HEADER CALCIUM-BINDING PROTEIN 16-JUL-92 2BBN 2BBN 2 COMPND CALMODULIN (CALCIUM-BOUND) COMPLEXED WITH RABBIT SKELETAL 2BBN 3 COMPND 2 MYOSIN LIGHT CHAIN KINASE (CALMODULIN-BINDING DOMAIN) 2BBN 4 COMPND 3 (NMR, 21 STRUCTURES) 2BBN 5 SOURCE CALMODULIN: (DROSOPHILA MELANOGASTER); PEPTIDE: SYNTHETIC 2BBN 6 EXPDTA NMR 2BBN 7 AUTHOR G.M.CLORE,A.BAX,M.IKURA,A.M.GRONENBORN 2BBN 8 REVDAT 1 31-JAN-94 2BBN 0 2BBN 9 JRNL AUTH M.IKURA,G.M.CLORE,A.M.GRONENBORN,G.ZHU,C.B.KLEE, 2BBN 10 JRNL AUTH 2 A.BAX 2BBN 11 JRNL TITL SOLUTION STRUCTURE OF A CALMODULIN-*TARGET PEPTIDE 2BBN 12 JRNL TITL 2 COMPLEX BY MULTIDIMENSIONAL /NMR$ 2BBN 13 JRNL REF SCIENCE V. 256 632 1992 2BBN 14 JRNL REFN ASTM SCIEAS US ISSN 0036-8075 038 2BBN 15 REMARK 1 2BBN 16 REMARK 2 2BBN 17 REMARK 2 RESOLUTION. NOT APPLICABLE. SEE REMARK 4. 2BBN 18 REMARK 3 2BBN 19 REMARK 3 REFINEMENT. NONE. 2BBN 20 REMARK 4 2BBN 21 REMARK 4 THESE COORDINATES WERE GENERATED FROM SOLUTION NMR DATA. 2BBN 22 REMARK 4 PROTEIN DATA BANK CONVENTIONS REQUIRE THAT *CRYST1* AND 2BBN 23 REMARK 4 *SCALE* RECORDS BE INCLUDED, BUT THE VALUES ON THESE 2BBN 24 REMARK 4 RECORDS ARE MEANINGLESS. 2BBN 25 REMARK 5 2BBN 26 REMARK 5 DETAILS OF THE STRUCTURE DETERMINATION AND ALL STRUCTURAL 2BBN 27 REMARK 5 STATISTICS ARE GIVEN IN THE PAPER CITED ON *JRNL* RECORDS 2BBN 28 REMARK 5 ABOVE (I.E. AGREEMENT WITH EXPERIMENTAL RESTRAINTS, 2BBN 29 REMARK 5 DEVIATIONS FROM IDEALITY FOR BOND LENGTHS, ANGLES, PLANES 2BBN 30 REMARK 5 AND CHIRALITY, NON-BONDED CONTACTS, ATOMIC RMS DIFFERENCES 2BBN 31 REMARK 5 BETWEEN THE CALCULATED STRUCTURES). 2BBN 32 REMARK 5 2BBN 33 REMARK 5 THE STRUCTURES ARE BASED ON 1827 INTERPROTON DISTANCE 2BBN 34 REMARK 5 RESTRAINTS DERIVED FROM NOE MEASUREMENTS; 148 2BBN 35 REMARK 5 HYDROGEN-BONDING DISTANCE RESTRAINTS FOR 74 HYDROGEN-BONDS 2BBN 36 REMARK 5 IDENTIFIED ON THE BASIS OF THE NOE AND AMIDE PROTON 2BBN 37 REMARK 5 EXCHANGE DATA, AS WELL AS THE INITIAL STRUCTURE 2BBN 38 REMARK 5 CALCULATIONS; 24 RESTRAINTS FOR THE 4 CALCIUM IONS, 2BBN 39 REMARK 5 AND 113 PHI TORSION ANGLE RESTRAINTS DERIVED FROM COUPLING 2BBN 40 REMARK 5 DATA, CONSTANTS, NOE AND 13C SECONDARY CHEMICAL SHIFTS. 2BBN 41 REMARK 5 2BBN 42 REMARK 5 THE METHOD USED TO DETERMINE THE STRUCTURES IS THE HYBRID 2BBN 43 REMARK 5 METRIC MATRIX DISTANCE GEOMETRY-DYNAMICAL SIMULATED 2BBN 44 REMARK 5 ANNEALING METHOD [M.NILGES, G.M.CLORE, AND A.M.GRONENBORN, 2BBN 45 REMARK 5 FEBS LETT. 229, 317-324 (1988)]. 