HEADER CALCIUM-BINDING PROTEIN 05-DEC-97 1UWO
TITLE CALCIUM FORM OF HUMAN S100B, NMR, 20 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: S100B;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: S-100B;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 TISSUE: NERVOUS;
SOURCE 7 CELL: GLIAL;
SOURCE 8 CELLULAR_LOCATION: CYTOPLASM;
SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 11 EXPRESSION_SYSTEM_STRAIN: N99;
SOURCE 12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 13 EXPRESSION_SYSTEM_VECTOR: PSD80;
SOURCE 14 EXPRESSION_SYSTEM_PLASMID: PSS2
KEYWDS HUMAN S100B, CALCIUM-BINDING PROTEIN, EF-HAND, CONFORMATIONAL CHANGE,
KEYWDS 2 SOLUTION STRUCTURE
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.P.SMITH,G.S.SHAW
REVDAT 3 02-MAR-22 1UWO 1 REMARK
REVDAT 2 24-FEB-09 1UWO 1 VERSN
REVDAT 1 10-JUN-98 1UWO 0
JRNL AUTH S.P.SMITH,G.S.SHAW
JRNL TITL A NOVEL CALCIUM-SENSITIVE SWITCH REVEALED BY THE STRUCTURE
JRNL TITL 2 OF HUMAN S100B IN THE CALCIUM-BOUND FORM.
JRNL REF STRUCTURE V. 6 211 1998
JRNL REFN ISSN 0969-2126
JRNL PMID 9519411
JRNL DOI 10.1016/S0969-2126(98)00022-7
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.P.SMITH,G.S.SHAW
REMARK 1 TITL ASSIGNMENT AND SECONDARY STRUCTURE OF CALCIUM-BOUND HUMAN
REMARK 1 TITL 2 S100B
REMARK 1 REF J.BIOMOL.NMR V. 10 77 1997
REMARK 1 REFN ISSN 0925-2738
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES OF THE MONOMERS WERE
REMARK 3 CALCULATED USING MATRIX DISTANCE GEOMETRY, FOLLOWED BY SIMULATED
REMARK 3 ANNEALING. THE MONOMERS WERE THEN DUPLICATED AND EACH NEW
REMARK 3 SUBUNIT WAS ROTATED 180 DEGREES AND SEPARATELY FROM ITS PARTNER
REMARK 3 BY 40 ANGSTROMS. NO DOCKING OF THE TWO MONOMERS WAS ATTEMPTED
REMARK 3 PRIOR THE FURTHER STRUCTURE CALCULATIONS. DIMER STRUCTURE
REMARK 3 CALCULATIONS USED THE 40 UNAMBIGUOUS INTERMONOMER NOES TO BRING
REMARK 3 THE SUBUNITS IN A POSITION RELATIVE TO ONE ANOTHER. A FURTHER
REMARK 3 FOUR ROUNDS OF SIMULATED ANNEALING GENERATED THE FINAL
REMARK 3 STRUCTURES. AT NO POINT DURING THE DIMER CALCULATIONS WAS NON-
REMARK 3 CRYSTALLOGRAPHIC SYMMETRY UTILIZED.
