PDB:1ITP HEADER PROTEIN BINDING 23-JAN-02 1ITP TITLE SOLUTION STRUCTURE OF POIA1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEINASE A INHIBITOR 1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: IA-1=SERINE PROTEINASE INHIBITOR; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PLEUROTUS OSTREATUS; SOURCE 3 ORGANISM_COMMON: OYSTER MUSHROOM; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET11D KEYWDS INHIBITOR, PROPEPTIDE, BETA-ALPHA-BETA EXPDTA NMR, 20 STRUCTURES AUTHOR H.SASAKAWA,S.YOSHINAGA,S.KOJIMA,A.TAMURA REVDAT 3 07-JAN-03 1ITP 1 REMARK REVDAT 2 10-APR-02 1ITP 1 JRNL REVDAT 1 13-FEB-02 1ITP 0 JRNL AUTH H.SASAKAWA,S.YOSHINAGA,S.KOJIMA,A.TAMURA JRNL TITL STRUCTURE OF POIA1, A HOMOLOGOUS PROTEIN TO THE JRNL TITL 2 PROPEPTIDE OF SUBTILISIN: IMPLICATION FOR PROTEIN JRNL TITL 3 FOLDABILITY AND THE FUNCTION AS AN INTRAMOLECULAR JRNL TITL 4 CHAPERONE JRNL REF J.MOL.BIOL. V. 317 159 2002 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.5 REMARK 3 AUTHORS : GNTERT REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1ITP COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JAN-2002. REMARK 100 THE RCSB ID CODE IS RCSB005264. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303; 303; 303 REMARK 210 PH : 7.0; 7.0; 7.0 REMARK 210 IONIC STRENGTH : 25MM PI; 25MM PI; 25MM PI REMARK 210 PRESSURE : 1; 1; 1 REMARK 210 SAMPLE CONTENTS : 1MM POIA1, 25MM PHOSPHATE REMARK 210 BUFFER, 95% H2O, 5% D2O; 1MM REMARK 210 POIA1 U-15N, 25MM PHOSPHATE REMARK 210 BUFFER, 95% H2O, 5% D2O; 1MM REMARK 210 POIA1 U-15N, 13C, 25MM REMARK 210 PHOSPHATE BUFFER, 95% H2O, 5% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY, 3D_15N-SEPARATED_ REMARK 210 NOESY, 3HJNC'-HNCO REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA 1.5, XWINNMR 1.3, REMARK 210 NMRPIPE 1.7 REMARK 210 METHOD USED : DISTANCE GEOMETRY REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 20 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY. 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 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 M RES CSSEQI PSI PHI REMARK 500 1 THR A 75 150.89 62.44 REMARK 500 2 SER A 2 135.78 72.44 REMARK 500 3 SER A 2 164.14 72.18 REMARK 500 4 THR A 75 143.98 63.40 REMARK 500 5 THR A 75 151.64 59.85 REMARK 500 5 THR A 76 -75.18 68.32 REMARK 500 9 THR A 75 150.43 67.15 REMARK 500 15 SER A 2 134.42 61.93 DBREF 1ITP A 2 77 GB 797424 AAB33247 1 76 SEQADV 1ITP GLY A 1 GB 797424 CLONING ARTIFACT SEQRES 1 A 77 GLY SER ALA GLY LYS PHE ILE VAL ILE PHE LYS ASN ASP SEQRES 2 A 77 VAL SER GLU ASP LYS ILE ARG GLU THR LYS ASP GLU VAL SEQRES 3 A 77 ILE ALA GLU GLY GLY THR ILE THR ASN GLU TYR ASN MET SEQRES 4 A 77 PRO GLY MET LYS GLY PHE ALA GLY GLU LEU THR PRO GLN SEQRES 5 A 77 SER LEU THR LYS PHE GLN GLY LEU GLN GLY ASP LEU ILE SEQRES 6 A 77 ASP SER ILE GLU GLU ASP GLY ILE VAL THR THR GLN HELIX 1 1 SER A 15 GLY A 30 1 16 HELIX 2 2 THR A 50 LEU A 60 1 11 SHEET 1 A 4 ASN A 35 MET A 39 0 SHEET 2 A 4 MET A 42 LEU A 49 -1 O ALA A 46 N ASN A 35 SHEET 3 A 4 GLY A 4 PHE A 10 -1 N PHE A 10 O LYS A 43 SHEET 4 A 4 ILE A 65 GLU A 70 -1 O GLU A 69 N ILE A 7 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 1 ATOM 1 N GLY A 1 1.707 -15.450 5.562 1.00 0.00 N 200201231NMR20JRNL AUTH H.SASAKAWA,S.YOSHINAGA,S.KOJIMA,A.TAMURA JRNL TITL STRUCTURE OF POIA1, A HOMOLOGOUS PROTEIN TO THE JRNL TITL 2 PROPEPTIDE OF SUBTILISIN: IMPLICATION FOR PROTEIN JRNL TITL 3 FOLDABILITY AND THE FUNCTION AS AN INTRAMOLECULAR JRNL TITL 4 CHAPERONE JRNL REF J.MOL.BIOL. V. 317 159 2002 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 99.0000001.0001.0001.00090.0090.0090.00P 