HEADER CALCIUM-BINDING PROTEIN 02-AUG-95 1CFC 1CFC 2 TITLE CALCIUM-FREE CALMODULIN 1CFC 3 COMPND MOL_ID: 1; 1CFC 4 COMPND 2 MOLECULE: CALMODULIN; 1CFC 5 COMPND 3 CHAIN: NULL 1CFC 6 SOURCE MOL_ID: 1; 1CFC 7 SOURCE 2 ORGANISM_SCIENTIFIC: XENOPUS LAEVIS; 1CFC 8 SOURCE 3 ORGANISM_COMMON: AFRICAN FROG 1CFC 9 EXPDTA NMR, 25 STRUCTURES 1CFC 10 AUTHOR H.KUBONIWA,N.TJANDRA,S.GRZESIEK,H.REN,C.B.KLEE,A.BAX 1CFC 11 REVDAT 1 07-DEC-95 1CFC 0 1CFC 12 JRNL AUTH H.KUBONIWA,N.TJANDRA,S.GRZESIEK,H.REN,C.B.KLEE, 1CFC 13 JRNL AUTH 2 A.BAX 1CFC 14 JRNL TITL SOLUTION STRUCTURE OF CALCIUM-FREE CALMODULIN 1CFC 15 JRNL REF NAT.STRUCT.BIOL. V. 2 768 1995 1CFC 16 JRNL REFN ASTM NSBIEW US ISSN 1072-8368 2024 1CFC 17 REMARK 1 1CFC 18 REMARK 2 1CFC 19 REMARK 2 RESOLUTION. NOT APPLICABLE. SEE REMARK 4. 1CFC 20 REMARK 3 1CFC 21 REMARK 3 REFINEMENT. 1CFC 22 REMARK 4 1CFC 23 REMARK 4 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION 1CFC 24 REMARK 4 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT 1CFC 25 REMARK 4 *CRYST1* AND *SCALE* RECORDS BE INCLUDED, BUT THE VALUES ON 1CFC 26 REMARK 4 THESE RECORDS ARE MEANINGLESS. 1CFC 27 REMARK 5 1CFC 28 REMARK 5 THE 3D SOLUTION STRUCTURE OF XENOPUS APO-CALMODULIN SOLVED 1CFC 29 REMARK 5 BY MULTI-DIMENSIONAL HETERONUCLEAR-EDITED AND -FILTERED NMR 1CFC 30 REMARK 5 IS BASED ON 1855 EXPERIMENTAL DISTANCE CONSTRAINTS, 1CFC 31 REMARK 5 INCLUDING 383 INTRARESIDUE ROES, 158 INTRARESIDUE NOES, 392 1CFC 32 REMARK 5 SEQUENTIAL ROES, 68 SEQUENTIAL NOES, 355 MEDIUM RANGE NOES 1CFC 33 REMARK 5 AND ROES, 443 LONG RANGE NOES AND ROES, AND 45 HYDROGEN 1CFC 34 REMARK 5 BONDS. A TOTAL OF 400 ANGULAR CONSTRAINTS WAS DERIVED FROM 1CFC 35 REMARK 5 MEASUREMENT OF OVER 700 HOMO- AND HETERONUCLEAR J 1CFC 36 REMARK 5 COUPLINGS. A COMPLETE LIST OF EXPERIMENTAL CONSTRAINTS HAS 1CFC 37 REMARK 5 BEEN DEPOSITED WITH THE PROTEIN DATA BANK. 1CFC 38 REMARK 6 1CFC 39 REMARK 6 THE STRUCTURES WERE CALCULATED USING THE SIMULATED 1CFC 40 REMARK 6 ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 1CFC 41 REMARK 6 229, 129-136 USING THE PROGRAM X-PLOR 3.1 (BRUNGER). 1CFC 42 REMARK 7 1CFC 43 REMARK 7 THE FIRST MODEL IN THIS ENTRY IS THE CLOSEST TO THE MEAN 1CFC 44 REMARK 7 STRUCTURE (PDB ENTRY 1CFD) FOR A SET COMPRISING THE 25 1CFC 45 REMARK 7 LOWEST ENERGY STRUCTURES OUT OF A SET OF 80 CALCULATED 1CFC 46 REMARK 7 STRUCTURES. THE ORIENTATION OF THE N-TERMINAL DOMAIN 1CFC 47 REMARK 7 RELATIVE TO THE C-TERMINAL DOMAIN IS ILL-DEFINED AND, 1CFC 48 REMARK 7 THEREFORE, THE MEAN STRUCTURE IS CALCULATED SEPARATELY FOR 1CFC 49 REMARK 7 THE N-TERMINAL DOMAIN (RESIDUES 1 - 76) AND THE C-TERMINAL 1CFC 50 REMARK 7 DOMAIN (RESIDUES 77 - 148) FROM A BEST FIT SUPERPOSITION OF 1CFC 51 REMARK 7 RESIDUES 5 - 75 AND 82 - 146. THE 25 LOWEST ENERGY 1CFC 52 REMARK 