HEADER CREATINASE 19-JUL-93 1CHM 1CHM 2 COMPND CREATINE AMIDINOHYDROLASE (E.C.3.5.3.3) 1CHM 3 SOURCE (PSEUDOMONAS PUTIDA) 1CHM 4 AUTHOR H.W.HOEFFKEN,S.H.KNOF,P.A.BARTLETT,R.HUBER,H.MOELLERING, 1CHM 5 AUTHOR 2 G.SCHUMACHER 1CHM 6 REVDAT 1 30-APR-94 1CHM 0 1CHM 7 JRNL AUTH M.COLL,S.H.KNOF,Y.OHGA,A.MESSERSCHMIDT,R.HUBER, 1CHM 8 JRNL AUTH 2 H.MOELLERING,L.RUESSMANN,GUENTER SCHUMACHER 1CHM 9 JRNL TITL ENZYMATIC MECHANISM OF CREATINE AMIDINOHYDROLASE 1CHM 10 JRNL TITL 2 AS DEDUCED FROM CRYSTAL STRUCTURES 1CHM 11 JRNL REF J.MOL.BIOL. V. 214 597 1990 1CHM 12 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 1CHM 13 REMARK 1 1CHM 14 REMARK 1 REFERENCE 1 1CHM 15 REMARK 1 AUTH H.W.HOEFFKEN,S.H.KNOF,P.A.BARTLETT,R.HUBER, 1CHM 16 REMARK 1 AUTH 2 H.MOELLERING,G.SCHUMACHER 1CHM 17 REMARK 1 TITL CRYSTAL STRUCTURE DETERMINATION, REFINEMENT AND 1CHM 18 REMARK 1 TITL 2 MOLECULAR MODEL OF CREATINE AMIDINOHYDROLASE FROM 1CHM 19 REMARK 1 TITL 3 PSEUDOMONAS PUTIDA 1CHM 20 REMARK 1 REF J.MOL.BIOL. V. 204 417 1988 1CHM 21 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 1CHM 22 REMARK 2 1CHM 23 REMARK 2 RESOLUTION. 1.9 ANGSTROMS. 1CHM 24 REMARK 3 1CHM 25 REMARK 3 REFINEMENT. 1CHM 26 REMARK 3 PROGRAM EREF 1CHM 27 REMARK 3 AUTHORS JACK,LEVITT 1CHM 28 REMARK 3 R VALUE 0.177 1CHM 29 REMARK 3 RMSD BOND DISTANCES 0.033 ANGSTROMS 1CHM 30 REMARK 3 RMSD BOND ANGLES 3.7 DEGREES 1CHM 31 REMARK 3 1CHM 32 REMARK 3 RESOLUTION RANGE 8.0 - 1.9 ANGSTROMS 1CHM 33 REMARK 3 1CHM 34 REMARK 3 NUMBER OF PROTEIN ATOMS 6374 1CHM 35 REMARK 3 NUMBER OF SOLVENT ATOMS 394 1CHM 36 SEQRES 1 A 401 GLN MET PRO LYS THR LEU ARG ILE ARG ASN GLY ASP LYS 1CHM 37 SEQRES 2 A 401 VAL ARG SER THR PHE SER ALA GLN GLU TYR ALA ASN ARG 1CHM 38 SEQRES 3 A 401 GLN ALA ARG LEU ARG ALA HIS LEU ALA ALA GLU ASN ILE 1CHM 39 SEQRES 4 A 401 ASP ALA ALA ILE PHE THR SER TYR HIS ASN ILE ASN TYR 1CHM 40 SEQRES 5 A 401 TYR SER ASP PHE LEU TYR CYS SER PHE GLY ARG PRO TYR 1CHM 41 SEQRES 6 A 401 ALA LEU VAL VAL THR GLU ASP ASP VAL ILE SER ILE SER 1CHM 42 SEQRES 7 A 401 ALA ASN ILE ASP GLY GLY GLN PRO TRP ARG ARG THR VAL 1CHM 43 SEQRES 8 A 401 GLY THR ASP ASN ILE VAL TYR THR ASP TRP GLN ARG ASP 1CHM 44 SEQRES 9 A 401 ASN TYR PHE ALA ALA ILE GLN GLN ALA LEU PRO LYS ALA 1CHM 45 SEQRES 10 A 401 ARG ARG ILE GLY ILE GLU HIS ASP HIS LEU ASN LEU GLN 