HEADER REDUCTASE(ACTING ON CH2) 19-JAN-93 1RIB 1RIB 2 COMPND PROTEIN R2 OF RIBONUCLEOTIDE REDUCTASE (E.C.1.17.4.1) 1RIB 3 SOURCE (ESCHERICHIA COLI) 1RIB 4 AUTHOR H.EKLUND 1RIB 5 REVDAT 1 31-JAN-94 1RIB 0 1RIB 6 JRNL AUTH P.NORDLUND,H.EKLUND 1RIB 7 JRNL TITL STRUCTURE AND FUNCTION OF THE ESCHERICHIA COLI 1RIB 8 JRNL TITL 2 RIBONUCLEOTIDE REDUCTASE PROTEIN R2 1RIB 9 JRNL REF J.MOL.BIOL. V. 232 123 1993 1RIB 10 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 1RIB 11 REMARK 1 1RIB 12 REMARK 1 REFERENCE 1 1RIB 13 REMARK 1 AUTH M.J.SIPPL 1RIB 14 REMARK 1 TITL RECOGNITION OF ERRORS IN THREE-DIMENSIONAL 1RIB 15 REMARK 1 TITL 2 STRUCTURES OF PROTEINS 1RIB 16 REMARK 1 REF PROTEINS.STRUCT.,FUNCT., V. 17 355 1993 1RIB 17 REMARK 1 REF 2 GENET. 1RIB 18 REMARK 1 REFN ASTM PSFGEY US ISSN 0887-3585 867 1RIB 19 REMARK 2 1RIB 20 REMARK 2 RESOLUTION. 2.2 ANGSTROMS. 1RIB 21 REMARK 3 1RIB 22 REMARK 3 REFINEMENT. 1RIB 23 REMARK 3 PROGRAM X-PLOR 1RIB 24 REMARK 3 AUTHORS BRUNGER 1RIB 25 REMARK 3 R VALUE 0.175 1RIB 26 REMARK 3 RMSD BOND DISTANCES 0.011 ANGSTROMS 1RIB 27 REMARK 3 RMSD BOND ANGLES 2.84 DEGREES 1RIB 28 REMARK 3 RMSD DIHEDRAL ANGLES 21.5 DEGREES 1RIB 29 REMARK 3 1RIB 30 REMARK 3 RESOLUTION RANGE 7.0 - 2.2 ANGSTROMS 1RIB 31 REMARK 3 DATA CUTOFF 0.0 SIGMA(F) 1RIB 32 REMARK 4 1RIB 33 REMARK 4 RESIDUES 341 - 375 ARE NOT VISIBLE IN THE ELECTRON DENSITY 1RIB 34 REMARK 4 MAP. SOME SCATTERED RESIDUAL ELECTRON DENSITY COULD 1RIB 35 REMARK 4 CORRESPOND TO THESE C-TERMINAL RESIDUES. THIS DENSITY HAS 1RIB 36 REMARK 4 BEEN MODELLED BY ABOUT 20 WATER MOLECULES. 1RIB 37 REMARK 5 1RIB 38 REMARK 5 SEQUENCE ADVISORY NOTICE: 1RIB 39 REMARK 5 DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. 1RIB 40 REMARK 5 1RIB 41 REMARK 5 SWISS-PROT ENTRY NAME: RIR2_ECOLI 1RIB 42 REMARK 5 1RIB 43 REMARK 5 SWISS-PROT RESIDUE PDB SEQRES 1RIB 44 REMARK 5 NAME NUMBER NAME CHAIN SEQ/INSERT CODE 1RIB 45 REMARK 5 GLN 7 ALA A 7 1RIB 46 REMARK 5 ASN 24 GLN A 24 1RIB 47 REMARK 5 GLN 326 ASN A 326 1RIB 48 REMARK 5 GLN 7 ALA B 7 1RIB 49 REMARK 5 ASN 24 GLN B 24 1RIB 50 REMARK 5 GLN 326 ASN B 326 1RIB 51 REMARK 5 1RIB 52 REMARK 5 THE AUTHORS ARE RE-REFINING THIS STRUCTURE WITH THE CORRECT 1RIB 53 REMARK 5 SEQUENCE AND EXPECT TO BE DEPOSITING THE REVISED ENTRY 1RIB 54 REMARK 5 SHORTLY. 