HEADER CALCIUM-BINDING PROTEIN 16-JUL-92 2BBM 2BBM 2 COMPND CALMODULIN (CALCIUM-BOUND) COMPLEXED WITH RABBIT SKELETAL 2BBM 3 COMPND 2 MYOSIN LIGHT CHAIN KINASE (CALMODULIN-BINDING DOMAIN) 2BBM 4 COMPND 3 (NMR, MINIMIZED AVERAGE STRUCTURE) 2BBM 5 SOURCE CALMODULIN: (DROSOPHILA MELANOGASTER); PEPTIDE: SYNTHETIC 2BBM 6 EXPDTA NMR 2BBM 7 AUTHOR G.M.CLORE,A.BAX,M.IKURA,A.M.GRONENBORN 2BBM 8 REVDAT 1 31-JAN-94 2BBM 0 2BBM 9 JRNL AUTH M.IKURA,G.M.CLORE,A.M.GRONENBORN,G.ZHU,C.B.KLEE, 2BBM 10 JRNL AUTH 2 A.BAX 2BBM 11 JRNL TITL SOLUTION STRUCTURE OF A CALMODULIN-*TARGET PEPTIDE 2BBM 12 JRNL TITL 2 COMPLEX BY MULTIDIMENSIONAL /NMR$ 2BBM 13 JRNL REF SCIENCE V. 256 632 1992 2BBM 14 JRNL REFN ASTM SCIEAS US ISSN 0036-8075 038 2BBM 15 REMARK 1 2BBM 16 REMARK 2 2BBM 17 REMARK 2 RESOLUTION. NOT APPLICABLE. SEE REMARK 4. 2BBM 18 REMARK 3 2BBM 19 REMARK 3 REFINEMENT. NONE. 2BBM 20 REMARK 4 2BBM 21 REMARK 4 THESE COORDINATES WERE GENERATED FROM SOLUTION NMR DATA. 2BBM 22 REMARK 4 PROTEIN DATA BANK CONVENTIONS REQUIRE THAT *CRYST1* AND 2BBM 23 REMARK 4 *SCALE* RECORDS BE INCLUDED, BUT THE VALUES ON THESE 2BBM 24 REMARK 4 RECORDS ARE MEANINGLESS. 2BBM 25 REMARK 5 2BBM 26 REMARK 5 DETAILS OF THE STRUCTURE DETERMINATION AND ALL STRUCTURAL 2BBM 27 REMARK 5 STATISTICS ARE GIVEN IN THE PAPER CITED ON *JRNL* RECORDS 2BBM 28 REMARK 5 ABOVE (I.E. AGREEMENT WITH EXPERIMENTAL RESTRAINTS, 2BBM 29 REMARK 5 DEVIATIONS FROM IDEALITY FOR BOND LENGTHS, ANGLES, PLANES 2BBM 30 REMARK 5 AND CHIRALITY, NON-BONDED CONTACTS, ATOMIC RMS DIFFERENCES 2BBM 31 REMARK 5 BETWEEN THE CALCULATED STRUCTURES). 2BBM 32 REMARK 5 2BBM 33 REMARK 5 THE STRUCTURES ARE BASED ON 1827 INTERPROTON DISTANCE 2BBM 34 REMARK 5 RESTRAINTS DERIVED FROM NOE MEASUREMENTS; 148 2BBM 35 REMARK 5 HYDROGEN-BONDING DISTANCE RESTRAINTS FOR 74 HYDROGEN-BONDS 2BBM 36 REMARK 5 IDENTIFIED ON THE BASIS OF THE NOE AND AMIDE PROTON 2BBM 37 REMARK 5 EXCHANGE DATA, AS WELL AS THE INITIAL STRUCTURE 2BBM 38 REMARK 5 CALCULATIONS; 24 RESTRAINTS FOR THE 4 CALCIUM IONS, 2BBM 39 REMARK 5 AND 113 PHI TORSION ANGLE RESTRAINTS DERIVED FROM COUPLING 2BBM 40 REMARK 5 DATA, CONSTANTS, NOE AND 13C SECONDARY CHEMICAL SHIFTS. 2BBM 41 REMARK 5 2BBM 42 REMARK 5 THE METHOD USED TO DETERMINE THE STRUCTURES IS THE HYBRID 2BBM 43 REMARK 5 METRIC MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED 2BBM 44 REMARK 5 ANNEALING METHOD [M.NILGES, G.M.CLORE, AND A.M.GRONENBORN, 2BBM 45 REMARK 5 FEBS LETT. 229, 317-324 (1988)]. 