HEADER BINDING PROTEIN 22-AUG-91 2SCP COMPND SARCOPLASMIC CALCIUM-BINDING PROTEIN SOURCE SANDWORM (NEREIS DIVERSICOLOR) AUTHOR W.J.COOK,S.VIJAY-KUMAR REVDAT 1 31-OCT-93 2SCP 0 JRNL AUTH S.VIJAY-KUMAR,W.J.COOK JRNL TITL STRUCTURE OF A SARCOPLASMIC CALCIUM-BINDING JRNL TITL 2 PROTEIN FROM NEREIS DIVERSICOLOR REFINED AT 2.0 JRNL TITL 3 ANGSTROMS RESOLUTION JRNL REF J.MOL.BIOL. V. 224 413 1992 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 2.0 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM PROLSQ REMARK 3 AUTHORS KONNERT,HENDRICKSON REMARK 3 R VALUE 0.180 REMARK 3 RMSD BOND DISTANCES 0.015 ANGSTROMS REMARK 3 RMSD BOND ANGLES 1.40 DEGREES REMARK 4 REMARK 4 IN THE SITE IDENTIFIERS, EF REFERS TO EF-HAND, A COMMON REMARK 4 CA-BINDING MOTIF. SITES *EF1* - *EF6* ARE PRESENTED ON REMARK 4 *SITE* RECORDS BELOW. SEQRES 1 A 174 SER ASP LEU TRP VAL GLN LYS MET LYS THR TYR PHE ASN SEQRES 2 A 174 ARG ILE ASP PHE ASP LYS ASP GLY ALA ILE THR ARG MET SEQRES 3 A 174 ASP PHE GLU SER MET ALA GLU ARG PHE ALA LYS GLU SER SEQRES 4 A 174 GLU MET LYS ALA GLU HIS ALA LYS VAL LEU MET ASP SER SEQRES 5 A 174 LEU THR GLY VAL TRP ASP ASN PHE LEU THR ALA VAL ALA SEQRES 6 A 174 GLY GLY LYS GLY ILE ASP GLU THR THR PHE ILE ASN SER SEQRES 7 A 174 MET LYS GLU MET VAL LYS ASN PRO GLU ALA LYS SER VAL SEQRES 8 A 174 VAL GLU GLY PRO LEU PRO LEU PHE PHE ARG ALA VAL ASP SEQRES 9 A 174 THR ASN GLU ASP ASN ASN ILE SER ARG ASP GLU TYR GLY SEQRES 10 A 174 ILE PHE PHE GLY MET LEU GLY LEU ASP LYS THR MET ALA SEQRES 11 A 174 PRO ALA SER PHE ASP ALA ILE ASP THR ASN ASN ASP GLY SEQRES 12 A 174 LEU LEU SER LEU GLU GLU PHE VAL ILE ALA GLY SER ASP SEQRES 13 A 174 PHE PHE MET ASN ASP GLY ASP SER THR ASN LYS VAL PHE SEQRES 14 A 174 TRP GLY PRO LEU VAL SEQRES 1 B 174 SER ASP LEU TRP VAL GLN LYS MET LYS THR TYR PHE ASN SEQRES 2 B 174 ARG ILE ASP PHE ASP LYS ASP GLY ALA ILE THR ARG MET SEQRES 3 B 174 ASP PHE GLU SER MET ALA GLU ARG PHE ALA LYS GLU SER SEQRES 4 B 174 GLU MET LYS ALA GLU HIS ALA LYS VAL LEU MET ASP SER SEQRES 5 B 174 LEU THR GLY VAL TRP ASP ASN PHE LEU THR ALA VAL ALA SEQRES 6 B 174 GLY GLY LYS GLY ILE ASP GLU THR THR PHE ILE ASN SER SEQRES 7 B 174 MET LYS GLU MET VAL LYS ASN PRO GLU ALA LYS SER VAL SEQRES 8 B 174 VAL GLU GLY PRO LEU PRO LEU PHE PHE ARG ALA VAL ASP SEQRES 9 B 174 THR ASN GLU ASP ASN ASN ILE SER ARG ASP GLU TYR GLY SEQRES 10 B 174 ILE PHE PHE GLY MET LEU GLY LEU ASP LYS THR MET ALA SEQRES 11 B 174 PRO ALA SER PHE ASP ALA ILE