7 STRUCTURES OF THE N-TERMINAL DOMAIN WERE COMBINED WITH 1CFC 53 REMARK 7 THE 25 LOWEST ENERGY STRUCTURES OF THE C-TERMINAL DOMAIN, 1CFC 54 REMARK 7 ALLOWING THE PHI AND PSI ANGLES OF RESIDUES 76 AND 77 TO 1CFC 55 REMARK 7 VARY IN ORDER TO AVOID STERIC CLASHES. THE NUMBERS IN THE 1CFC 56 REMARK 7 B-VALUE FIELD OF THE 25 INDIVIDUAL SIMULATED ANNEALING 1CFC 57 REMARK 7 STRUCTURES (MODELS 1 - 25) REPRESENT THE ATOMIC 1CFC 58 REMARK 7 DISPLACEMENT RELATIVE TO THE AVERAGE STRUCTURE OF THE 1CFC 59 REMARK 7 INDIVIDUAL DOMAINS. 1CFC 60 REMARK 8 1CFC 61 REMARK 8 ORIGINAL DEPOSITION REVISED PRIOR TO RELEASE 1CFC 62 REMARK 8 TRACKING NUMBER: T6844, DATE REVISED: 18-OCT-95 1CFC 63 REMARK 999 1CFC 64 REMARK 999 THE SEQUENCE IS IDENTICAL TO BOVINE CALMODULIN (M.S. 1CFC 65 REMARK 999 LIVINGSTON ET AL., CELL, VOL 37, 205-215, 1986). THE 1CFC 66 REMARK 999 PROTEIN USED IN THE EXPERIMENT WAS DERIVED FROM E. COLI 1CFC 67 REMARK 999 EXPRESSION AND LACKS THE POST-TRANSLATIONAL MODIFICATIONS 1CFC 68 REMARK 999 NATURALLY PRESENT AT THE N-TERMINUS AND AT LYS 115. 1CFC 69 DBREF 1CFC 1 148 SWS P02593 CALM_HUMAN 1 148 1CFC 70 SEQRES 1 148 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS 1CFC 71 SEQRES 2 148 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR 1CFC 72 SEQRES 3 148 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU 1CFC 73 SEQRES 4 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE 1CFC 74 SEQRES 5 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE 1CFC 75 SEQRES 6 148 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP 1CFC 76 SEQRES 7 148 THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL 1CFC 77 SEQRES 8 148 PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU 1CFC 78 SEQRES 9 148 LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR 1CFC 79 SEQRES 10 148 ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE 1CFC 80 SEQRES 11 148 ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN 1CFC 81 SEQRES 12 148 MET MET THR ALA LYS 1CFC 82 HELIX 1 1 GLU 6 PHE 19 1 1CFC 83 HELIX 2 2 THR 29 SER 38 5 1CFC 84 HELIX 3 3 GLU 45 VAL 55 1 1CFC 85 HELIX 4 4 PHE 65 LYS 75 1 1CFC 86 HELIX 5 5 GLU 82 VAL 91 1 1CFC 87 HELIX 6 6 ALA 102 ASN 111 1 1CFC 88 HELIX 7 7 ASP 118 GLU 127 1 1CFC 89 HELIX 8 8 GLU 139 THR 146 1 1CFC 90 SHEET 1 A 2 THR 26 THR 28 0 1CFC 91 SHEET 2 A 2 THR 62 ASP 64 -1 N ILE 63 O ILE 27 1CFC 92 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 1CFC 93 ORIGX1 1.000000 0.000000 0.000000 0.00000 1CFC 94 ORIGX2 0.000000 1.000000 0.000000 0.00000 1CFC 95 ORIGX3 0.000000 0.000000 1.000000 0.00000 1CFC 96 SCALE1 1.000000 0.000000 0.000000 0.00000 1CFC 97 SCALE2 0.000000 1.000000 0.000000 0.00000 1CFC 98 SCALE3 0.000000 0.000000 1.000000 0.00000 1CFC 99 MODEL 1 1CFC 100 (ATOM LINES ARE NOT SHOWN.) END