Header list of 1d1o.pdb file
Complete list - b 16 2 Bytes
HEADER SIGNALING PROTEIN 20-SEP-99 1D1O
TITLE COOPERATIVITY IN EF-HAND CA2+-BINDING PROTEINS: EVIDENCE OF SITE-SITE
TITLE 2 COMMUNICATION FROM BINDING-INDUCED CHANGES IN STRUCTURE AND DYNAMICS
TITLE 3 OF N56A CALBINDIN D9K
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALBINDIN D9K;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CALBINDIN D9K;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: 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_VECTOR_TYPE: PLASMID
KEYWDS EF-HAND, CALCIUM-BINDING PROTEIN, SIGNAL TRANSDUCTION, SIGNALING
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 24
AUTHOR L.MALER,J.BLANKENSHIP,M.RANCE,W.J.CHAZIN
REVDAT 4 16-FEB-22 1D1O 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1D1O 1 VERSN
REVDAT 2 23-MAY-00 1D1O 1 REMARK
REVDAT 1 08-MAR-00 1D1O 0
JRNL AUTH L.MALER,J.BLANKENSHIP,M.RANCE,W.J.CHAZIN
JRNL TITL SITE-SITE COMMUNICATION IN THE EF-HAND CA2+-BINDING PROTEIN
JRNL TITL 2 CALBINDIN D9K.
JRNL REF NAT.STRUCT.BIOL. V. 7 245 2000
JRNL REFN ISSN 1072-8368
JRNL PMID 10700285
JRNL DOI 10.1038/73369
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.AKKE,S.FORSEN,W.J.CHAZIN
REMARK 1 TITL SOLUTION STRUCTURE OF (CD2+)1-CALBINDIN D9K REVEALS DETAILS
REMARK 1 TITL 2 OF THE STEPWISE STRUCTURAL CHANGES ALONG THE
REMARK 1 TITL 3 APO-(CA2+)1-(CA2+)2 BINDING PATHWAY.
REMARK 1 REF J.MOL.BIOL. V. 252 102 1995
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1995.0478
REMARK 1 REFERENCE 2
REMARK 1 AUTH J.KORDEL,N.J.SKELTON,M.AKKE,W.J.CHAZIN
REMARK 1 TITL HIGH RESOLUTION SOLUTION STRUCTURE OF CALCIUM-LOADED
REMARK 1 TITL 2 CALBINDIN D9K.
REMARK 1 REF J.MOL.BIOL. V. 231 711 1993
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1993.1322
REMARK 1 REFERENCE 3
REMARK 1 AUTH N.J.SKELTON,J.KORDEL,W.J.CHAZIN
REMARK 1 TITL DETERMINATION OF THE SOLUTION STRUCTURE OF APO CALBINDIN D9K
REMARK 1 TITL 2 BY NMR SPECTROSCOPY.
REMARK 1 REF J.MOL.BIOL. V. 249 441 1995
REMARK 1 REFN ISSN 0022-2836
REMARK 1 DOI 10.1006/JMBI.1995.0308
REMARK 1 REFERENCE 4
REMARK 1 AUTH B.WIMBERLY,E.THULIN,W.J.CHAZIN
REMARK 1 TITL CHARACTERIZATION OF THE N-TERMINAL HALF-SATURATED STATE OF
REMARK 1 TITL 2 CALBINDIN D9K: NMR STUDIES OF THE N56A MUTANT.
REMARK 1 REF PROTEIN SCI. V. 4 1045 1995
REMARK 1 REFN ISSN 0961-8368
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : FELIX 97.0, AMBER 4.1
REMARK 3 AUTHORS : MSI, SAN DIEGO, CA (FELIX), PEARLMAN, CASE,
REMARK 3 CALDWELL, ROSS, CHEATHAM, FERGUSON, SEIBEL, SINGH,
REMARK 3 WEINER, KOLLMAN (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NMR REFINEMENT WAS BASED ON A TOTAL OF
REMARK 3 910 NOE-DERIVED DISTANCE CONSTRAINTS AND 78 TORSION ANGLE
REMARK 3 CONSTRAINTS. SIMULATED ANNEALING CYCLE OF 20 PS HEATING TO 1200
REMARK 3 K.