ASP THR ASN ASN ASP GLY SEQRES 12 B 174 LEU LEU SER LEU GLU GLU PHE VAL ILE ALA GLY SER ASP SEQRES 13 B 174 PHE PHE MET ASN ASP GLY ASP SER THR ASN LYS VAL PHE SEQRES 14 B 174 TRP GLY PRO LEU VAL HET CA 190 1 CALCIUM +2 COUNTER ION HET CA 191 1 CALCIUM +2 COUNTER ION HET CA 192 1 CALCIUM +2 COUNTER ION HET CA 193 1 CALCIUM +2 COUNTER ION HET CA 194 1 CALCIUM +2 COUNTER ION HET CA 195 1 CALCIUM +2 COUNTER ION FORMUL 3 CA 6(CA1) FORMUL 4 HOH *213(H2 O1) HELIX 1 A SER A 1 ILE A 15 1 HELIX 2 B ARG A 25 GLU A 38 1 HELIX 3 C ALA A 43 THR A 62 1 HELIX 4 D GLU A 72 LYS A 84 1 HELIX 5 E LYS A 89 VAL A 103 1 HELIX 6 F ARG A 113 MET A 122 1 HELIX 7 G LYS A 127 ILE A 137 1 HELIX 8 H LEU A 147 MET A 159 1 HELIX 9 I SER B 1 ILE B 15 1 HELIX 10 J ARG B 25 GLU B 38 1 HELIX 11 K ALA B 43 THR B 62 1 HELIX 12 L GLU B 72 LYS B 84 1 HELIX 13 M LYS B 89 VAL B 103 1 HELIX 14 N ARG B 113 MET B 122 1 HELIX 15 O LYS B 127 ILE B 137 1 HELIX 16 P LEU B 147 MET B 159 1 SHEET 1 AA 2 ALA A 22 THR A 24 0 SHEET 2 AA 2 GLY A 69 ASP A 71 -1 SHEET 1 BA 2 ASN A 110 SER A 112 0 SHEET 2 BA 2 LEU A 144 SER A 146 -1 SHEET 1 AB 2 ALA B 22 THR B 24 0 SHEET 2 AB 2 GLY B 69 ASP B 71 -1 SHEET 1 BB 2 ASN B 110 SER B 112 0 SHEET 2 BB 2 LEU B 144 SER B 146 -1 TURN 1 T1 ASN A 85 ALA A 88 TURN 2 T2 ASN B 85 ALA B 88 SITE 1 EF1 12 ASP A 16 PHE A 17 ASP A 18 LYS A 19 SITE 2 EF1 12 ASP A 20 GLY A 21 ALA A 22 ILE A 23 SITE 3 EF1 12 THR A 24 ARG A 25 MET A 26 ASP A 27 SITE 1 EF2 12 ASP A 104 THR A 105 ASN A 106 GLU A 107 SITE 2 EF2 12 ASP A 108 ASN A 109 ASN A 110 ILE A 111 SITE 3 EF2 12 SER A 112 ARG A 113 ASP A 114 GLU A 115 SITE 1 EF3 12 ASP A 138 THR A 139 ASN A 140 ASN A 141 SITE 2 EF3 12 ASP A 142 GLY A 143 LEU A 144 LEU A 145 SITE 3 EF3 12 SER A 146 LEU A 147 GLU A 148 GLU A 149 SITE 1 EF4 12 ASP B 16 PHE B 17 ASP B 18 LYS B 19 SITE 2 EF4 12 ASP B 20 GLY B 21 ALA B 22 ILE B 23 SITE 3 EF4 12 THR B 24 ARG B 25 MET B 26 ASP B 27 SITE 1 EF5 12 ASP B 104 THR B 105 ASN B 106 GLU B 107 SITE 2 EF5 12 ASP B 108 ASN B 109 ASN B 110 ILE B 111 SITE 3 EF5 12 SER B 112 ARG B 113 ASP B 114 GLU B 115 SITE 1 EF6 12 ASP B 138 THR B 139 ASN B 140 ASN B 141 SITE 2 EF6 12 ASP B 142 GLY B 143 LEU B 144 LEU B 145 SITE 3 EF6 12 SER B 146 LEU B 147 GLU B 148 GLU B 149 CRYST1 43.600 56.000 65.800 90.00 92.60 90.00 P 21 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.022936 0.000000 0.001042 0.00000 SCALE2 0.000000 0.017857 0.000000 0.00000 SCALE3 0.000000 0.000000 0.015213 0.00000