1CHM 46 SEQRES 11 A 401 ASN ARG ASP LYS LEU ALA ALA ARG TYR PRO ASP ALA GLU 1CHM 47 SEQRES 12 A 401 LEU VAL ASP VAL ALA ALA ALA CYS MET ARG MET ARG MET 1CHM 48 SEQRES 13 A 401 ILE LYS SER ALA GLU GLU HIS VAL MET ILE ARG HIS GLY 1CHM 49 SEQRES 14 A 401 ALA ARG ILE ALA ASP ILE GLY GLY ALA ALA VAL VAL GLU 1CHM 50 SEQRES 15 A 401 ALA LEU GLY ASP GLN VAL PRO GLU TYR GLU VAL ALA LEU 1CHM 51 SEQRES 16 A 401 HIS ALA THR GLN ALA MET VAL ARG ALA ILE ALA ASP THR 1CHM 52 SEQRES 17 A 401 PHE GLU ASP VAL GLU LEU MET ASP THR TRP THR TRP PHE 1CHM 53 SEQRES 18 A 401 GLN SER GLY ILE ASN THR ASP GLY ALA HIS ASN PRO VAL 1CHM 54 SEQRES 19 A 401 THR THR ARG LYS VAL ASN LYS GLY ASP ILE LEU SER LEU 1CHM 55 SEQRES 20 A 401 ASN CYS PHE PRO MET ILE ALA GLY TYR TYR THR ALA LEU 1CHM 56 SEQRES 21 A 401 GLU ARG THR LEU PHE LEU ASP HIS CYS SER ASP ASP HIS 1CHM 57 SEQRES 22 A 401 LEU ARG LEU TRP GLN VAL ASN VAL GLU VAL HIS GLU ALA 1CHM 58 SEQRES 23 A 401 GLY LEU LYS LEU ILE LYS PRO GLY ALA ARG CYS SER ASP 1CHM 59 SEQRES 24 A 401 ILE ALA ARG GLU LEU ASN GLU ILE PHE LEU LYS HIS ASP 1CHM 60 SEQRES 25 A 401 VAL LEU GLN TYR ARG THR PHE GLY TYR GLY HIS SER PHE 1CHM 61 SEQRES 26 A 401 GLY THR LEU SER HIS TYR TYR GLY ARG GLU ALA GLY LEU 1CHM 62 SEQRES 27 A 401 GLU LEU ARG GLU ASP ILE ASP THR VAL LEU GLU PRO GLY 1CHM 63 SEQRES 28 A 401 MET VAL VAL SER MET GLU PRO MET ILE MET LEU PRO GLU 1CHM 64 SEQRES 29 A 401 GLY LEU PRO GLY ALA GLY GLY TYR ARG GLU HIS ASP ILE 1CHM 65 SEQRES 30 A 401 LEU ILE VAL ASN GLU ASN GLY ALA GLU ASN ILE THR LYS 1CHM 66 SEQRES 31 A 401 PHE PRO TYR GLY PRO GLU LYS ASN ILE ILE ARG 1CHM 67 SEQRES 1 B 401 GLN MET PRO LYS THR LEU ARG ILE ARG ASN GLY ASP LYS 1CHM 68 SEQRES 2 B 401 VAL ARG SER THR PHE SER ALA GLN GLU TYR ALA ASN ARG 1CHM 69 SEQRES 3 B 401 GLN ALA ARG LEU ARG ALA HIS LEU ALA ALA GLU ASN ILE 1CHM 70 SEQRES 4 B 401 ASP ALA ALA ILE PHE THR SER TYR HIS ASN ILE ASN TYR 1CHM 71 SEQRES 5 B 401 TYR SER ASP PHE LEU TYR CYS SER PHE GLY ARG PRO TYR 1CHM 72 SEQRES 6 B 401 ALA LEU VAL VAL THR GLU ASP ASP VAL ILE SER ILE SER 1CHM 73 SEQRES 7 B 401 ALA ASN ILE ASP GLY GLY GLN PRO TRP ARG ARG THR VAL 1CHM 74 SEQRES 8 B 401 GLY THR ASP ASN ILE VAL TYR THR ASP TRP GLN ARG ASP 1CHM 75 SEQRES 9 B 401 ASN TYR PHE ALA ALA ILE GLN GLN ALA LEU PRO LYS ALA 1CHM 76 SEQRES 10 B 401 ARG ARG ILE GLY