HEADER CALCIUM-BINDING PROTEIN 18-OCT-95 1CFD 1CFD 2 TITLE CALCIUM-FREE CALMODULIN 1CFD 3 COMPND MOL_ID: 1; 1CFD 4 COMPND 2 MOLECULE: CALMODULIN; 1CFD 5 COMPND 3 CHAIN: NULL 1CFD 6 SOURCE MOL_ID: 1; 1CFD 7 SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS; 1CFD 8 SOURCE 3 ORGANISM_COMMON: AFRICAN FROG 1CFD 9 EXPDTA NMR, MINIMIZED AVERAGE STRUCTURE 1CFD 10 AUTHOR H.KUBONIWA,N.TJANDRA,S.GRZESIEK,H.REN,C.B.KLEE,A.BAX 1CFD 11 REVDAT 1 07-DEC-95 1CFD 0 1CFD 12 JRNL AUTH H.KUBONIWA,N.TJANDRA,S.GRZESIEK,H.REN,C.B.KLEE, 1CFD 13 JRNL AUTH 2 A.BAX 1CFD 14 JRNL TITL SOLUTION STRUCTURE OF CALCIUM-FREE CALMODULIN 1CFD 15 JRNL REF NAT.STRUCT.BIOL. V. 2 768 1995 1CFD 16 JRNL REFN ASTM NSBIEW US ISSN 1072-8368 2024 1CFD 17 REMARK 1 1CFD 18 REMARK 2 1CFD 19 REMARK 2 RESOLUTION. NOT APPLICABLE. SEE REMARK 4. 1CFD 20 REMARK 3 1CFD 21 REMARK 3 REFINEMENT. 1CFD 22 REMARK 4 1CFD 23 REMARK 4 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION 1CFD 24 REMARK 4 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT 1CFD 25 REMARK 4 *CRYST1* AND *SCALE* RECORDS BE INCLUDED, BUT THE VALUES ON 1CFD 26 REMARK 4 THESE RECORDS ARE MEANINGLESS. 1CFD 27 REMARK 5 1CFD 28 REMARK 5 THE 3D SOLUTION STRUCTURE OF XENOPUS APO-CALMODULIN SOLVED 1CFD 29 REMARK 5 BY MULTI-DIMENSIONAL HETERONUCLEAR-EDITED AND -FILTERED NMR 1CFD 30 REMARK 5 IS BASED ON 1855 EXPERIMENTAL DISTANCE CONSTRAINTS, 1CFD 31 REMARK 5 INCLUDING 383 INTRARESIDUE ROES, 158 INTRARESIDUE NOES, 392 1CFD 32 REMARK 5 SEQUENTIAL ROES, 68 SEQUENTIAL NOES, 355 MEDIUM RANGE NOES 1CFD 33 REMARK 5 AND ROES, 443 LONG RANGE NOES AND ROES, AND 45 HYDROGEN 1CFD 34 REMARK 5 BONDS. A TOTAL OF 400 ANGULAR CONSTRAINTS WAS DERIVED FROM 1CFD 35 REMARK 5 MEASUREMENT OF OVER 700 HOMO- AND HETERONUCLEAR J 1CFD 36 REMARK 5 COUPLINGS. A COMPLETE LIST OF EXPERIMENTAL CONSTRAINTS HAS 1CFD 37 REMARK 5 BEEN DEPOSITED WITH THE PROTEIN DATA BANK. 1CFD 38 REMARK 6 1CFD 39 REMARK 6 THE STRUCTURES WERE CALCULATED USING THE SIMULATED 1CFD 40 REMARK 6 ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 1CFD 41 REMARK 6 229, 129-136 USING THE PROGRAM X-PLOR 3.1 (BRUNGER). 1CFD 42 REMARK 7 1CFD 43 REMARK 7 ENERGY-MINIMIZED MEAN STRUCTURE CALCULATED FROM A SET 1CFD 44 REMARK 7 COMPRISING THE 25 LOWEST ENERGY STRUCTURES (ENTRY 1CFC) OUT 1CFD 45 REMARK 7 OF A SET OF 80 CA STRUCTURES. THE REPORTED RMSD (THE B 1CFD 46 REMARK 7 VALUE FIELD IN X-RAY STRUCTURES) GIVES THE RMS DIFFERENCE 1CFD 47 REMARK 7 IN COORDINATES BETWEEN THE 25 INDIVIDUAL STRUCTURES AND 1CFD 48 REMARK 7 THEIR MEAN STRUCTURE. THE ORIENTATION OF THE N-TERMINAL 1CFD 49 REMARK 7 DOMAIN RELATIVE TO THE C-TERMINAL DOMAIN IS ILL-DEFINED 1CFD 50 REMARK 7 AND, THEREFORE, THE MEAN STRUCTURE IS CALCULATED SEPARATELY 1CFD 51 REMARK 7 FOR THE N-TERMINAL DOMAIN (RESIDUES 1 - 76) AND THE 1CFD 