Header list of 1bod.pdb file
Complete list - n 12 2 Bytes
HEADER CALCIUM-BINDING PROTEIN 23-APR-93 1BOD
TITLE THE SOLUTION STRUCTURES OF MUTANT CALBINDIN D9K'S, AS DETERMINED BY
TITLE 2 NMR, SHOW THAT THE CALCIUM BINDING SITE CAN ADOPT DIFFERENT FOLDS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALBINDIN D9K;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 ORGAN: INTESTINE
KEYWDS CALCIUM-BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 24
AUTHOR C.JOHANSSON,M.ULLNER,T.DRAKENBERG
REVDAT 3 01-MAY-13 1BOD 1 COMPND SEQADV VERSN
REVDAT 2 24-FEB-09 1BOD 1 VERSN
REVDAT 1 31-OCT-93 1BOD 0
JRNL AUTH C.JOHANSSON,M.ULLNER,T.DRAKENBERG
JRNL TITL THE SOLUTION STRUCTURES OF MUTANT CALBINDIN D9K'S, AS
JRNL TITL 2 DETERMINED BY NMR, SHOW THAT THE CALCIUM-BINDING SITE CAN
JRNL TITL 3 ADOPT DIFFERENT FOLDS.
JRNL REF BIOCHEMISTRY V. 32 8429 1993
JRNL REFN ISSN 0006-2960
JRNL PMID 8357794
JRNL DOI 10.1021/BI00084A007
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 1BOD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
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 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 1 ILE A 9 -77.70 169.92
REMARK 500 1 TYR A 13 0.81 -67.30
REMARK 500 1 ASP A 15 46.84 -86.17
REMARK 500 1 LYS A 16 37.72 -79.61
REMARK 500 1 THR A 34 -67.00 85.88
REMARK 500 1 PHE A 36 62.75 -117.62
REMARK 500 1 LEU A 40 35.27 -89.69
REMARK 500 1 SER A 44 72.57 51.84
REMARK 500 1 LEU A 46 -82.45 23.87
REMARK 500 1 ASP A 47 32.82 -85.06
REMARK 500 1 LEU A 49 -39.98 171.37
REMARK 500 1 ASP A 58 29.02 -150.56
REMARK 500 1 SER A 62 -166.19 -75.80
REMARK 500 1 GLN A 67 -82.55 -44.90
REMARK 500 1 ILE A 73 44.24 -83.69
REMARK 500 1 SER A 74 -157.60 178.82
REMARK 500 2 LYS A 1 108.90 74.44
REMARK 500 2 ILE A 9 -79.32 167.64
REMARK 500 2 TYR A 13 3.83 -69.68
REMARK 500 2 ASP A 15 45.72 -86.39
REMARK 500 2 LEU A 32 -70.59 -70.71
REMARK 500 2 GLU A 35 -20.06 82.54
REMARK 500 2 SER A 38 -35.50 -37.49
REMARK 500 2 MET A 43 -160.79 162.00
REMARK 500 2 LEU A 46 -98.17 6.65
REMARK 500 2 GLU A 52 -30.23 -39.14
REMARK 500 2 GLN A 67 -21.54 -37.53
REMARK 500 2 VAL A 68 -11.61 -49.25
REMARK 500 2 SER A 74 -166.15 -55.26
REMARK 500 3 LYS A 1 49.11 38.62
REMARK 500 3 ILE A 9 -56.25 -127.32
REMARK 500 3 ASP A 15 38.44 -84.33
REMARK 500 3 LYS A 16 45.63 -81.56
REMARK 500 3 ASP A 19 -43.06 -145.67
REMARK 500 3 LYS A 29 -29.83 -39.99
REMARK 500 3 GLN A 33 -83.30 -43.51
REMARK 500 3 GLU A 35 -27.94 90.63
REMARK 500 3 LEU A 40 42.99 -95.16
REMARK 500 3 MET A 43 -76.63 173.05
REMARK 500 3 LEU A 46 -90.15 60.15
REMARK 500 3 ASP A 54 18.15 45.84
REMARK 500 3 LYS A 55 -169.34 -55.46
REMARK 500 3 SER A 62 -158.55 -60.85
REMARK 500 3 PHE A 63 -75.91 -75.16
REMARK 500 3 GLN A 67 2.52 -59.71
REMARK 500 4 GLU A 4 41.95 -82.70
REMARK 500 4 GLU A 17 -72.84 -99.26
REMARK 500 4 GLN A 22 -152.31 -111.41
REMARK 500 4 GLU A 26 -39.40 -39.96
REMARK 500 4 LYS A 29 -29.48 -39.04
REMARK 500
REMARK 500 THIS ENTRY HAS 423 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: I
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: II
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
DBREF 1BOD A 1 75 UNP P02633 S100G_BOVIN 4 78
SEQADV 1BOD A UNP P02633 ALA 17 DELETION
SEQADV 1BOD ASP A 15 UNP P02633 ALA 18 ENGINEERED MUTATION
SEQADV 1BOD GLY A 20 UNP P02633 PRO 23 ENGINEERED MUTATION
SEQADV 1BOD A UNP P02633 ASN 24 DELETION
SEQADV 1BOD MET A 43 UNP P02633 PRO 46 ENGINEERED MUTATION
SEQRES 1 A 74 MET LYS SER PRO GLU GLU LEU LYS GLY ILE PHE GLU LYS
SEQRES 2 A 74 TYR ASP LYS GLU GLY ASP GLY GLN LEU SER LYS GLU GLU
SEQRES 3 A 74 LEU LYS LEU LEU LEU GLN THR GLU PHE PRO SER LEU LEU
SEQRES 4 A 74 LYS GLY MET SER THR LEU ASP GLU LEU PHE GLU GLU LEU
SEQRES 5 A 74 ASP LYS ASN GLY ASP GLY GLU VAL SER PHE GLU GLU PHE
SEQRES 6 A 74 GLN VAL LEU VAL LYS LYS ILE SER GLN
HELIX 1 1 SER A 2 LEU A 6 5 5
HELIX 2 2 ILE A 9 ASP A 15 1 6
HELIX 3 3 SER A 24 GLN A 33 1 10
HELIX 4 4 LEU A 49 ASP A 54 1 6
HELIX 5 5 PHE A 66 ILE A 73 1 8
SITE 1 I 12 ASP A 15 LYS A 16 GLU A 17 GLY A 18
SITE 2 I 12 ASP A 19 GLY A 20 GLN A 22 LEU A 23
SITE 3 I 12 SER A 24 LYS A 25 GLU A 26 GLU A 27
SITE 1 II 12 ASP A 54 LYS A 55 ASN A 56 GLY A 57
SITE 2 II 12 ASP A 58 GLY A 59 GLU A 60 VAL A 61
SITE 3 II 12 SER A 62 PHE A 63 GLU A 64 GLU A 65
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 - n 12 2 Bytes