Click here to see the 3D structure Header list of 2bvb.pdb file

Complete list - 23 20 Bytes
HEADER ADHESION 23-JUN-05 2BVB TITLE THE C-TERMINAL DOMAIN FROM MICRONEMAL PROTEIN 1 (MIC1) FROM TOXOPLASMA TITLE 2 GONDII COMPND MOL_ID: 1; COMPND 2 MOLECULE: MICRONEMAL PROTEIN 1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C-TERMINAL DOMAIN RESIDUES 320-456; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: TOXOPLASMA GONDII; SOURCE 3 ORGANISM_TAXID: 5811; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS MIC1, MICRONEME, INVASION, ADHESION EXPDTA SOLUTION NMR MDLTYP MINIMIZED AVERAGE AUTHOR S.SAOUROS,B.EDWARDS-JONES,M.REISS,K.SAWMYNADEN,E.COTA,P.SIMPSON, AUTHOR 2 T.J.DOWSE,U.JAKLE,S.RAMBOARINA,T.SHIVARATTAN,S.MATTHEWS,D.SOLDATI- AUTHOR 3 FAVRE REVDAT 4 23-JUN-21 2BVB 1 REMARK REVDAT 3 24-FEB-09 2BVB 1 VERSN REVDAT 2 17-NOV-05 2BVB 1 SOURCE JRNL REVDAT 1 12-OCT-05 2BVB 0 JRNL AUTH S.SAOUROS,B.EDWARDS-JONES,M.REISS,K.SAWMYNADEN,E.COTA, JRNL AUTH 2 P.SIMPSON,T.J.DOWSE,U.JAKLE,S.RAMBOARINA,T.SHIVARATTAN, JRNL AUTH 3 S.MATTHEWS,D.SOLDATI-FAVRE JRNL TITL A NOVEL GALECTIN-LIKE DOMAIN FROM TOXOPLASMA GONDLL JRNL TITL 2 MICRONEMAL PROTEIN 1 ASSISTS THE FOLDING, ASSEMBLY,AND JRNL TITL 3 TRANSPORT OF A CELL-ADHESION COMPLEX. JRNL REF J.BIOL.CHEM. V. 280 38583 2005 JRNL REFN ISSN 0021-9258 JRNL PMID 16166092 JRNL DOI 10.1074/JBC.C500365200 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE- REMARK 3 KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ, RICE, REMARK 3 SIMONSON,WARREN REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2BVB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-JUN-05. REMARK 100 THE DEPOSITION ID IS D_1290024620. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 310.0 REMARK 210 PH : NULL REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ REMARK 210 SPECTROMETER MODEL : OTHER REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NMRVIEW REMARK 210 METHOD USED : ARIA REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 10 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 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: NONE 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 ASP A 7 -32.14 -168.04 REMARK 500 GLU A 15 139.71 -38.69 REMARK 500 ILE A 24 79.32 -117.01 REMARK 500 VAL A 32 97.98 -61.97 REMARK 500 THR A 51 -74.04 -98.43 REMARK 500 ASN A 54 138.79 66.50 REMARK 500 SER A 55 -79.70 66.38 REMARK 500 GLU A 63 172.53 -56.52 REMARK 500 HIS A 77 -169.35 -178.14 REMARK 500 SER A 104 -81.44 -113.02 REMARK 500 CYS A 106 -158.97 -90.04 REMARK 500 SER A 107 -70.66 -172.12 REMARK 500 GLU A 110 105.38 -160.99 REMARK 500 LEU A 128 -79.30 59.75 REMARK 500 THR A 133 87.60 -63.71 REMARK 500 ALA A 134 -4.70 63.20 REMARK 500 VAL A 135 37.89 30.40 REMARK 500 SER A 136 -18.35 -168.33 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 6376 RELATED DB: BMRB DBREF 2BVB A 1 137 UNP O00834 O00834_TOXGO 320 456 SEQRES 1 A 137 LYS THR GLU ILE HIS GLY ASP SER THR LYS ALA THR LEU SEQRES 2 A 137 GLU GLU GLY GLN GLN LEU THR LEU THR PHE ILE SER THR SEQRES 3 A 137 LYS LEU ASP VAL ALA VAL GLY SER CYS HIS SER LEU VAL SEQRES 4 A 137 ALA ASN PHE LEU ASP GLY PHE LEU LYS PHE GLN THR GLY SEQRES 5 A 137 SER ASN SER ALA PHE ASP VAL VAL GLU VAL GLU GLU PRO SEQRES 6 A 137 ALA GLY PRO ALA VAL LEU THR ILE GLY LEU GLY HIS LYS SEQRES 7 A 137 GLY ARG LEU ALA VAL VAL LEU ASP TYR THR ARG LEU ASN SEQRES 8 A 137 ALA ALA LEU GLY SER ALA ALA TYR VAL VAL GLU ASP SER SEQRES 9 A 137 GLY CYS SER SER SER GLU GLU VAL SER PHE GLN GLY VAL SEQRES 10 A 137 GLY SER GLY ALA THR LEU VAL VAL THR THR LEU GLY GLU SEQRES 11 A 137 SER PRO THR ALA VAL SER ALA SHEET 1 AA 6 SER A 8 LEU A 13 0 SHEET 2 AA 6 GLU A 110 GLN A 115 -1 O GLU A 110 N LEU A 13 SHEET 3 AA 6 LYS A 27 ALA A 31 -1 O ASP A 29 N GLN A 115 SHEET 4 AA 6 SER A 37 ASN A 41 -1 O LEU A 38 N VAL A 30 SHEET 5 AA 6 PHE A 46 GLN A 50 -1 O PHE A 46 N ASN A 41 SHEET 6 AA 6 ASP A 58 VAL A 60 -1 O ASP A 58 N PHE A 49 SHEET 1 AB 5 LEU A 94 VAL A 101 0 SHEET 2 AB 5 LEU A 81 ARG A 89 -1 O LEU A 81 N VAL A 101 SHEET 3 AB 5 PRO A 65 LEU A 75 -1 N ALA A 66 O THR A 88 SHEET 4 AB 5 GLN A 18 ILE A 24 -1 O LEU A 19 N ILE A 73 SHEET 5 AB 5 THR A 122 THR A 126 -1 O THR A 122 N THR A 22 SSBOND 1 CYS A 35 CYS A 106 1555 1555 2.03 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
Complete list - 23 20 Bytes