HEADER ELECTRON TRANSPORT(CYTOCHROME) 02-JAN-94 1CTM 1CTM 2 COMPND CYTOCHROME F (REDUCED) 1CTM 3 SOURCE TURNIP (BRASSICA RAPA) 1CTM 4 AUTHOR S.E.MARTINEZ,D.HUANG,A.SZCZEPANIAK,W.A.CRAMER,J.L.SMITH 1CTM 5 REVDAT 1 31-MAY-94 1CTM 0 1CTM 6 JRNL AUTH S.E.MARTINEZ,D.HUANG,A.SZCZEPANIAK,W.A.CRAMER, 1CTM 7 JRNL AUTH 2 J.L.SMITH 1CTM 8 JRNL TITL CRYSTAL STRUCTURE OF CHLOROPLAST CYTOCHROME F 1CTM 9 JRNL TITL 2 REVEALS A NOVEL CYTOCHROME FOLD AND UNEXPECTED 1CTM 10 JRNL TITL 3 HEME LIGATION 1CTM 11 JRNL REF STRUCTURE V. 2 95 1994 1CTM 12 JRNL REFN ASTM UK ISSN 0969-2126 0200 1CTM 13 REMARK 1 1CTM 14 REMARK 1 REFERENCE 1 1CTM 15 REMARK 1 AUTH S.E.MARTINEZ,J.L.SMITH,D.HUANG,A.SZCZEPANIAK, 1CTM 16 REMARK 1 AUTH 2 W.A.CRAMER 1CTM 17 REMARK 1 TITL CRYSTALLOGRAPHIC STUDIES OF THE LUMEN-SIDE DOMAIN 1CTM 18 REMARK 1 TITL 2 OF TURNIP CYTOCHROME 1CTM 19 REMARK 1 EDIT N.MURATA 1CTM 20 REMARK 1 REF RESEARCH IN PHOTOSYNTHESIS: V. 2 495 1992 1CTM 21 REMARK 1 REF 2 PROCEEDINGS OF THE IXTH 1CTM 22 REMARK 1 REF 3 INTERNATIONAL CONGRESS ON 1CTM 23 REMARK 1 REF 4 PHOTOSYNTHESIS 1CTM 24 REMARK 1 PUBL KLUWER ACADEMIC, DORDRECHT 1CTM 25 REMARK 1 REFN ISBN 0-7923-2073-5 2025 1CTM 26 REMARK 2 1CTM 27 REMARK 2 RESOLUTION. 2.3 ANGSTROMS. 1CTM 28 REMARK 3 1CTM 29 REMARK 3 REFINEMENT. 1CTM 30 REMARK 3 PROGRAM X-PLOR 1CTM 31 REMARK 3 AUTHORS BRUNGER 1CTM 32 REMARK 3 R VALUE 0.198 1CTM 33 REMARK 3 FREE R VALUE 0.277 1CTM 34 REMARK 3 RMSD BOND DISTANCES 0.014 ANGSTROMS 1CTM 35 REMARK 3 RMSD BOND ANGLES 2.99 DEGREES 1CTM 36 REMARK 3 1CTM 37 REMARK 3 NUMBER OF REFLECTIONS 10903 1CTM 38 REMARK 3 RESOLUTION RANGE 6.0 - 2.3 ANGSTROMS 1CTM 39 REMARK 3 DATA CUTOFF 1.0 SIGMA(F) 1CTM 40 REMARK 3 PERCENT COMPLETION 89.4 1CTM 41 REMARK 3 1CTM 42 REMARK 3 NUMBER OF PROTEIN ATOMS 1968 1CTM 43 REMARK 3 NUMBER OF SOLVENT ATOMS 113 1CTM 44 REMARK 3 1CTM 45 REMARK 3 FURTHER REFINEMENT IS IN PROGRESS. 1CTM 46 REMARK 4 1CTM 47 REMARK 4 THE THYLAKOID LUMEN-SIDE DOMAIN (RESIDUES 1 - 252) OF 1CTM 48 REMARK 4 CYTOCHROME F (285 RESIDUES) WAS CRYSTALLIZED. ITS 1CTM 49 REMARK 4 STRUCTURE WAS DETERMINED BY MIRAS AT 2.8 ANGSTROMS 1CTM 50 REMARK 4 RESOLUTION. 1CTM 51 REMARK 5 1CTM 52 REMARK 5 2FO-FC ELECTRON DENSITY AT 2.3 ANGSTROMS RESOLUTION IS 1CTM 53 REMARK 5 CONTINUOUS FOR RESIDUES 1 - 248, WEAK FOR RESIDUES 249 - 1CTM 54 REMARK 5 250, AND MISSING FOR RESIDUES 251 - 252. 