REMARK 4
REMARK 4 1D1O COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-SEP-99.
REMARK 100 THE DEPOSITION ID IS D_1000009713.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 300
REMARK 210 PH : 6.0; 6.0
REMARK 210 IONIC STRENGTH : 0; 0
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 4 MM N56A-CALBINDIN D9K; 4 MM
REMARK 210 15N-LABELED N56A-CALBINDIN D9K;
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HSQC-J
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; DRX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DIANA 2.8
REMARK 210 METHOD USED : DISTANCE GEOMETRY FOLLOWED BY
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 24
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 MOLECULAR ENEGIES WERE ORDERED
REMARK 210 BY LEAST RESTRAINT VIOLATIONS.
REMARK 210 THE 24 BEST CONFORMERS WERE
REMARK 210 SELECTED TO FACILITATE
REMARK 210 COMPARISON TO PREVIOUS
REMARK 210 STRUCTURES OF THE PROTEIN AND
REMARK 210 BECAUSE THIS SURPASSES THE
REMARK 210 STATISTICAL REQUIREMENT TO
REMARK 210 REPRESENT ALL OF CONFORMATIONAL
REMARK 210 SPACE CONSISTENT WITH THE DATA.
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: 1H RESONANCE ASIGNMENTS WERE REPORTED IN THE PROTEIN
REMARK 210 SCIENCE PAPER BY WIMBERLY ET AL. A 3D 15N SPARATED TOCSY WAS
REMARK 210 RECORDED TO CONFIRM THESE ASSIGNMENTS AND ASSIGN THE 15N
REMARK 210 RESONANCES.
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 PRO A 37 -36.24 -39.24
REMARK 500 1 LYS A 41 -65.80 62.98
REMARK 500 1 ASP A 54 45.15 -81.08
REMARK 500 1 ASP A 58 -57.67 66.43
REMARK 500 1 SER A 74 -44.16 76.25
REMARK 500 2 PRO A 37 71.72 -69.69
REMARK 500 2 SER A 38 -73.55 -170.63
REMARK 500 2 LYS A 41 -56.75 49.02
REMARK 500 2 ASP A 58 54.49 34.16
REMARK 500 2 SER A 74 -46.88 78.23
REMARK 500 3 PRO A 37 75.55 -66.23
REMARK 500 3 SER A 38 -42.93 173.59
REMARK 500 3 LEU A 40 40.66 -169.33
REMARK 500 3 ASP A 54 43.32 -78.81
REMARK 500 3 ALA A 56 -54.06 177.43
REMARK 500 3 ASP A 58 -59.70 68.64
REMARK 500 4 ASN A 21 38.79 -159.83
REMARK 500 4 SER A 38 -40.08 75.18
REMARK 500 4 MET A 43 -122.86 -87.61
REMARK 500 4 ASP A 54 48.23 -80.55
REMARK 500 4 ASP A 58 75.10 0.34
REMARK 500 5 ASN A 21 53.74 -148.76
REMARK 500 5 PRO A 37 72.15 -69.31
REMARK 500 5 SER A 38 -35.69 -178.84
REMARK 500 5 LEU A 40 64.63 -68.59
REMARK 500 5 LYS A 41 77.66 -65.62
REMARK 500 5 ASP A 54 45.80 -80.24
REMARK 500 5 ALA A 56 -55.00 -172.26
REMARK 500 6 ASN A 21 42.08 -143.59
