Header list of 2tmp.pdb file
Complete list - r 16 2 Bytes
HEADER METALLOPROTEASE INHIBITOR 26-MAY-98 2TMP TITLE N-TERMINAL DOMAIN OF TISSUE INHIBITOR OF METALLOPROTEINASE-2 (N-TIMP- TITLE 2 2), NMR, 49 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: TISSUE INHIBITOR OF METALLOPROTEINASES-2; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: N-TERMINAL DOMAIN, RESIDUES 1-127; COMPND 5 SYNONYM: METALLOPROTEINASE INHIBITOR, TIMP-2; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 8 EXPRESSION_SYSTEM_VARIANT: DE3; SOURCE 9 EXPRESSION_SYSTEM_CELLULAR_LOCATION: INTRACELLULAR INCLUSION BODIES; SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET23D; SOURCE 12 OTHER_DETAILS: PROTEIN REFOLDED FROM INCLUSION BODIES KEYWDS TIMP, METALLOPROTEINASE INHIBITOR, OB PROTEIN FOLD, METALLOPROTEASE KEYWDS 2 INHIBITOR EXPDTA SOLUTION NMR NUMMDL 49 AUTHOR F.W.MUSKETT,T.A.FRENKIEL,J.FEENEY,R.B.FREEDMAN,M.D.CARR, AUTHOR 2 R.A.WILLIAMSON REVDAT 4 16-MAR-22 2TMP 1 REMARK SEQADV REVDAT 3 24-FEB-09 2TMP 1 VERSN REVDAT 2 13-JAN-99 2TMP 1 COMPND REMARK TITLE HEADER REVDAT 2 2 1 JRNL REVDAT 1 09-DEC-98 2TMP 0 JRNL AUTH F.W.MUSKETT,T.A.FRENKIEL,J.FEENEY,R.B.FREEDMAN,M.D.CARR, JRNL AUTH 2 R.A.WILLIAMSON JRNL TITL HIGH RESOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF TISSUE JRNL TITL 2 INHIBITOR OF METALLOPROTEINASES-2 AND CHARACTERIZATION OF JRNL TITL 3 ITS INTERACTION SITE WITH MATRIX METALLOPROTEINASE-3. JRNL REF J.BIOL.CHEM. V. 273 21736 1998 JRNL REFN ISSN 0021-9258 JRNL PMID 9705310 JRNL DOI 10.1074/JBC.273.34.21736 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH R.A.WILLIAMSON,M.D.CARR,T.A.FRENKIEL,J.FEENEY,R.B.FREEDMAN REMARK 1 TITL MAPPING THE BINDING SITE FOR MATRIX METALLOPROTEINASE ON THE REMARK 1 TITL 2 N-TERMINAL DOMAIN OF THE TISSUE INHIBITOR OF REMARK 1 TITL 3 METALLOPROTEINASES-2 BY NMR CHEMICAL SHIFT PERTURBATION REMARK 1 REF BIOCHEMISTRY V. 36 13882 1997 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 2 REMARK 1 AUTH R.A.WILLIAMSON,D.NATALIA,C.K.GEE,G.MURPHY,M.D.CARR, REMARK 1 AUTH 2 R.B.FREEDMAN REMARK 1 TITL CHEMICALLY AND CONFORMATIONALLY AUTHENTIC ACTIVE DOMAIN OF REMARK 1 TITL 2 HUMAN TISSUE INHIBITOR OF METALLOPROTEINASES-2 REFOLDED FROM REMARK 1 TITL 3 BACTERIAL INCLUSION BODIES REMARK 1 REF EUR.J.BIOCHEM. V. 241 476 1996 REMARK 1 REFN ISSN 0014-2956 REMARK 1 REFERENCE 3 REMARK 1 AUTH R.A.WILLIAMSON,G.MARTORELL,M.D.CARR,G.MURPHY,A.J.DOCHERTY, REMARK 1 AUTH 2 R.B.FREEDMAN,J.FEENEY REMARK 1 TITL SOLUTION STRUCTURE OF THE ACTIVE DOMAIN OF TISSUE INHIBITOR REMARK 1 TITL 2 OF METALLOPROTEINASES-2. A NEW MEMBER OF THE OB FOLD PROTEIN REMARK 1 TITL 