1RIB 55 SEQRES 1 A 375 ALA TYR THR THR PHE SER ALA THR LYS ASN ASP GLN LEU 1RIB 56 SEQRES 2 A 375 LYS GLU PRO MET PHE PHE GLY GLN PRO VAL GLN VAL ALA 1RIB 57 SEQRES 3 A 375 ARG TYR ASP GLN GLN LYS TYR ASP ILE PHE GLU LYS LEU 1RIB 58 SEQRES 4 A 375 ILE GLU LYS GLN LEU SER PHE PHE TRP ARG PRO GLU GLU 1RIB 59 SEQRES 5 A 375 VAL ASP VAL SER ARG ASP ARG ILE ASP TYR GLN ALA LEU 1RIB 60 SEQRES 6 A 375 PRO GLU HIS GLU LYS HIS ILE PHE ILE SER ASN LEU LYS 1RIB 61 SEQRES 7 A 375 TYR GLN THR LEU LEU ASP SER ILE GLN GLY ARG SER PRO 1RIB 62 SEQRES 8 A 375 ASN VAL ALA LEU LEU PRO LEU ILE SER ILE PRO GLU LEU 1RIB 63 SEQRES 9 A 375 GLU THR TRP VAL GLU THR TRP ALA PHE SER GLU THR ILE 1RIB 64 SEQRES 10 A 375 HIS SER ARG SER TYR THR HIS ILE ILE ARG ASN ILE VAL 1RIB 65 SEQRES 11 A 375 ASN ASP PRO SER VAL VAL PHE ASP ASP ILE VAL THR ASN 1RIB 66 SEQRES 12 A 375 GLU GLN ILE GLN LYS ARG ALA GLU GLY ILE SER SER TYR 1RIB 67 SEQRES 13 A 375 TYR ASP GLU LEU ILE GLU MET THR SER TYR TRP HIS LEU 1RIB 68 SEQRES 14 A 375 LEU GLY GLU GLY THR HIS THR VAL ASN GLY LYS THR VAL 1RIB 69 SEQRES 15 A 375 THR VAL SER LEU ARG GLU LEU LYS LYS LYS LEU TYR LEU 1RIB 70 SEQRES 16 A 375 CYS LEU MET SER VAL ASN ALA LEU GLU ALA ILE ARG PHE 1RIB 71 SEQRES 17 A 375 TYR VAL SER PHE ALA CYS SER PHE ALA PHE ALA GLU ARG 1RIB 72 SEQRES 18 A 375 GLU LEU MET GLU GLY ASN ALA LYS ILE ILE ARG LEU ILE 1RIB 73 SEQRES 19 A 375 ALA ARG ASP GLU ALA LEU HIS LEU THR GLY THR GLN HIS 1RIB 74 SEQRES 20 A 375 MET LEU ASN LEU LEU ARG SER GLY ALA ASP ASP PRO GLU 1RIB 75 SEQRES 21 A 375 MET ALA GLU ILE ALA GLU GLU CYS LYS GLN GLU CYS TYR 1RIB 76 SEQRES 22 A 375 ASP LEU PHE VAL GLN ALA ALA GLN GLN GLU LYS ASP TRP 1RIB 77 SEQRES 23 A 375 ALA ASP TYR LEU PHE ARG ASP GLY SER MET ILE GLY LEU 1RIB 78 SEQRES 24 A 375 ASN LYS ASP ILE LEU CYS GLN TYR VAL GLU TYR ILE THR 1RIB 79 SEQRES 25 A 375 ASN ILE ARG MET GLN ALA VAL GLY LEU ASP LEU PRO PHE 1RIB 80 SEQRES 26 A 375 ASN THR ARG SER ASN PRO ILE PRO TRP ILE ASN THR TRP 1RIB 81 SEQRES 27 A 375 LEU VAL SER ASP ASN VAL GLN VAL ALA PRO GLN GLU VAL 1RIB 82 SEQRES 28 A 375 GLU VAL SER SER TYR LEU VAL GLY GLN ILE ASP SER GLU 1RIB 83 SEQRES 29 A 375 VAL ASP THR ASP ASP LEU SER ASN PHE GLN LEU 1RIB 84 SEQRES 1 B 375 ALA TYR THR THR PHE SER ALA THR LYS ASN ASP GLN LEU 1RIB 85 SEQRES 2 B 375 LYS GLU PRO MET PHE PHE GLY GLN PRO VAL GLN VAL ALA 1RIB 86 SEQRES 3 B 375 ARG TYR ASP GLN GLN LYS TYR ASP ILE PHE GLU LYS LEU 1RIB 87 SEQRES 4 B 375 ILE GLU LYS GLN LEU SER PHE PHE TRP ARG PRO GLU GLU 1RIB 88 SEQRES 5 B 375 VAL ASP VAL SER ARG ASP ARG ILE ASP TYR GLN ALA LEU 1RIB 89 SEQRES 6 B 375 PRO GLU HIS GLU LYS HIS