HEADER HYDROLASE (SERINE PROTEINASE) 07-MAR-85 2ALP 2ALP 3 COMPND ALPHA-LYTIC PROTEASE (E.C.3.4.21.12) 2ALPB 1 SOURCE (LYSOBACTER $ENZYMOGENES) 2ALP 5 AUTHOR M.FUJINAGA,L.T.J.DELBAERE,G.D.BRAYER,M.N.G.JAMES 2ALP 6 REVDAT 3 15-OCT-89 2ALPB 1 COMPND 2ALPB 2 REVDAT 2 29-OCT-85 2ALPA 1 JRNL 2ALPA 1 REVDAT 1 17-JUL-85 2ALP 0 2ALP 7 SPRSDE 17-JUL-85 2ALP 1ALP 2ALP 8 JRNL AUTH M.FUJINAGA,L.T.J.DELBAERE,G.D.BRAYER,M.N.G.JAMES 2ALP 9 JRNL TITL REFINED STRUCTURE OF ALPHA-LYTIC PROTEASE AT 1.7 2ALP 10 JRNL TITL 2 ANGSTROMS RESOLUTION. ANALYSIS OF HYDROGEN BONDING 2ALP 11 JRNL TITL 3 AND SOLVENT STRUCTURE 2ALP 12 JRNL REF J.MOL.BIOL. V. 184 479 1985 2ALPA 2 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 2ALPA 3 REMARK 1 2ALP 15 REMARK 1 REFERENCE 1 2ALP 16 REMARK 1 AUTH G.D.BRAYER,L.T.J.DELBAERE,M.N.G.JAMES 2ALP 17 REMARK 1 TITL MOLECULAR STRUCTURE OF THE ALPHA-*LYTIC PROTEASE 2ALP 18 REMARK 1 TITL 2 FROM MYXOBACTER 495 AT 2.8 ANGSTROMS RESOLUTION 2ALP 19 REMARK 1 REF J.MOL.BIOL. V. 131 743 1979 2ALP 20 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 2ALP 21 REMARK 1 REFERENCE 2 2ALP 22 REMARK 1 AUTH L.T.J.DELBAERE,G.D.BRAYER,M.N.G.JAMES 2ALP 23 REMARK 1 TITL COMPARISON OF THE PREDICTED MODEL OF ALPH-LYTIC 2ALP 24 REMARK 1 TITL 2 PROTEASE WITH THE X-RAY STRUCTURE 2ALP 25 REMARK 1 REF NATURE V. 279 165 1979 2ALP 26 REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 006 2ALP 27 REMARK 1 REFERENCE 3 2ALP 28 REMARK 1 AUTH M.N.G.JAMES,L.T.J.DELBAERE,G.D.BRAYER 2ALP 29 REMARK 1 TITL AMINO ACID SEQUENCE ALIGNMENT OF BACTERIAL AND 2ALP 30 REMARK 1 TITL 2 MAMMALIAN PANCREATIC SERINE PROTEASES BASED ON 2ALP 31 REMARK 1 TITL 3 TOPOLOGICAL EQUIVALENCES 2ALP 32 REMARK 1 REF CAN.J.BIOCHEM. V. 56 396 1978 2ALP 33 REMARK 1 REFN ASTM CJBIAE CN ISSN 0008-4018 415 2ALP 34 REMARK 2 2ALP 35 REMARK 2 RESOLUTION. 1.7 ANGSTROMS. 2ALP 36 REMARK 3 2ALP 37 REMARK 3 REFINEMENT. BY THE METHOD OF KONNERT AND HENDRICKSON. 2ALP 38 REMARK 3 THE R VALUE IS 0.131 FOR ALL DATA IN THE RANGE 8.0 TO 1.7 2ALP 39 REMARK 3 ANGSTROMS WITH INTENSITY .GT. 2*SIGMA(I). THE RMS 2ALP 40 REMARK 3 DEVIATION FROM IDEALITY OF THE COORDINATES IS 0.14 2ALP 41 REMARK 3 ANGSTROMS. THE RMS DEVIATION FROM IDEALITY OF THE BOND 2ALP 42 REMARK 3 LENGTHS IS 0.019 ANGSTROMS. THE RMS DEVIATION FROM 2ALP 43 REMARK 3 IDEALITY OF THE BOND ANGLES IS 0.030 ANGSTROMS. 