Header list of 1cdn.pdb file
Complete list - v 3 2 Bytes
HEADER CALCIUM-BINDING PROTEIN 04-AUG-95 1CDN
TITLE SOLUTION STRUCTURE OF (CD2+)1-CALBINDIN D9K REVEALS DETAILS OF THE
TITLE 2 STEPWISE STRUCTURAL CHANGES ALONG THE APO--> (CA2+)II1--> (CA2+)I,II2
TITLE 3 BINDING PATHWAY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALBINDIN D9K;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: INTESTINAL CALCIUM-BINDING PROTEIN, ICBP, ICABP, CABP9K,
COMPND 5 S100D;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 OTHER_DETAILS: BOVINE MINOR A FORM, CADMIUM-HALF-SATURATED, CADMIUM
COMPND 9 ION IS BOUND IN C-TERMINAL SITE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 GENE: ICABP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PICB1;
SOURCE 9 EXPRESSION_SYSTEM_GENE: ICABP
KEYWDS EF-HAND, CALCIUM-BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 24
AUTHOR M.AKKE,S.FORSEN,W.J.CHAZIN
REVDAT 3 03-NOV-21 1CDN 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1CDN 1 VERSN
REVDAT 1 14-NOV-95 1CDN 0
JRNL AUTH M.AKKE,S.FORSEN,W.J.CHAZIN
JRNL TITL SOLUTION STRUCTURE OF (CD2+)1-CALBINDIN D9K REVEALS DETAILS
JRNL TITL 2 OF THE STEPWISE STRUCTURAL CHANGES ALONG THE
JRNL TITL 3 APO-->(CA2+)II1-->(CA2+)I,II2 BINDING PATHWAY.
JRNL REF J.MOL.BIOL. V. 252 102 1995
JRNL REFN ISSN 0022-2836
JRNL PMID 7666423
JRNL DOI 10.1006/JMBI.1995.0478
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH N.J.SKELTON,J.KOERDEL,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 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 REFERENCE 3
REMARK 1 AUTH M.AKKE,S.FORSEN,W.J.CHAZIN
REMARK 1 TITL MOLECULAR BASIS FOR CO-OPERATIVITY IN CA2+ BINDING IN
REMARK 1 TITL 2 CALBINDIN D9K. 1H NUCLEAR MAGNETIC RESONANCE STUDIES OF
REMARK 1 TITL 3 (CD2+)1-BOVINE CALBINDIN D9K
REMARK 1 REF J.MOL.BIOL. V. 220 173 1991
REMARK 1 REFN ISSN 0022-2836
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DISGEO, AMBER 4.0
REMARK 3 AUTHORS : HAVEL,WUTHRICH (DISGEO),
REMARK 3 PEARLMAN,CASE,CALDWELL,SEIBEL,SINGH,WEINER,KOLLMAN
REMARK 3 (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CDN 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_1000172259.
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 MET A 0
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500
REMARK 500 REMARK: NULL
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 3 SER A 74 -39.93 64.06
REMARK 500 4 GLU A 17 -46.20 78.57
REMARK 500 4 SER A 74 -70.91 -178.18
REMARK 500 5 SER A 44 -93.12 34.07
REMARK 500 5 ASP A 58 -45.50 -139.81
REMARK 500 5 SER A 74 -54.32 -159.61
REMARK 500 6 GLU A 17 116.24 60.74
REMARK 500 6 LYS A 41 -88.18 20.83
REMARK 500 6 SER A 44 -136.08 52.25
REMARK 500 6 SER A 74 -62.31 73.14
REMARK 500 7 SER A 74 73.42 -168.54
REMARK 500 8 LYS A 16 91.27 -61.32
REMARK 500 8 GLU A 17 -41.49 77.53
REMARK 500 8 LEU A 40 -73.76 51.20
REMARK 500 8 LYS A 55 89.60 -65.08
REMARK 500 8 ASP A 58 -42.51 -137.01
REMARK 500 9 GLU A 17 -47.48 -154.62
REMARK 500 9 SER A 44 -59.49 -26.54
REMARK 500 9 ASN A 56 48.81 28.92
REMARK 500 10 SER A 44 -146.59 55.10
REMARK 500 11 LYS A 41 -151.63 -114.94
REMARK 500 11 SER A 44 -102.46 52.22
REMARK 500 11 ASN A 56 38.28 39.85
REMARK 500 11 SER A 74 -94.60 45.27
REMARK 500 12 LYS A 16 44.90 -79.10