ILE PHE ILE SER ASN LEU LYS 1RIB 90 SEQRES 7 B 375 TYR GLN THR LEU LEU ASP SER ILE GLN GLY ARG SER PRO 1RIB 91 SEQRES 8 B 375 ASN VAL ALA LEU LEU PRO LEU ILE SER ILE PRO GLU LEU 1RIB 92 SEQRES 9 B 375 GLU THR TRP VAL GLU THR TRP ALA PHE SER GLU THR ILE 1RIB 93 SEQRES 10 B 375 HIS SER ARG SER TYR THR HIS ILE ILE ARG ASN ILE VAL 1RIB 94 SEQRES 11 B 375 ASN ASP PRO SER VAL VAL PHE ASP ASP ILE VAL THR ASN 1RIB 95 SEQRES 12 B 375 GLU GLN ILE GLN LYS ARG ALA GLU GLY ILE SER SER TYR 1RIB 96 SEQRES 13 B 375 TYR ASP GLU LEU ILE GLU MET THR SER TYR TRP HIS LEU 1RIB 97 SEQRES 14 B 375 LEU GLY GLU GLY THR HIS THR VAL ASN GLY LYS THR VAL 1RIB 98 SEQRES 15 B 375 THR VAL SER LEU ARG GLU LEU LYS LYS LYS LEU TYR LEU 1RIB 99 SEQRES 16 B 375 CYS LEU MET SER VAL ASN ALA LEU GLU ALA ILE ARG PHE 1RIB 100 SEQRES 17 B 375 TYR VAL SER PHE ALA CYS SER PHE ALA PHE ALA GLU ARG 1RIB 101 SEQRES 18 B 375 GLU LEU MET GLU GLY ASN ALA LYS ILE ILE ARG LEU ILE 1RIB 102 SEQRES 19 B 375 ALA ARG ASP GLU ALA LEU HIS LEU THR GLY THR GLN HIS 1RIB 103 SEQRES 20 B 375 MET LEU ASN LEU LEU ARG SER GLY ALA ASP ASP PRO GLU 1RIB 104 SEQRES 21 B 375 MET ALA GLU ILE ALA GLU GLU CYS LYS GLN GLU CYS TYR 1RIB 105 SEQRES 22 B 375 ASP LEU PHE VAL GLN ALA ALA GLN GLN GLU LYS ASP TRP 1RIB 106 SEQRES 23 B 375 ALA ASP TYR LEU PHE ARG ASP GLY SER MET ILE GLY LEU 1RIB 107 SEQRES 24 B 375 ASN LYS ASP ILE LEU CYS GLN TYR VAL GLU TYR ILE THR 1RIB 108 SEQRES 25 B 375 ASN ILE ARG MET GLN ALA VAL GLY LEU ASP LEU PRO PHE 1RIB 109 SEQRES 26 B 375 ASN THR ARG SER ASN PRO ILE PRO TRP ILE ASN THR TRP 1RIB 110 SEQRES 27 B 375 LEU VAL SER ASP ASN VAL GLN VAL ALA PRO GLN GLU VAL 1RIB 111 SEQRES 28 B 375 GLU VAL SER SER TYR LEU VAL GLY GLN ILE ASP SER GLU 1RIB 112 SEQRES 29 B 375 VAL ASP THR ASP ASP LEU SER ASN PHE GLN LEU 1RIB 113 FTNOTE 1 1RIB 114 FTNOTE 1 ASN B 131 - ASP B 132 OMEGA =149.75 1RIB 115 FTNOTE 1 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 1RIB 116 HET FEO 401 3 MU-OXO-DIIRON 1RIB 117 HET FEO 402 3 MU-OXO-DIIRON 1RIB 118 FORMUL 3 FEO 2(O1 FE2) 1RIB 119 FORMUL 4 HOH *325(H2 O1) 1RIB 120 CRYST1 74.300 85.500 115.700 90.00 90.00 90.00 P 21 21 21 8 1RIB 121 ORIGX1 1.000000 0.000000 0.000000 0.00000 1RIB 122 ORIGX2 0.000000 1.000000 0.000000 0.00000 1RIB 123 ORIGX3 0.000000 0.000000 1.000000 0.00000 1RIB 124 SCALE1 0.013459 0.000000 0.000000 0.00000 1RIB 125 SCALE2 0.000000 0.011696 0.000000 0.00000 1RIB 126 SCALE3 0.000000 0.000000 0.008643 0.00000 1RIB 127