Header list of 1jsa.pdb file
Complete list - b 23 2 Bytes
HEADER CALCIUM BINDING 04-JUN-97 1JSA
TITLE MYRISTOYLATED RECOVERIN WITH TWO CALCIUMS BOUND, NMR, 24 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RECOVERIN;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PTREC2
KEYWDS CALCIUM BINDING PROTEIN, CALCIUM-MYRISTOYL SWITCH, CALCIUM BINDING
EXPDTA SOLUTION NMR
NUMMDL 24
AUTHOR J.B.AMES,R.ISHIMA,T.TANAKA,J.I.GORDON,L.STRYER,M.IKURA
REVDAT 3 23-FEB-22 1JSA 1 REMARK LINK
REVDAT 2 24-FEB-09 1JSA 1 VERSN
REVDAT 1 15-OCT-97 1JSA 0
JRNL AUTH J.B.AMES,R.ISHIMA,T.TANAKA,J.I.GORDON,L.STRYER,M.IKURA
JRNL TITL MOLECULAR MECHANICS OF CALCIUM-MYRISTOYL SWITCHES.
JRNL REF NATURE V. 389 198 1997
JRNL REFN ISSN 0028-0836
JRNL PMID 9296500
JRNL DOI 10.1038/38310
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1JSA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000174364.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 24
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-24
REMARK 465 RES C SSSEQI
REMARK 465 PRO A 189
REMARK 465 GLN A 190
REMARK 465 LYS A 191
REMARK 465 VAL A 192
REMARK 465 LYS A 193
REMARK 465 GLU A 194
REMARK 465 LYS A 195
REMARK 465 LEU A 196
REMARK 465 LYS A 197
REMARK 465 GLU A 198
REMARK 465 LYS A 199
REMARK 465 LYS A 200
REMARK 465 LEU A 201
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 500 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 73 OD1
REMARK 620 2 ASN A 75 OD1 129.1
REMARK 620 3 ASP A 77 OD2 65.8 91.1
REMARK 620 4 THR A 79 O 57.0 148.9 62.4
REMARK 620 5 GLU A 84 OE1 95.5 89.8 156.0 121.1
REMARK 620 6 GLU A 84 OE2 113.0 109.6 148.2 89.7 51.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 109 OD1
REMARK 620 2 ASP A 111 OD1 60.9
REMARK 620 3 ASN A 113 OD1 90.8 62.0
REMARK 620 4 THR A 115 O 109.4 165.3 131.6
REMARK 620 5 GLU A 120 OE1 66.9 58.2 119.8 108.6
REMARK 620 6 GLU A 120 OE2 116.5 72.6 103.7 105.2 52.1
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 500
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR A 502
DBREF 1JSA A 1 201 UNP P21457 RECO_BOVIN 1 201
SEQRES 1 A 201 GLY ASN SER LYS SER GLY ALA LEU SER LYS GLU ILE LEU
SEQRES 2 A 201 GLU GLU LEU GLN LEU ASN THR LYS PHE THR GLU GLU GLU
SEQRES 3 A 201 LEU SER SER TRP TYR GLN SER PHE LEU LYS GLU CYS PRO
SEQRES 4 A 201 SER GLY ARG ILE THR ARG GLN GLU PHE GLN THR ILE TYR
SEQRES 5 A 201 SER LYS PHE PHE PRO GLU ALA ASP PRO LYS ALA TYR ALA
SEQRES 6 A 201 GLN HIS VAL PHE ARG SER PHE ASP ALA ASN SER ASP GLY
SEQRES 7 A 201 THR LEU ASP PHE LYS GLU TYR VAL ILE ALA LEU HIS MET
SEQRES 8 A 201 THR SER ALA GLY LYS THR ASN GLN LYS LEU GLU TRP ALA
SEQRES 9 A 201 PHE SER LEU TYR ASP VAL ASP GLY ASN GLY THR ILE SER
SEQRES 10 A 201 LYS ASN GLU VAL LEU GLU ILE VAL THR ALA ILE PHE LYS
SEQRES 11 A 201 MET ILE SER PRO GLU ASP THR LYS HIS LEU PRO GLU ASP
SEQRES 12 A 201 GLU ASN THR PRO GLU LYS ARG ALA GLU LYS ILE TRP GLY
SEQRES 13 A 201 PHE PHE GLY LYS LYS ASP ASP ASP LYS LEU THR GLU LYS
SEQRES 14 A 201 GLU PHE ILE GLU GLY THR LEU ALA ASN LYS GLU ILE LEU
SEQRES 15 A 201 ARG LEU ILE GLN PHE GLU PRO GLN LYS VAL LYS GLU LYS
SEQRES 16 A 201 LEU LYS GLU LYS LYS LEU
HET CA A 500 1
HET CA A 501 1
HET MYR A 502 42
HETNAM CA CALCIUM ION
HETNAM MYR MYRISTIC ACID
FORMUL 2 CA 2(CA 2+)
FORMUL 4 MYR C14 H28 O2
HELIX 1 1 LYS A 10 LEU A 16 1 7
HELIX 2 2 GLU A 26 GLU A 37 1 12
HELIX 3 3 PHE A 48 PHE A 55 5 8
HELIX 4 4 LYS A 62 ALA A 65 1 4
HELIX 5 5 HIS A 67 ARG A 70 1 4
HELIX 6 6 PHE A 82 MET A 91 1 10
HELIX 7 7 GLU A 102 LEU A 107 5 6
HELIX 8 8 LYS A 118 MET A 131 1 14
HELIX 9 9 PRO A 134 THR A 137 1 4
HELIX 10 10 GLU A 142 GLU A 144 5 3
HELIX 11 11 PRO A 147 PHE A 158 1 12
HELIX 12 12 GLU A 170 LEU A 176 1 7
SHEET 1 A 2 THR A 115 ILE A 116 0
SHEET 2 A 2 LEU A 166 THR A 167 -1 O LEU A 166 N ILE A 116
LINK N GLY A 1 C1 MYR A 502 1555 1555 1.31
LINK OD1 ASP A 73 CA CA A 500 1555 1555 2.53
LINK OD1 ASN A 75 CA CA A 500 1555 1555 2.57
LINK OD2 ASP A 77 CA CA A 500 1555 1555 2.47
LINK O THR A 79 CA CA A 500 1555 1555 2.56
LINK OE1 GLU A 84 CA CA A 500 1555 1555 2.53
LINK OE2 GLU A 84 CA CA A 500 1555 1555 2.51
LINK OD1 ASP A 109 CA CA A 501 1555 1555 2.51
LINK OD1 ASP A 111 CA CA A 501 1555 1555 2.51
LINK OD1 ASN A 113 CA CA A 501 1555 1555 2.48
LINK O THR A 115 CA CA A 501 1555 1555 2.51
LINK OE1 GLU A 120 CA CA A 501 1555 1555 2.48
LINK OE2 GLU A 120 CA CA A 501 1555 1555 2.50
SITE 1 AC1 5 ASP A 73 ASN A 75 ASP A 77 THR A 79
SITE 2 AC1 5 GLU A 84
SITE 1 AC2 5 ASP A 109 ASP A 111 ASN A 113 THR A 115
SITE 2 AC2 5 GLU A 120
SITE 1 AC3 1 GLY A 1
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - b 23 2 Bytes