1CTM 55 REMARK 6 1CTM 56 REMARK 6 THE HEME GROUP IS COVALENTLY BOUND THROUGH THIOETHER 1CTM 57 REMARK 6 LINKS TO CYS 21 AND CYS 24. HEME FE LIGANDS ARE HIS 25 AND 1CTM 58 REMARK 6 THE AMINO GROUP OF TYR 1. 1CTM 59 REMARK 7 1CTM 60 REMARK 7 INDIVIDUAL BETA SHEETS ARE DENOTED BY A LETTER AND BY A 1CTM 61 REMARK 7 DOMAIN INDICATOR. THERE ARE TWO DOMAINS, LARGE DOMAIN (LD) 1CTM 62 REMARK 7 AND SMALL DOMAIN (SD). SHEET A IN THE LARGE DOMAIN IS THEN 1CTM 63 REMARK 7 DENOTED LDA, SHEET A IN THE SMALL DOMAIN SDA, ETC. 1CTM 64 REMARK 8 1CTM 65 REMARK 8 ALL HELICES ARE IN THE LARGE DOMAIN ONLY AND ARE DENOTED BY 1CTM 66 REMARK 8 A LETTER ONLY. 1CTM 67 REMARK 9 1CTM 68 REMARK 9 STRAND 3 OF SHEET SDA AND STRAND 3 OF SHEET SDB ARE PARTS 1CTM 69 REMARK 9 OF A PIECE OF EXTENDED CHAIN WHICH IS SPLIT BETWEEN BETWEEN 1CTM 70 REMARK 9 THE TWO SHEETS. RESIDUES 176 - 179 BELONG TO SHEET SDA AND 1CTM 71 REMARK 9 RESIDUES 181 - 185 BELONG TO SHEET SDB WITH A KINK IN 1CTM 72 REMARK 9 BETWEEN. 1CTM 73 REMARK 10 1CTM 74 REMARK 10 THE SEQUENCE PRESENTED IN THIS ENTRY HAS NOT BEEN DEPOSITED 1CTM 75 REMARK 10 IN THE SEQUENCE DATABASES. IT IS DESCRIBED IN THE *JRNL* 1CTM 76 REMARK 10 ARTICLE. 1CTM 77 SEQRES 1 250 TYR PRO ILE PHE ALA GLN GLN ASN TYR GLU ASN PRO ARG 1CTM 78 SEQRES 2 250 GLU ALA THR GLY ARG ILE VAL CYS ALA ASN CYS HIS LEU 1CTM 79 SEQRES 3 250 ALA SER LYS PRO VAL ASP ILE GLU VAL PRO GLN ALA VAL 1CTM 80 SEQRES 4 250 LEU PRO ASP THR VAL PHE GLU ALA VAL VAL LYS ILE PRO 1CTM 81 SEQRES 5 250 TYR ASP MET GLN LEU LYS GLN VAL LEU ALA ASN GLY LYS 1CTM 82 SEQRES 6 250 LYS GLY ALA LEU ASN VAL GLY ALA VAL LEU ILE LEU PRO 1CTM 83 SEQRES 7 250 GLU GLY PHE GLU LEU ALA PRO PRO ASP ARG ILE SER PRO 1CTM 84 SEQRES 8 250 GLU MET LYS GLU LYS ILE GLY ASN LEU SER PHE GLN ASN 1CTM 85 SEQRES 9 250 TYR ARG PRO ASN LYS LYS ASN ILE LEU VAL ILE GLY PRO 1CTM 86 SEQRES 10 250 VAL PRO GLY GLN LYS TYR SER GLU ILE THR PHE PRO ILE 1CTM 87 SEQRES 11 250 LEU ALA PRO ASP PRO ALA THR ASN LYS ASP VAL HIS PHE 1CTM 88 SEQRES 12 250 LEU LYS TYR PRO ILE TYR VAL GLY GLY ASN ARG GLY ARG 1CTM 89 SEQRES 13 250 GLY GLN ILE TYR PRO ASP GLY SER LYS SER ASN ASN THR 1CTM 90 SEQRES 14 250 VAL TYR ASN ALA THR ALA GLY GLY ILE ILE SER LYS ILE 1CTM 91 SEQRES 15 250 LEU ARG LYS