3 FAMILY REMARK 1 REF BIOCHEMISTRY V. 33 11745 1994 REMARK 1 REFN ISSN 0006-2960 REMARK 1 REFERENCE 4 REMARK 1 AUTH R.A.WILLIAMSON,F.A.MARSTON,S.ANGAL,P.KOKLITIS,M.PANICO, REMARK 1 AUTH 2 H.R.MORRIS,A.F.CARNE,B.J.SMITH,T.J.HARRIS,R.B.FREEDMAN REMARK 1 TITL DISULPHIDE BOND ASSIGNMENT IN HUMAN TISSUE INHIBITOR OF REMARK 1 TITL 2 METALLOPROTEINASES (TIMP) REMARK 1 REF BIOCHEM.J. V. 268 267 1990 REMARK 1 REFN ISSN 0264-6021 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA REMARK 3 AUTHORS : GUNTERT,WUTHRICH REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: SEE GUNTERT ET AL. (1997) J. MOL. BIOL. REMARK 3 273(1), 283-298 REMARK 4 REMARK 4 2TMP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000178686. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 6.7 REMARK 210 IONIC STRENGTH : 125 MM REMARK 210 PRESSURE : 1 ATMOSPHERE REMARK 210 SAMPLE CONTENTS : AQUEOUS REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D-NOESY; 2D-TOCSY; 2D-COSY; 3D REMARK 210 -NOESY-TOCSY; 2D-HSQC; 3D-15N- REMARK 210 NOESY-HSQC; 3D-15N-HNHA; 3D-15N- REMARK 210 HNHB; 3D HCCH-TOCSY; 3D CBCA(CO) REMARK 210 NH; 3D-CBCAHN; 3D-13C-HMQC-NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : UNITYPLUS & INOVA REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA REMARK 210 METHOD USED : SIMULATED ANNEALING USING REMARK 210 TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 49 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 3 REMARK 210 REMARK 210 REMARK: THE STRUCTURE CLOSEST TO THE MEAN OF THE 49 CONFORMERS 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 DBREF 2TMP A 1 127 UNP P16035 TIMP2_HUMAN 27 153 SEQADV 2TMP THR A 21 UNP P16035 ALA 47 CONFLICT SEQRES 1 A 127 CYS SER CYS SER PRO VAL HIS PRO GLN GLN ALA PHE CYS SEQRES 2 A 127 ASN ALA ASP VAL VAL ILE ARG THR LYS ALA VAL SER GLU SEQRES 3 A 127 LYS GLU VAL ASP SER GLY ASN ASP ILE TYR GLY ASN PRO SEQRES 4 A 127 ILE LYS ARG ILE GLN TYR GLU ILE LYS GLN ILE LYS MET SEQRES 5 A 127 PHE LYS GLY PRO GLU LYS ASP ILE GLU PHE ILE TYR THR SEQRES 6 A 127 ALA PRO SER SER ALA VAL CYS GLY VAL SER LEU ASP VAL SEQRES 7 A 127 GLY GLY LYS LYS GLU TYR LEU ILE ALA GLY LYS ALA GLU SEQRES 8 A 127 GLY ASP GLY LYS MET HIS ILE THR LEU CYS ASP PHE ILE SEQRES 9 A 127 VAL PRO TRP ASP THR LEU SER THR THR GLN LYS LYS SER SEQRES 10 A 127 LEU ASN HIS ARG TYR GLN MET GLY CYS GLU SHEET 1 A 2 GLN A 44 GLU A 46 0 SHEET 2 A 2 PHE A 62 TYR A 64 -1 N ILE A 63 O TYR A 45 SSBOND 1 CYS A 1 CYS A 72 1555 1555 1.96 SSBOND 2 CYS A 3 CYS A 101 1555 1555 2.07 SSBOND 3 CYS A 13 CYS A 126 1555 1555 1.94 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 16 2 Bytes