2ALP 44 REMARK 4 2ALP 45 REMARK 4 THE RESIDUE NUMBERING SCHEME HAS BEEN CHANGED FROM THAT 2ALP 46 REMARK 4 USED IN PREVIOUS PUBLICATIONS AND IS DESCRIBED IN THE 2ALP 47 REMARK 4 PAPER CITED IN THE *JRNL* RECORDS ABOVE. 2ALP 48 REMARK 5 2ALPA 4 REMARK 5 CORRECTION. UPDATE JRNL REFERENCE TO REFLECT PUBLICATION. 2ALPA 5 REMARK 5 29-OCT-85. 2ALPA 6 REMARK 6 2ALPB 3 REMARK 6 CORRECTION. ADD E.C. NUMBER TO COMPND RECORD. 15-OCT-89. 2ALPB 4 SEQRES 1 198 ALA ASN ILE VAL GLY GLY ILE GLU TYR SER ILE ASN ASN 2ALP 49 SEQRES 2 198 ALA SER LEU CYS SER VAL GLY PHE SER VAL THR ARG GLY 2ALP 50 SEQRES 3 198 ALA THR LYS GLY PHE VAL THR ALA GLY HIS CYS GLY THR 2ALP 51 SEQRES 4 198 VAL ASN ALA THR ALA ARG ILE GLY GLY ALA VAL VAL GLY 2ALP 52 SEQRES 5 198 THR PHE ALA ALA ARG VAL PHE PRO GLY ASN ASP ARG ALA 2ALP 53 SEQRES 6 198 TRP VAL SER LEU THR SER ALA GLN THR LEU LEU PRO ARG 2ALP 54 SEQRES 7 198 VAL ALA ASN GLY SER SER PHE VAL THR VAL ARG GLY SER 2ALP 55 SEQRES 8 198 THR GLU ALA ALA VAL GLY ALA ALA VAL CYS ARG SER GLY 2ALP 56 SEQRES 9 198 ARG THR THR GLY TYR GLN CYS GLY THR ILE THR ALA LYS 2ALP 57 SEQRES 10 198 ASN VAL THR ALA ASN TYR ALA GLU GLY ALA VAL ARG GLY 2ALP 58 SEQRES 11 198 LEU THR GLN GLY ASN ALA CYS MET GLY ARG GLY ASP SER 2ALP 59 SEQRES 12 198 GLY GLY SER TRP ILE THR SER ALA GLY GLN ALA GLN GLY 2ALP 60 SEQRES 13 198 VAL MET SER GLY GLY ASN VAL GLN SER ASN GLY ASN ASN 2ALP 61 SEQRES 14 198 CYS GLY ILE PRO ALA SER GLN ARG SER SER LEU PHE GLU 2ALP 62 SEQRES 15 198 ARG LEU GLN PRO ILE LEU SER GLN TYR GLY LEU SER LEU 2ALP 63 SEQRES 16 198 VAL THR GLY 2ALP 64 FTNOTE 1 2ALP 65 FTNOTE 1 RESIDUE 95 IS A CIS-PROLINE. 2ALP 66 HET SO4 1 5 SULFATE 2ALP 67 HET SO4 2 5 SULFATE 2ALP 68 FORMUL 2 SO4 2(O4 S1) 2ALP 69 FORMUL 3 HOH *156(H2 O1) 2ALP 70 SSBOND 1 CYS 42 CYS 58 2ALP 71 SSBOND 2 CYS 137 CYS 159 2ALP 72 SSBOND 3 CYS 189 CYS 220A 2ALP 73 CRYST1 66.210 66.210 80.010 90.00 90.00 120.00 P 32 2 1 6 2ALP 74 ORIGX1 .015103 .008720 0.000000 0.00000 2ALP 75 ORIGX2 0.000000 .017440 0.000000 0.00000 2ALP 76 ORIGX3 0.000000 0.000000 .012498 0.00000 2ALP 77 SCALE1 .015103 .008720 0.000000 0.00000 2ALP 78 SCALE2 0.000000 .017440 0.000000 0.00000 2ALP 79 SCALE3 0.000000 0.000000 .012498 0.00000 2ALP 80