2BBN 46 REMARK 6 2BBN 47 REMARK 6 A TOTAL OF 21 STRUCTURES WERE CALCULATED. 2BBN 48 REMARK 6 THE COORDINATES OF THE RESTRAINED MINIMIZED STRUCTURE ARE 2BBN 49 REMARK 6 PRESENTED IN PROTEIN DATA BANK ENTRY 2BBM. THIS WAS 2BBN 50 REMARK 6 GENERATED BY AVERAGING THE COORDINATES OF THE INDIVIDUAL 2BBN 51 REMARK 6 STRUCTURES AND SUBJECTING THE RESULTING COORDINATES TO 2BBN 52 REMARK 6 RESTRAINED MINIMIZATION. THE COORDINATES OF THE 21 2BBN 53 REMARK 6 INDIVIDUAL SA STRUCTURES FOLLOW AND ARE PRESENTED AS MODELS 2BBN 54 REMARK 6 1 TO 21. 2BBN 55 REMARK 7 2BBN 56 REMARK 7 THE QUANTITY PRESENTED IN THE B VALUE FIELD OF ATOM AND 2BBN 57 REMARK 7 HETATM RECORDS BELOW HAS NO MEANING. 2BBN 58 REMARK 8 2BBN 59 REMARK 8 RESIDUES 1 - 5, 74 - 82 AND 147 - 148 OF CALMODULIN, AND 2BBN 60 REMARK 8 RESIDUES 1 - 2 AND 22 - 26 OF THE PEPTIDE ARE DISORDERED. 2BBN 61 SEQRES 1 A 148 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS 2BBN 62 SEQRES 2 A 148 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR 2BBN 63 SEQRES 3 A 148 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU 2BBN 64 SEQRES 4 A 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE 2BBN 65 SEQRES 5 A 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE 2BBN 66 SEQRES 6 A 148 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP 2BBN 67 SEQRES 7 A 148 THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL 2BBN 68 SEQRES 8 A 148 PHE ASP LYS ASP GLY ASN GLY PHE ILE SER ALA ALA GLU 2BBN 69 SEQRES 9 A 148 LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR 2BBN 70 SEQRES 10 A 148 ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE 2BBN 71 SEQRES 11 A 148 ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL THR 2BBN 72 SEQRES 12 A 148 MET MET THR SER LYS 2BBN 73 SEQRES 1 B 26 LYS ARG ARG TRP LYS LYS ASN PHE ILE ALA VAL SER ALA 2BBN 74 SEQRES 2 B 26 ALA ASN ARG PHE LYS LYS ILE SER SER SER GLY ALA LEU 2BBN 75 HET CA A 181 1 CALCIUM ++ ION 2BBN 76 HET CA A 182 1 CALCIUM ++ ION 2BBN 77 HET CA A 183 1 CALCIUM ++ ION 2BBN 78 HET CA A 184 1 CALCIUM ++ ION 2BBN 79 FORMUL 3 CA 4(CA1 ++) 2BBN 80 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 2BBN 81 ORIGX1 1.000000 0.000000 0.000000 0.00000 2BBN 82 ORIGX2 0.000000 1.000000 0.000000 0.00000 2BBN 83 ORIGX3 0.000000 0.000000 1.000000 0.00000 2BBN 84 SCALE1 1.000000 0.000000 0.000000 0.00000 2BBN 85 SCALE2 0.000000 1.000000 0.000000 0.00000 2BBN 86 SCALE3 0.000000 0.000000 1.000000 0.00000 2BBN 87 MODEL 1 (ATOM LINES ARE NOT SHOWN.) END