52 REMARK 7 C-TERMINAL DOMAIN (RESIDUES 77 - 148) FROM A BEST FIT 1CFD 53 REMARK 7 SUPERPOSITION OF RESIDUES 5 - 75 AND 82 - 146. THE 25 1CFD 54 REMARK 7 LOWEST ENERGY STRUCTURES OF THE N-TERMINAL DOMAIN WERE 1CFD 55 REMARK 7 COMBINED WITH THE 25 LOWEST ENERGY STRUCTURES OF THE 1CFD 56 REMARK 7 C-TERMINAL DOMAIN, ALLOWING THE PHI AND PSI ANGLES OF 1CFD 57 REMARK 7 RESIDUES 76 AND 77 TO VARY IN ORDER TO AVOID STERIC 1CFD 58 REMARK 7 CLASHES. THE NUMBERS IN THE B-VALUE FIELD OF THE OTHER 24 1CFD 59 REMARK 7 INDIVIDUAL SIMULATED ANNEALING STRUCTURES (MODELS 2 - 25 OF 1CFD 60 REMARK 7 ENTRY 1CFC) REPRESENT THE ATOMIC DISPLACEMENT RELATIVE TO 1CFD 61 REMARK 7 THE AVERAGE STRUCTURE OF THE INDIVIDUAL DOMAINS. 1CFD 62 REMARK 999 1CFD 63 REMARK 999 THE SEQUENCE IS IDENTICAL TO BOVINE CALMODULIN (M.S. 1CFD 64 REMARK 999 LIVINGSTON ET AL., CELL, VOL 37, 205-215, 1986). THE 1CFD 65 REMARK 999 PROTEIN USED IN THE EXPERIMENT WAS DERIVED FROM E. COLI 1CFD 66 REMARK 999 EXPRESSION AND LACKS THE POST-TRANSLATIONAL MODIFICATIONS 1CFD 67 REMARK 999 NATURALLY PRESENT AT THE N-TERMINUS AND AT LYS 115. 1CFD 68 DBREF 1CFD 1 148 SWS P02593 CALM_HUMAN 1 148 1CFD 69 SEQRES 1 148 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS 1CFD 70 SEQRES 2 148 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR 1CFD 71 SEQRES 3 148 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU 1CFD 72 SEQRES 4 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE 1CFD 73 SEQRES 5 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE 1CFD 74 SEQRES 6 148 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP 1CFD 75 SEQRES 7 148 THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL 1CFD 76 SEQRES 8 148 PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU 1CFD 77 SEQRES 9 148 LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR 1CFD 78 SEQRES 10 148 ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE 1CFD 79 SEQRES 11 148 ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN 1CFD 80 SEQRES 12 148 MET MET THR ALA LYS 1CFD 81 HELIX 1 1 GLU 6 PHE 19 1 1CFD 82 HELIX 2 2 THR 29 LEU 39 1 1CFD 83 HELIX 3 3 GLU 45 ALA 57 1 1CFD 84 HELIX 4 4 PHE 65 LYS 75 1 1CFD 85 HELIX 5 5 GLU 82 PHE 92 1 1CFD 86 HELIX 6 6 ALA 102 ASN 111 1 1CFD 87 HELIX 7 7 ASP 118 GLU 127 1 1CFD 88 HELIX 8 8 GLU 139 THR 146 1 1CFD 89 SHEET 1 A 2 THR 26 THR 28 0 1CFD 90 SHEET 2 A 2 THR 62 ASP 64 -1 N ILE 63 O ILE 27 1CFD 91 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 1CFD 92 ORIGX1 1.000000 0.000000 0.000000 0.00000 1CFD 93 ORIGX2 0.000000 1.000000 0.000000 0.00000 1CFD 94 ORIGX3 0.000000 0.000000 1.000000 0.00000 1CFD 95 SCALE1 1.000000 0.000000 0.000000 0.00000 1CFD 96 SCALE2 0.000000 1.000000 0.000000 0.00000 1CFD 97 SCALE3 0.000000 0.000000 1.000000 0.00000 1CFD 98 (ATOM LINES ARE NOT SHOWN.) END