REMARK 500 12 GLU A 17 -51.17 -170.72
REMARK 500 12 SER A 44 -111.22 35.51
REMARK 500 12 ASN A 56 41.19 37.91
REMARK 500 13 GLU A 17 -42.44 -139.94
REMARK 500 13 ASP A 54 72.83 -67.41
REMARK 500 13 LYS A 55 99.77 -57.30
REMARK 500 13 ASN A 56 5.32 95.75
REMARK 500 13 SER A 74 57.05 -160.76
REMARK 500 14 GLU A 17 -45.76 -155.29
REMARK 500 14 SER A 74 -47.82 -173.85
REMARK 500 15 PHE A 36 56.91 -145.34
REMARK 500 15 ASN A 56 32.12 -154.28
REMARK 500 16 GLU A 17 -37.21 73.20
REMARK 500 16 SER A 44 -162.21 57.00
REMARK 500 16 ASP A 54 73.89 -116.42
REMARK 500 16 ASN A 56 32.32 -148.20
REMARK 500 16 ASP A 58 -18.79 -145.92
REMARK 500 16 SER A 74 47.25 -77.71
REMARK 500 17 GLU A 17 109.71 54.85
REMARK 500 17 SER A 44 -105.00 55.78
REMARK 500 17 SER A 74 -63.76 71.21
REMARK 500 18 SER A 44 -89.57 -96.69
REMARK 500 18 SER A 74 47.20 -76.74
REMARK 500 19 GLU A 17 -43.49 -141.93
REMARK 500 19 ASN A 56 35.71 37.28
REMARK 500
REMARK 500 THIS ENTRY HAS 62 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 3 PHE A 50 0.09 SIDE CHAIN
REMARK 500 4 PHE A 36 0.09 SIDE CHAIN
REMARK 500 5 PHE A 50 0.08 SIDE CHAIN
REMARK 500 6 PHE A 50 0.09 SIDE CHAIN
REMARK 500 8 PHE A 50 0.11 SIDE CHAIN
REMARK 500 9 TYR A 13 0.08 SIDE CHAIN
REMARK 500 9 PHE A 50 0.10 SIDE CHAIN
REMARK 500 10 PHE A 50 0.09 SIDE CHAIN
REMARK 500 11 PHE A 50 0.10 SIDE CHAIN
REMARK 500 12 PHE A 50 0.11 SIDE CHAIN
REMARK 500 13 TYR A 13 0.07 SIDE CHAIN
REMARK 500 15 PHE A 50 0.09 SIDE CHAIN
REMARK 500 16 TYR A 13 0.10 SIDE CHAIN
REMARK 500 16 PHE A 50 0.09 SIDE CHAIN
REMARK 500 17 PHE A 36 0.10 SIDE CHAIN
REMARK 500 17 PHE A 50 0.08 SIDE CHAIN
REMARK 500 18 PHE A 50 0.09 SIDE CHAIN
REMARK 500 19 PHE A 50 0.10 SIDE CHAIN
REMARK 500 20 TYR A 13 0.12 SIDE CHAIN
REMARK 500 20 PHE A 50 0.09 SIDE CHAIN
REMARK 500 21 PHE A 50 0.10 SIDE CHAIN
REMARK 500 22 TYR A 13 0.08 SIDE CHAIN
REMARK 500 23 TYR A 13 0.07 SIDE CHAIN
REMARK 500 23 PHE A 50 0.10 SIDE CHAIN
REMARK 500 24 PHE A 50 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: LOA
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 800
REMARK 800 SITE_IDENTIFIER: LOB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
DBREF 1CDN A 1 75 UNP P02633 S100G_BOVIN 4 78
SEQADV 1CDN GLY A 43 UNP P02633 PRO 46 ENGINEERED MUTATION
SEQRES 1 A 76 MET LYS SER PRO GLU GLU LEU LYS GLY ILE PHE GLU LYS
SEQRES 2 A 76 TYR ALA ALA LYS GLU GLY ASP PRO ASN GLN LEU SER LYS
SEQRES 3 A 76 GLU GLU LEU LYS LEU LEU LEU GLN THR GLU PHE PRO SER
SEQRES 4 A 76 LEU LEU LYS GLY GLY SER THR LEU ASP GLU LEU PHE GLU
SEQRES 5 A 76 GLU LEU ASP LYS ASN GLY ASP GLY GLU VAL SER PHE GLU
SEQRES 6 A 76 GLU PHE GLN VAL LEU VAL LYS LYS ILE SER GLN
HELIX 1 1 PRO A 3 GLU A 17 1 15
HELIX 2 2 LYS A 25 GLU A 35 1 11
HELIX 3 3 LEU A 46 LEU A 53 1 8
HELIX 4 4 PHE A 63 ILE A 73 1 11
SHEET 1 A 2 GLN A 22 LEU A 23 0
SHEET 2 A 2 VAL A 61 SER A 62 -1 O VAL A 61 N LEU A 23
SITE 1 LOA 14 ALA A 14 ALA A 15 LYS A 16 GLU A 17
SITE 2 LOA 14 GLY A 18 ASP A 19 PRO A 20 ASN A 21
SITE 3 LOA 14 GLN A 22 LEU A 23 SER A 24 LYS A 25
SITE 4 LOA 14 GLU A 26 GLU A 27
SITE 1 LOB 12 ASP A 54 LYS A 55 ASN A 56 GLY A 57
SITE 2 LOB 12 ASP A 58 GLY A 59 GLU A 60 VAL A 61
SITE 3 LOB 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 - v 3 2 Bytes