Header list of 1iku.pdb file
Complete list - b 23 2 Bytes
HEADER CALCIUM-BINDING PROTEIN 18-JAN-96 1IKU
TITLE MYRISTOYLATED RECOVERIN IN THE CALCIUM-FREE STATE, NMR, 22 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 TISSUE: RETINA;
SOURCE 6 CELL: ROD;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTREC2
KEYWDS CALCIUM-MYRISTOYL SWITCH, CALCUIM-BINDING PROTEIN, CALCIUM-BINDING
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 22
AUTHOR T.TANAKA,J.B.AMES,T.S.HARVEY,L.STRYER,M.IKURA
REVDAT 3 23-FEB-22 1IKU 1 REMARK LINK
REVDAT 2 24-FEB-09 1IKU 1 VERSN
REVDAT 1 11-JUL-96 1IKU 0
JRNL AUTH T.TANAKA,J.B.AMES,T.S.HARVEY,L.STRYER,M.IKURA
JRNL TITL SEQUESTRATION OF THE MEMBRANE-TARGETING MYRISTOYL GROUP OF
JRNL TITL 2 RECOVERIN IN THE CALCIUM-FREE STATE.
JRNL REF NATURE V. 376 444 1995
JRNL REFN ISSN 0028-0836
JRNL PMID 7630423
JRNL DOI 10.1038/376444A0
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 2.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1IKU 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_1000174176.
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 : 22
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 1-22
REMARK 465 RES C SSSEQI
REMARK 465 PRO A 190
REMARK 465 GLN A 191
REMARK 465 LYS A 192
REMARK 465 VAL A 193
REMARK 465 LYS A 194
REMARK 465 GLU A 195
REMARK 465 LYS A 196
REMARK 465 LEU A 197
REMARK 465 LYS A 198
REMARK 465 GLU A 199
REMARK 465 LYS A 200
REMARK 465 LYS A 201
REMARK 465 LEU A 202
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MYR A 1
DBREF 1IKU A 2 202 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 MYR A 1 42
HETNAM MYR MYRISTIC ACID
FORMUL 2 MYR C14 H28 O2
HELIX 1 1 SER A 4 GLU A 16 1 13
HELIX 2 2 GLU A 25 GLU A 38 1 14
HELIX 3 3 ARG A 46 PHE A 56 1 11
HELIX 4 4 ALA A 66 PHE A 73 1 8
HELIX 5 5 PHE A 83 HIS A 91 1 9
HELIX 6 6 THR A 98 TYR A 109 1 12
HELIX 7 7 LYS A 119 MET A 132 1 14
HELIX 8 8 PRO A 135 HIS A 140 1 6
HELIX 9 9 PRO A 148 PHE A 159 1 12
HELIX 10 10 GLU A 169 ALA A 178 1 10
HELIX 11 11 LYS A 180 ILE A 186 1 7
SHEET 1 S1 2 ARG A 43 THR A 45 0
SHEET 2 S1 2 THR A 80 ASP A 82 -1
SHEET 1 S2 2 THR A 116 SER A 118 0
SHEET 2 S2 2 LYS A 166 THR A 168 -1
LINK C1 MYR A 1 N GLY A 2 1555 1555 1.31
SITE 1 AC1 4 GLY A 2 ASN A 3 TYR A 32 VAL A 87
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