2BBM 46 REMARK 6 2BBM 47 REMARK 6 A TOTAL OF 21 STRUCTURES WERE CALCULATED. 2BBM 48 REMARK 6 THE COORDINATES OF THE RESTRAINED MINIMIZED STRUCTURE ARE 2BBM 49 REMARK 6 PRESENTED IN THIS ENTRY. THIS WAS OBTAINED BY AVERAGING 2BBM 50 REMARK 6 THE COORDINATES OF THE INDIVIDUAL STRUCTURES AND SUBJECTING 2BBM 51 REMARK 6 THE RESULTING COORDINATES TO RESTRAINED MINIMIZATION. THE 2BBM 52 REMARK 6 COORDINATES OF THE 21 INDIVIDUAL SA STRUCTURES ARE 2BBM 53 REMARK 6 PRESENTED IN PROTEIN DATA BANK ENTRY 2BBN. 2BBM 54 REMARK 7 2BBM 55 REMARK 7 THE LAST COLUMN IN THIS COORDINATE FILE REPRESENTS THE 2BBM 56 REMARK 7 ATOMIC RMS DEVIATION OF THE INDIVIDUAL STRUCTURES ABOUT THE 2BBM 57 REMARK 7 MEAN COORDINATE POSITIONS. 2BBM 58 REMARK 8 2BBM 59 REMARK 8 RESIDUES 1 - 5, 74 - 82 AND 147 - 148 OF CALMODULIN, AND 2BBM 60 REMARK 8 RESIDUES 1 - 2 AND 22 - 26 OF THE PEPTIDE ARE DISORDERED 2BBM 61 SEQRES 1 A 148 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS 2BBM 62 SEQRES 2 A 148 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR 2BBM 63 SEQRES 3 A 148 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU 2BBM 64 SEQRES 4 A 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE 2BBM 65 SEQRES 5 A 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE 2BBM 66 SEQRES 6 A 148 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP 2BBM 67 SEQRES 7 A 148 THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL 2BBM 68 SEQRES 8 A 148 PHE ASP LYS ASP GLY ASN GLY PHE ILE SER ALA ALA GLU 2BBM 69 SEQRES 9 A 148 LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR 2BBM 70 SEQRES 10 A 148 ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE 2BBM 71 SEQRES 11 A 148 ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL THR 2BBM 72 SEQRES 12 A 148 MET MET THR SER LYS 2BBM 73 SEQRES 1 B 26 LYS ARG ARG TRP LYS LYS ASN PHE ILE ALA VAL SER ALA 2BBM 74 SEQRES 2 B 26 ALA ASN ARG PHE LYS LYS ILE SER SER SER GLY ALA LEU 2BBM 75 HET CA A 181 1 CALCIUM ++ ION 2BBM 76 HET CA A 182 1 CALCIUM ++ ION 2BBM 77 HET CA A 183 1 CALCIUM ++ ION 2BBM 78 HET CA A 184 1 CALCIUM ++ ION 2BBM 79 FORMUL 3 CA 4(CA1 ++) 2BBM 80 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 2BBM 81 ORIGX1 1.000000 0.000000 0.000000 0.00000 2BBM 82 ORIGX2 0.000000 1.000000 0.000000 0.00000 2BBM 83 ORIGX3 0.000000 0.000000 1.000000 0.00000 2BBM 84 SCALE1 1.000000 0.000000 0.000000 0.00000 2BBM 85 SCALE2 0.000000 1.000000 0.000000 0.00000 2BBM 86 SCALE3 0.000000 0.000000 1.000000 0.00000 2BBM 87 (ATOM LINES ARE NOT SHOWN.) END