1HELIX 1 1 SER A 15 GLY A 30 1 16 HELIX 2 2 THR A 50 LEU A 60 1 11 SHEET 1 A 4 ASN A 35 MET A 39 0 SHEET 2 A 4 MET A 42 LEU A 49 -1 O ALA A 46 N ASN A 35 SHEET 3 A 4 GLY A 4 PHE A 10 -1 N PHE A 10 O LYS A 43 SHEET 4 A 4 ILE A 65 GLU A 70 -1 O GLU A 69 N ILE A 7 HEADER PROTEIN BINDING 23-JAN-02 1ITP TITLE SOLUTION STRUCTURE OF POIA1 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEINASE A INHIBITOR 1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: IA-1=SERINE PROTEINASE INHIBITOR; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PLEUROTUS OSTREATUS; SOURCE 3 ORGANISM_COMMON: OYSTER MUSHROOM; SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA; SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET11D KEYWDS INHIBITOR, PROPEPTIDE, BETA-ALPHA-BETA EXPDTA NMR, 20 STRUCTURES AUTHOR H.SASAKAWA,S.YOSHINAGA,S.KOJIMA,A.TAMURA REVDAT 3 07-JAN-03 1ITP 1 REMARK REVDAT 2 10-APR-02 1ITP 1 JRNL REVDAT 1 13-FEB-02 1ITP 0 JRNL AUTH H.SASAKAWA,S.YOSHINAGA,S.KOJIMA,A.TAMURA JRNL TITL STRUCTURE OF POIA1, A HOMOLOGOUS PROTEIN TO THE JRNL TITL 2 PROPEPTIDE OF SUBTILISIN: IMPLICATION FOR PROTEIN JRNL TITL 3 FOLDABILITY AND THE FUNCTION AS AN INTRAMOLECULAR JRNL TITL 4 CHAPERONE JRNL REF J.MOL.BIOL. V. 317 159 2002 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.5 REMARK 3 AUTHORS : GNTERT REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1ITP COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-JAN-2002. REMARK 100 THE RCSB ID CODE IS RCSB005264. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303; 303; 303 REMARK 210 PH : 7.0; 7.0; 7.0 REMARK 210 IONIC STRENGTH : 25MM PI; 25MM PI; 25MM PI REMARK 210 PRESSURE : 1; 1; 1 REMARK 210 SAMPLE CONTENTS : 1MM POIA1, 25MM PHOSPHATE REMARK 210 BUFFER, 95% H2O, 5% D2O; 1MM REMARK 210 POIA1 U-15N, 25MM PHOSPHATE REMARK 210 BUFFER, 95% H2O, 5% D2O; 1MM REMARK 210 POIA1 U-15N, 13C, 25MM REMARK 210 PHOSPHATE BUFFER, 95% H2O, 5% REMARK 210 D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY, 3D_15N-SEPARATED_ REMARK 210 NOESY, 3HJNC'-HNCO REMARK 210 SPECTROMETER FIELD STRENGTH : 750 MHZ REMARK 210 SPECTROMETER MODEL : DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : DYANA 1.5, XWINNMR 1.3, REMARK 210 NMRPIPE 1.7 REMARK 210 METHOD USED : DISTANCE GEOMETRY REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 20 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY. 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 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 M RES CSSEQI PSI PHI REMARK 500 1 THR A 75 150.89 62.44 REMARK 500 2 SER A 2 135.78 72.44 REMARK 500 3 SER A 2 164.14 72.18 REMARK 500 4 THR A 75 143.98 63.40 REMARK 500 5 THR A 75 151.64 59.85 REMARK 500 5 THR A 76 -75.18 68.32 REMARK 500 9 THR A 75 150.43 67.15 REMARK 500 15 SER A 2 134.42 61.93 DBREF 1ITP A 2 77 GB 797424 AAB33247 1 76 SEQADV 1ITP GLY A 1 GB 797424 CLONING ARTIFACT SEQRES 1 A 77 GLY SER ALA GLY LYS PHE ILE VAL ILE PHE LYS ASN ASP SEQRES 2 A 77 VAL SER GLU ASP LYS ILE ARG GLU THR LYS ASP GLU VAL SEQRES 3 A 77 ILE ALA GLU GLY GLY THR ILE THR ASN GLU TYR ASN MET SEQRES 4 A 77 PRO GLY MET LYS GLY PHE ALA GLY GLU LEU THR PRO GLN SEQRES 5 A 77 SER LEU THR LYS PHE GLN GLY LEU GLN GLY ASP LEU ILE SEQRES 6 A 77 ASP SER ILE GLU GLU ASP GLY ILE VAL THR THR GLN HELIX 1 1 SER A 15 GLY A 30 1 16 HELIX 2 2 THR A 50 LEU A 60 1 11 SHEET 1 A 4 ASN A 35 MET A 39 0 SHEET 2 A 4 MET A 42 LEU A 49 -1 O ALA A 46 N ASN A 35 SHEET 3 A 4 GLY A 4 PHE A 10 -1 N PHE A 10 O LYS A 43 SHEET 4 A 4 ILE A 65 GLU A 70 -1 O GLU A 69 N ILE A 7 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 1 N GLY A 1 1.707 -15.450 5.562 1.00 0.00 N