HEADER CALCIUM-BINDING PROTEIN 30-JUL-93 2SAS 2SAS 2 COMPND SARCOPLASMIC CALCIUM-BINDING PROTEIN (ISO TYPE II) 2SAS 3 SOURCE AMPHIOXUS (BRANCHIOSTOMA LANCEOLATUM) 2SAS 4 AUTHOR W.J.COOK,Y.S.BABU,J.A.COX 2SAS 5 REVDAT 2 15-MAY-95 2SASA 1 JRNL 2SASA 1 REVDAT 1 31-OCT-93 2SAS 0 2SAS 6 JRNL AUTH W.J.COOK,L.C.JEFFREY,J.A.COX,S.VIJAY-KUMAR 2SASA 2 JRNL TITL STRUCTURE OF A SARCOPLASMIC CALCIUM-BINDING 2SAS 8 JRNL TITL 2 PROTEIN FROM AMPHIOXUS REFINED AT 2.4 ANGSTROMS 2SAS 9 JRNL TITL 3 RESOLUTION 2SAS 10 JRNL REF J.MOL.BIOL. V. 229 461 1993 2SAS 11 JRNL REFN ASTM JMOBAK UK ISSN 0022-2836 070 2SAS 12 REMARK 1 2SAS 13 REMARK 1 REFERENCE 1 2SAS 14 REMARK 1 AUTH W.J.COOK,Y.S.BABU,J.A.COX 2SAS 15 REMARK 1 TITL CRYSTALLIZATION AND PRELIMINARY X-RAY INVESTIGATION 2SAS 16 REMARK 1 TITL 2 OF A SARCOPLASMIC CALCIUM-BINDING PROTEIN FROM 2SAS 17 REMARK 1 TITL 3 AMPHIOXUS 2SAS 18 REMARK 1 REF J.MOL.BIOL. V. 221 1071 1991 2SAS 19 REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 070 2SAS 20 REMARK 2 2SAS 21 REMARK 2 RESOLUTION. 2.4 ANGSTROMS. 2SAS 22 REMARK 3 2SAS 23 REMARK 3 REFINEMENT. 2SAS 24 REMARK 3 PROGRAM 1 X-PLOR 2SAS 25 REMARK 3 AUTHORS 1 BRUNGER 2SAS 26 REMARK 3 PROGRAM 2 PROLSQ 2SAS 27 REMARK 3 AUTHORS 2 KONNERT,HENDRICKSON 2SAS 28 REMARK 3 R VALUE 0.199 2SAS 29 REMARK 3 2SAS 30 REMARK 3 RESOLUTION RANGE 5.0 - 2.4 ANGSTROMS 2SAS 31 REMARK 3 DATA CUTOFF 2.0 SIGMA(F) 2SAS 32 REMARK 3 2SAS 33 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES (THE VALUES OF 2SAS 34 REMARK 3 SIGMA, IN PARENTHESES, ARE THE INPUT ESTIMATED 2SAS 35 REMARK 3 STANDARD DEVIATIONS THAT DETERMINE THE RELATIVE 2SAS 36 REMARK 3 WEIGHTS OF THE CORRESPONDING RESTRAINTS) 2SAS 37 REMARK 3 DISTANCE RESTRAINTS (ANGSTROMS) 2SAS 38 REMARK 3 BOND DISTANCE 0.016(0.020) 2SAS 39 REMARK 3 ANGLE DISTANCE 0.045(0.030) 2SAS 40 REMARK 3 PLANAR 1-4 DISTANCE 0.062(0.050) 2SAS 41 REMARK 3 PLANE RESTRAINT (ANGSTROMS) 0.014(0.020) 2SAS 42 REMARK 3 CHIRAL-CENTER RESTRAINT (ANGSTROMS**3) 0.153(0.150) 2SAS 43 REMARK 3 NON-BONDED CONTACT RESTRAINTS (ANGSTROMS) 2SAS 44 REMARK 3 SINGLE TORSION CONTACT 0.190(0.400) 2SAS 45 REMARK 3 MULTIPLE TORSION CONTACT 0.209(0.400) 2SAS 46 REMARK 3 POSSIBLE HYDROGEN BOND 0.124(0.400) 2SAS 47 REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINT (DEGREES) 2SAS 48 REMARK 3 PLANAR 2.0(3.0) 2SAS 49 REMARK 3 STAGGERED 21.5(15.0) 2SAS 50 REMARK 3 ORTHONORMAL 30.5(20.0) 2SAS 51 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS (ANGSTROMS**2) 2SAS 52 REMARK 3 MAIN-CHAIN BOND 1.088(1.000) 2SAS 53 REMARK 3 MAIN-CHAIN ANGLE 1.683(1.500) 2SAS 54 REMARK 3 SIDE-CHAIN BOND 1.888(1.500) 2SAS 55 REMARK 3 SIDE-CHAIN ANGLE 2.677(2.000) 2SAS 56 REMARK 4 2SASA 3 REMARK 4 CORRECTION. DELETE TYPESETTING CODE FROM JRNL RECORD. 