ILE GLU HIS ASP HIS LEU ASN LEU GLN 1CHM 77 SEQRES 11 B 401 ASN ARG ASP LYS LEU ALA ALA ARG TYR PRO ASP ALA GLU 1CHM 78 SEQRES 12 B 401 LEU VAL ASP VAL ALA ALA ALA CYS MET ARG MET ARG MET 1CHM 79 SEQRES 13 B 401 ILE LYS SER ALA GLU GLU HIS VAL MET ILE ARG HIS GLY 1CHM 80 SEQRES 14 B 401 ALA ARG ILE ALA ASP ILE GLY GLY ALA ALA VAL VAL GLU 1CHM 81 SEQRES 15 B 401 ALA LEU GLY ASP GLN VAL PRO GLU TYR GLU VAL ALA LEU 1CHM 82 SEQRES 16 B 401 HIS ALA THR GLN ALA MET VAL ARG ALA ILE ALA ASP THR 1CHM 83 SEQRES 17 B 401 PHE GLU ASP VAL GLU LEU MET ASP THR TRP THR TRP PHE 1CHM 84 SEQRES 18 B 401 GLN SER GLY ILE ASN THR ASP GLY ALA HIS ASN PRO VAL 1CHM 85 SEQRES 19 B 401 THR THR ARG LYS VAL ASN LYS GLY ASP ILE LEU SER LEU 1CHM 86 SEQRES 20 B 401 ASN CYS PHE PRO MET ILE ALA GLY TYR TYR THR ALA LEU 1CHM 87 SEQRES 21 B 401 GLU ARG THR LEU PHE LEU ASP HIS CYS SER ASP ASP HIS 1CHM 88 SEQRES 22 B 401 LEU ARG LEU TRP GLN VAL ASN VAL GLU VAL HIS GLU ALA 1CHM 89 SEQRES 23 B 401 GLY LEU LYS LEU ILE LYS PRO GLY ALA ARG CYS SER ASP 1CHM 90 SEQRES 24 B 401 ILE ALA ARG GLU LEU ASN GLU ILE PHE LEU LYS HIS ASP 1CHM 91 SEQRES 25 B 401 VAL LEU GLN TYR ARG THR PHE GLY TYR GLY HIS SER PHE 1CHM 92 SEQRES 26 B 401 GLY THR LEU SER HIS TYR TYR GLY ARG GLU ALA GLY LEU 1CHM 93 SEQRES 27 B 401 GLU LEU ARG GLU ASP ILE ASP THR VAL LEU GLU PRO GLY 1CHM 94 SEQRES 28 B 401 MET VAL VAL SER MET GLU PRO MET ILE MET LEU PRO GLU 1CHM 95 SEQRES 29 B 401 GLY LEU PRO GLY ALA GLY GLY TYR ARG GLU HIS ASP ILE 1CHM 96 SEQRES 30 B 401 LEU ILE VAL ASN GLU ASN GLY ALA GLU ASN ILE THR LYS 1CHM 97 SEQRES 31 B 401 PHE PRO TYR GLY PRO GLU LYS ASN ILE ILE ARG 1CHM 98 FTNOTE 1 1CHM 99 FTNOTE 1 GLU B 383 - ASN B 384 OMEGA =212.90 1CHM 100 FTNOTE 1 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 1CHM 101 HET CMS A 404 9 CARBAMOYL SARCOSINE 1CHM 102 HET CMS B 404 9 CARBAMOYL SARCOSINE 1CHM 103 FORMUL 3 CMS 2(C4 H8 N2 O3) 1CHM 104 FORMUL 4 HOH *394(H2 O1) 1CHM 105 CRYST1 60.830 110.550 62.630 90.00 102.22 90.00 P 21 4 1CHM 106 ORIGX1 1.000000 0.000000 0.216573 0.00000 1CHM 107 ORIGX2 0.000000 1.000000 0.000000 0.00000 1CHM 108 ORIGX3 0.000000 0.000000 1.023183 0.00000 1CHM 109 SCALE1 0.016439 0.000000 0.003560 0.00000 1CHM 110 SCALE2 0.000000 0.009046 0.000000 0.00000 1CHM 111 SCALE3 0.000000 0.000000 0.016337 0.00000 1CHM 112