HEADER ELECTRON TRANSFER(CUPROPROTEIN) 28-JAN-94 1PMY 1PMY 2 COMPND PSEUDOAZURIN (CUPREDOXIN) 1PMY 3 SOURCE (METHYLOBACTERIUM EXTORQUENS, STRAIN AM1) 1PMY 4 AUTHOR T.INOUE,Y.KAI,S.HARADA,N.KASAI,Y.OHSHIRO,S.SUZUKI, 1PMY 5 AUTHOR 2 T.KOHZUMA,J.TOBARI 1PMY 6 REVDAT 1 31-JUL-94 1PMY 0 1PMY 7 JRNL AUTH T.INOUE,Y.KAI,S.HARADA,N.KASAI,Y.OHSHIRO,S.SUZUKI, 1PMY 8 JRNL AUTH 2 T.KOHZUMA,J.TOBARI 1PMY 9 JRNL TITL REFINED CRYSTAL STRUCTURE OF PSEUDOAZURIN FROM 1PMY 10 JRNL TITL 2 METHYLOBACTERIUM EXTORQUENS AM1 AT 1.5 ANGSTROMS 1PMY 11 JRNL TITL 3 RESOLUTION 1PMY 12 JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 50 317 1994 1PMY 13 JRNL REFN ASTM ABCRE6 DK ISSN 0907-4449 0766 1PMY 14 REMARK 1 1PMY 15 REMARK 1 REFERENCE 1 1PMY 16 REMARK 1 AUTH T.INOUE,Y.KAI,S.HARADA,N.KASAI,S.SUZUKI,T.KOHZUMA, 1PMY 17 REMARK 1 AUTH 2 J.TOBARI 1PMY 18 REMARK 1 TITL PRELIMINARY CRYSTALLOGRAPHIC STUDY OF A 1PMY 19 REMARK 1 TITL 2 PSEUDOAZURIN FROM METHYLOTROPHIC BACTERIUM, 1PMY 20 REMARK 1 TITL 3 METHYLOBACTERIUM EXTORQUENS AM1 1PMY 21 REMARK 1 REF J.MOL.BIOL. V. 218 19 1991 1PMY 22 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 0070 1PMY 23 REMARK 2 1PMY 24 REMARK 2 RESOLUTION. 1.5 ANGSTROMS. 1PMY 25 REMARK 3 1PMY 26 REMARK 3 REFINEMENT. 1PMY 27 REMARK 3 PROGRAM 1 X-PLOR 1PMY 28 REMARK 3 AUTHORS 1 BRUNGER 1PMY 29 REMARK 3 PROGRAM 2 PROLSQ 1PMY 30 REMARK 3 AUTHORS 2 KONNERT,HENDRICKSON 1PMY 31 REMARK 3 R VALUE 0.199 1PMY 32 REMARK 3 RMSD BOND DISTANCES 0.024 ANGSTROMS 1PMY 33 REMARK 3 RMSD BOND ANGLE DISTANCES 0.039 ANGSTROMS 1PMY 34 REMARK 3 RMSD PLANAR 1-4 DISTANCE 0.044 ANGSTROMS 1PMY 35 REMARK 3 1PMY 36 REMARK 3 NUMBER OF REFLECTIONS 14365 1PMY 37 REMARK 3 RESOLUTION RANGE 8.0 - 1.5 ANGSTROMS 1PMY 38 REMARK 3 DATA CUTOFF 3.0 SIGMA(F) 1PMY 39 REMARK 3 PERCENT COMPLETION 75.5 1PMY 40 REMARK 4 1PMY 41 REMARK 4 PDB ADVISORY NOTICE: 1PMY 42 REMARK 4 THERE IS A VERY SHORT PACKING INTERACTION BETWEEN TYR 55 1PMY 43 REMARK 4 AND SER 10. 1PMY 44 SEQRES 1 123 ASP GLU VAL ALA VAL LYS MET LEU ASN SER GLY PRO GLY 1PMY 45 SEQRES 2 123 GLY MET MET VAL PHE ASP PRO ALA LEU VAL ARG LEU LYS 1PMY 46 SEQRES 3 123 PRO GLY ASP SER ILE LYS PHE LEU PRO THR ASP LYS GLY 1PMY 47 SEQRES 4 123 HIS ASN VAL GLU THR ILE LYS GLY MET ALA PRO ASP GLY 1PMY 48 SEQRES 5 123 ALA ASP TYR VAL LYS THR THR VAL GLY GLN GLU ALA VAL 1PMY 49 SEQRES 6 123 VAL LYS PHE ASP LYS GLU GLY VAL TYR GLY PHE LYS CYS 1PMY 50 SEQRES 7 123 ALA PRO HIS TYR MET MET GLY MET VAL ALA LEU VAL VAL 1PMY 51 SEQRES 8 123 VAL GLY ASP LYS ARG ASP ASN LEU GLU ALA ALA LYS SER 1PMY 52 SEQRES 9 123 VAL GLN HIS ASN LYS LEU THR GLN LYS ARG LEU ASP PRO 1PMY 53 SEQRES 10 123 LEU PHE ALA GLN ILE GLN 1PMY 54 FTNOTE 1 1PMY 55 FTNOTE 1 CIS PROLINE - PRO 20 1PMY 56 HET CU 124 1 COPPER ++ ION 1PMY 57 FORMUL 2 CU CU1 ++ 1PMY 58 FORMUL 3 HOH *132(H2 O1) 1PMY 59 HELIX 1 A1 LEU 99 SER 104 1 1PMY 60 HELIX 2 A2 LYS 109 GLN 123 1 HIGH B VALUE AT END DISTORTS 1PMY 61 SHEET 1 S1 4 VAL 17 ASP 19 0 1PMY 62 SHEET 2 S1 4 ASP 1 LEU 8 -1 N LEU 8 O VAL 17 1PMY 63 SHEET 3 S1 4 ASP 29 PRO 35 1 O SER 30 N VAL 3 1PMY 64 SHEET 4 S1 4 GLU 63 PHE 68 -1 O ALA 64 N PHE 33 1PMY 65 SHEET 1 S2 5 VAL 56 THR 58 0 1PMY 66 SHEET 2 S2 5 VAL 42 THR 44 -1 O VAL 42 N THR 58 1PMY 67 SHEET 3 S2 5 GLY 72 CYS 78 -1 N LYS 77 O GLU 43 1PMY 68 SHEET 4 S2 5 MET 86 VAL 92 -1 N VAL 92 O GLY 72 1PMY 69 SHEET 5 S2 5 ALA 21 LEU 25 1 O ALA 21 N LEU 89 1PMY 70 TURN 1 T1 GLY 11 GLY 14 1PMY 71 TURN 2 T2 LYS 26 ASP 29 1PMY 72 TURN 3 T3 ILE 45 MET 48 1PMY 73 TURN 4 T4 PRO 50 ALA 53 1PMY 74 TURN 5 T5 THR 59 GLN 62 1PMY 75 CRYST1 52.619 63.280 35.133 90.00 90.00 90.00 P 21 21 21 4 1PMY 76 ORIGX1 1.000000 0.000000 0.000000 0.00000 1PMY 77 ORIGX2 0.000000 1.000000 0.000000 0.00000 1PMY 78 ORIGX3 0.000000 0.000000 1.000000 0.00000 1PMY 79 SCALE1 0.019005 0.000000 0.000000 0.00000 1PMY 80 SCALE2 0.000000 0.015803 0.000000 0.00000 1PMY 81 SCALE3 0.000000 0.000000 0.028463 0.00000 1PMY 82