2SASA 4 REMARK 4 15-MAY-95. 2SASA 5 SEQRES 1 185 GLY LEU ASN ASP PHE GLN LYS GLN LYS ILE LYS PHE THR 2SAS 57 SEQRES 2 185 PHE ASP PHE PHE LEU ASP MET ASN HIS ASP GLY SER ILE 2SAS 58 SEQRES 3 185 GLN ASP ASN ASP PHE GLU ASP MET MET THR ARG TYR LYS 2SAS 59 SEQRES 4 185 GLU VAL ASN LYS GLY SER LEU SER ASP ALA ASP TYR LYS 2SAS 60 SEQRES 5 185 SER MET GLN ALA SER LEU GLU ASP GLU TRP ARG ASP LEU 2SAS 61 SEQRES 6 185 LYS GLY ARG ALA ASP ILE ASN LYS ASP ASP VAL VAL SER 2SAS 62 SEQRES 7 185 TRP GLU GLU TYR LEU ALA MET TRP GLU LYS THR ILE ALA 2SAS 63 SEQRES 8 185 THR CYS LYS SER VAL ALA ASP LEU PRO ALA TRP CYS GLN 2SAS 64 SEQRES 9 185 ASN ARG ILE PRO PHE LEU PHE LYS GLY MET ASP VAL SER 2SAS 65 SEQRES 10 185 GLY ASP GLY ILE VAL ASP LEU GLU GLU PHE GLN ASN TYR 2SAS 66 SEQRES 11 185 CYS LYS ASN PHE GLN LEU GLN CYS ALA ASP VAL PRO ALA 2SAS 67 SEQRES 12 185 VAL TYR ASN VAL ILE THR ASP GLY GLY LYS VAL THR PHE 2SAS 68 SEQRES 13 185 ASP LEU ASN ARG TYR LYS GLU LEU TYR TYR ARG LEU LEU 2SAS 69 SEQRES 14 185 THR SER PRO ALA ALA ASP ALA GLY ASN THR LEU MET GLY 2SAS 70 SEQRES 15 185 GLN LYS PRO 2SAS 71 HET CA 186 1 CALCIUM +2 COUNTER ION 2SAS 72 HET CA 187 1 CALCIUM +2 COUNTER ION 2SAS 73 HET CA 188 1 CALCIUM +2 COUNTER ION 2SAS 74 FORMUL 2 CA 3(CA1) 2SAS 75 FORMUL 3 HOH *H2 O1 2SAS 76 HELIX 1 A ASP 4 LEU 18 1 2SAS 77 HELIX 2 B ASP 28 ASN 42 1 2SAS 78 HELIX 3 C ASP 48 ALA 69 1 2SAS 79 HELIX 4 D TRP 79 ALA 91 1 2SAS 80 HELIX 5 E CYS 103 MET 114 1 2SAS 81 HELIX 6 F LEU 124 LYS 132 1 2SAS 82 HELIX 7 G VAL 141 ILE 148 1 2SAS 83 HELIX 8 H LEU 158 THR 170 1 2SAS 84 HELIX 9 I ALA 176 MET 181 5 2SAS 85 SHEET 1 A 2 SER 25 GLN 27 0 2SAS 86 SHEET 2 A 2 VAL 76 SER 78 -1 2SAS 87 SSBOND 1 CYS 131 CYS 138 2SAS 88 SITE 1 EF1 12 ASP 19 MET 20 ASN 21 HIS 22 2SAS 89 SITE 2 EF1 12 ASP 23 GLY 24 SER 25 ILE 26 2SAS 90 SITE 3 EF1 12 GLN 27 ASP 28 ASN 29 ASP 30 2SAS 91 SITE 1 EF2 12 ASP 70 ILE 71 ASN 72 LYS 73 2SAS 92 SITE 2 EF2 12 ASP 74 ASP 75 VAL 76 VAL 77 2SAS 93 SITE 3 EF2 12 SER 78 TRP 79 GLU 80 GLU 81 2SAS 94 SITE 1 EF3 12 ASP 115 VAL 116 SER 117 GLY 118 2SAS 95 SITE 2 EF3 12 ASP 119 GLY 120 ILE 121 VAL 122 2SAS 96 SITE 3 EF3 12 ASP 123 LEU 124 GLU 125 GLU 126 2SAS 97 CRYST1 59.600 81.300 82.400 90.00 90.00 90.00 C 2 2 21 8 2SAS 98 ORIGX1 1.000000 0.000000 0.000000 0.00000 2SAS 99 ORIGX2 0.000000 1.000000 0.000000 0.00000 2SAS 100 ORIGX3 0.000000 0.000000 1.000000 0.00000 2SAS 101 SCALE1 0.016779 0.000000 0.000000 0.00000 2SAS 102 SCALE2 0.000000 0.012300 0.000000 0.00000 2SAS 103 SCALE3 0.000000 0.000000 0.012136 0.00000 2SAS 104