GLU LYS GLY GLY TYR GLU ILE THR ILE VAL 1CTM 92 SEQRES 16 250 ASP ALA SER ASN GLU ARG GLN VAL ILE ASP ILE ILE PRO 1CTM 93 SEQRES 17 250 ARG GLY LEU GLU LEU LEU VAL SER GLU GLY GLU SER ILE 1CTM 94 SEQRES 18 250 LYS LEU ASP GLN PRO LEU THR SER ASN PRO ASN VAL GLY 1CTM 95 SEQRES 19 250 GLY PHE GLY GLN GLY ASP ALA GLU ILE VAL LEU GLN ASP 1CTM 96 SEQRES 20 250 PRO LEU ARG 1CTM 97 FTNOTE 1 1CTM 98 FTNOTE 1 CIS PROLINE - PRO 117 1CTM 99 HET HEM 253 43 PROTOPORPHYRIN IX CONTAINS FE(II) 1CTM 100 FORMUL 2 HEM C34 H32 N4 O4 FE1 ++ 1CTM 101 FORMUL 3 HOH *113(H2 O1) 1CTM 102 HELIX 1 A TYR 1 TYR 9 1 MIXED 4/16 AND 3/10 H BONDING 1CTM 103 HELIX 2 B ILE 19 HIS 25 1 MIXED 4/16 AND 3/10 H BONDING 1CTM 104 HELIX 3 C SER 90 ILE 97 1 1CTM 105 SHEET 1 LDA 4 PRO 30 PRO 36 0 1CTM 106 SHEET 2 LDA 4 THR 43 ILE 51 -1 O VAL 48 N GLU 34 1CTM 107 SHEET 3 LDA 4 SER 124 ALA 132 -1 O PHE 128 N ALA 47 1CTM 108 SHEET 4 LDA 4 GLU 82 ALA 84 -1 O GLU 82 N LEU 131 1CTM 109 SHEET 1 LDB 6 GLN 37 VAL 39 0 1CTM 110 SHEET 2 LDB 6 GLY 234 GLN 246 1 O VAL 244 N VAL 39 1CTM 111 SHEET 3 LDB 6 LEU 144 GLY 155 -1 O VAL 150 N GLY 239 1CTM 112 SHEET 4 LDB 6 ASN 70 LEU 77 -1 O VAL 74 N GLY 151 1CTM 113 SHEET 5 LDB 6 ASN 111 VAL 118 -1 O ILE 115 N ALA 73 1CTM 114 SHEET 6 LDB 6 GLN 103 TYR 105 -1 O GLN 103 N VAL 114 1CTM 115 SHEET 1 LDC 2 GLN 59 LEU 61 0 1CTM 116 SHEET 2 LDC 2 LYS 65 GLY 67 -1 N GLY 67 O GLN 59 1CTM 117 SHEET 1 LDD 2 GLN 158 TYR 160 0 1CTM 118 SHEET 2 LDD 2 SER 164 SER 166 -1 O SER 164 N TYR 160 1CTM 119 SHEET 1 SDA 4 ARG 201 PRO 208 0 1CTM 120 SHEET 2 SDA 4 GLY 189 ASP 196 -1 O ILE 192 N ASP 205 1CTM 121 SHEET 3 SDA 4 GLY 176 ILE 179 -1 O ILE 178 N VAL 195 1CTM 122 SHEET 4 SDA 4 GLU 219 LYS 222 -1 N ILE 221 O GLY 177 1CTM 123 SHEET 1 SDB 4 ARG 201 PRO 208 0 1CTM 124 SHEET 2 SDB 4 GLY 189 ASP 196 -1 O ILE 192 N ASP 205 1CTM 125 SHEET 3 SDB 4 LYS 181 LYS 185 -1 N LEU 183 O GLU 191 1CTM 126 SHEET 4 SDB 4 GLU 219 LYS 222 -1 1CTM 127 CRYST1 79.200 81.900 46.300 90.00 90.00 90.00 P 21 21 21 4 1CTM 128 ORIGX1 1.000000 0.000000 0.000000 0.00000 1CTM 129 ORIGX2 0.000000 1.000000 0.000000 0.00000 1CTM 130 ORIGX3 0.000000 0.000000 1.000000 0.00000 1CTM 131 SCALE1 0.012626 0.000000 0.000000 0.00000 1CTM 132 SCALE2 0.000000 0.012210 0.000000 0.00000 1CTM 133 SCALE3 0.000000 0.000000 0.021598 0.00000 1CTM 134