REMARK 500 6 PRO A 37 79.83 -22.04
REMARK 500 6 LYS A 41 -54.67 68.06
REMARK 500 6 SER A 44 -61.96 64.68
REMARK 500 6 THR A 45 -33.97 -37.05
REMARK 500 6 SER A 74 -66.25 69.55
REMARK 500 7 ASP A 19 115.18 -39.69
REMARK 500 7 GLN A 22 142.96 -173.75
REMARK 500 7 PHE A 36 73.86 -112.40
REMARK 500 7 SER A 38 -41.12 66.79
REMARK 500 7 LEU A 40 9.56 -53.39
REMARK 500 7 ASP A 54 43.61 -80.87
REMARK 500 7 SER A 74 -57.92 73.06
REMARK 500 8 GLN A 22 140.20 -171.69
REMARK 500 8 SER A 38 -50.78 70.98
REMARK 500 8 MET A 43 -72.39 -67.12
REMARK 500 8 ALA A 56 -36.94 176.83
REMARK 500 8 SER A 74 -57.70 65.82
REMARK 500 9 ASN A 21 38.56 -144.47
REMARK 500 9 SER A 38 -68.48 -160.53
REMARK 500 9 LEU A 40 -44.79 -179.04
REMARK 500 9 LYS A 41 -68.31 61.15
REMARK 500
REMARK 500 THIS ENTRY HAS 149 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 2 PHE A 10 0.08 SIDE CHAIN
REMARK 500 3 PHE A 10 0.09 SIDE CHAIN
REMARK 500 7 PHE A 10 0.09 SIDE CHAIN
REMARK 500 8 PHE A 10 0.09 SIDE CHAIN
REMARK 500 8 PHE A 36 0.09 SIDE CHAIN
REMARK 500 10 PHE A 36 0.08 SIDE CHAIN
REMARK 500 11 PHE A 10 0.09 SIDE CHAIN
REMARK 500 13 PHE A 36 0.10 SIDE CHAIN
REMARK 500 14 PHE A 10 0.09 SIDE CHAIN
REMARK 500 15 PHE A 10 0.09 SIDE CHAIN
REMARK 500 16 PHE A 36 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2BCB RELATED DB: PDB
REMARK 900 NMR SOLUTION STRUCTURE OF CA2+-LOADED CALBINDIN D9K
REMARK 900 RELATED ID: 1CDN RELATED DB: PDB
REMARK 900 NMR SOLUTION STRUCTURE OF (CD2+)1 CALBINDIN D9K
REMARK 900 RELATED ID: 1CLB RELATED DB: PDB
REMARK 900 NMR SOLUTION STRUCTURE OF APO CALBINDIN D9K
DBREF 1D1O A 1 75 UNP P02633 S100G_BOVIN 5 79
SEQADV 1D1O MET A 43 UNP P02633 PRO 47 CONFLICT
SEQADV 1D1O ALA A 56 UNP P02633 ASN 60 CONFLICT
SEQRES 1 A 75 LYS SER PRO GLU GLU LEU LYS GLY ILE PHE GLU LYS TYR
SEQRES 2 A 75 ALA ALA LYS GLU GLY ASP PRO ASN GLN LEU SER LYS GLU
SEQRES 3 A 75 GLU LEU LYS LEU LEU LEU GLN THR GLU PHE PRO SER LEU
SEQRES 4 A 75 LEU LYS GLY MET SER THR LEU ASP GLU LEU PHE GLU GLU
SEQRES 5 A 75 LEU ASP LYS ALA GLY ASP GLY GLU VAL SER PHE GLU GLU
SEQRES 6 A 75 PHE GLN VAL LEU VAL LYS LYS ILE SER GLN
HELIX 1 1 LYS A 1 GLU A 17 1 17
HELIX 2 2 LYS A 25 PHE A 36 1 12
HELIX 3 3 GLY A 42 SER A 44 5 3
HELIX 4 4 THR A 45 ASP A 54 1 10
HELIX 5 5 PHE A 63 SER A 74 1 12
SHEET 1 A 2 GLN A 22 SER A 24 0
SHEET 2 A 2 GLU A 60 SER A 62 -1 N VAL A 61 O LEU A 23
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 16 2 Bytes