEP 19 GLU A 116 PRO A 117 19 0.05 CISPEP 20 GLU A 116 PRO A 117 20 0.06 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