REMARK 4
REMARK 4 1UWO 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_1000176991.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 7.05
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCACB; CBCA(CO)NH; HNCO; HNHA;
REMARK 210 1H-15N NOESY-HSQC; 15N/13C NOESY-
REMARK 210 HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY500
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : HYBRID DISTANCE GEOMETRY AND
REMARK 210 SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATIONS
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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 ASP A 23 -158.41 -57.91
REMARK 500 1 LYS A 24 89.79 -153.93
REMARK 500 1 HIS A 25 -36.41 -169.05
REMARK 500 1 LYS A 29 -85.80 43.17
REMARK 500 1 ASN A 37 -71.83 -94.92
REMARK 500 1 LEU A 40 61.97 -106.90
REMARK 500 1 HIS A 42 -56.15 -124.24
REMARK 500 1 GLU A 46 -136.31 -67.83
REMARK 500 1 ILE A 47 -146.44 64.75
REMARK 500 1 LYS A 48 -44.58 83.59
REMARK 500 1 GLN A 50 59.28 78.34
REMARK 500 1 GLU A 51 -70.60 -90.08
REMARK 500 1 LEU A 60 -36.43 -37.82
REMARK 500 1 ASP A 65 -32.47 176.87
REMARK 500 1 ASP B 23 174.93 52.06
REMARK 500 1 LYS B 24 59.43 -172.44
REMARK 500 1 HIS B 25 -35.24 -169.20
REMARK 500 1 ASN B 37 -65.35 -93.01
REMARK 500 1 LEU B 40 67.11 -108.14
REMARK 500 1 HIS B 42 -77.28 -103.81
REMARK 500 1 GLU B 45 -150.97 48.75
REMARK 500 1 ILE B 47 160.24 57.26
REMARK 500 1 LYS B 48 55.33 -111.28
REMARK 500 1 GLU B 49 41.79 74.31
REMARK 500 1 GLN B 50 51.48 72.51
REMARK 500 1 GLU B 51 -70.16 -88.65
REMARK 500 1 ASP B 63 28.82 -171.73
REMARK 500 1 ASP B 65 -34.44 -179.34
REMARK 500 1 THR B 81 -70.16 -75.11
REMARK 500 1 HIS B 85 -70.06 -65.54
REMARK 500 1 GLU B 89 96.13 -44.18
REMARK 500 2 GLU A 2 -79.45 -68.28
REMARK 500 2 ASP A 23 -169.70 47.75
REMARK 500 2 LYS A 24 -38.67 -169.31
REMARK 500 2 LYS A 29 -83.03 41.53
REMARK 500 2 HIS A 42 -51.31 -176.07
REMARK 500 2 PHE A 43 -77.10 -101.23
REMARK 500 2 ILE A 47 -83.05 -63.24
REMARK 500 2 LYS A 48 28.48 40.24
REMARK 500 2 GLU A 49 -78.83 170.56
REMARK 500 2 GLN A 50 26.88 -168.04
REMARK 500 2 MET A 57 -29.08 -39.78
REMARK 500 2 ASP A 65 -35.19 -177.89
REMARK 500 2 MET A 79 -70.76 -71.94
REMARK 500 2 TYR B 17 -70.27 -92.47
REMARK 500 2 SER B 18 29.01 38.87
REMARK 500 2 GLU B 21 69.91 -100.05
REMARK 500 2 LYS B 29 -86.19 60.97
REMARK 500 2 LEU B 32 -70.17 -61.25
REMARK 500 2 PHE B 43 -72.48 -97.57
REMARK 500
REMARK 500 THIS ENTRY HAS 596 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 1 ARG A 20 0.26 SIDE CHAIN
REMARK 500 1 ARG B 20 0.24 SIDE CHAIN
REMARK 500 2 ARG A 20 0.27 SIDE CHAIN
REMARK 500 2 ARG B 20 0.30 SIDE CHAIN
REMARK 500 3 ARG A 20 0.24 SIDE CHAIN
REMARK 500 3 ARG B 20 0.28 SIDE CHAIN
REMARK 500 4 ARG A 20 0.32 SIDE CHAIN
REMARK 500 4 ARG B 20 0.12 SIDE CHAIN
REMARK 500 5 ARG A 20 0.32 SIDE CHAIN
REMARK 500 5 ARG B 20 0.32 SIDE CHAIN
REMARK 500 6 ARG A 20 0.31 SIDE CHAIN
REMARK 500 6 ARG B 20 0.28 SIDE CHAIN
REMARK 500 7 ARG A 20 0.28 SIDE CHAIN
REMARK 500 7 ARG B 20 0.28 SIDE CHAIN
REMARK 500 8 ARG A 20 0.32 SIDE CHAIN
REMARK 500 8 ARG B 20 0.27 SIDE CHAIN
REMARK 500 9 ARG A 20 0.26 SIDE CHAIN
REMARK 500 9 ARG B 20 0.32 SIDE CHAIN
REMARK 500 10 ARG A 20 0.21 SIDE CHAIN
REMARK 500 10 ARG B 20 0.18 SIDE CHAIN
REMARK 500 11 ARG A 20 0.25 SIDE CHAIN
REMARK 500 11 ARG B 20 0.28 SIDE CHAIN
REMARK 500 12 ARG A 20 0.28 SIDE CHAIN
REMARK 500 12 ARG B 20 0.19 SIDE CHAIN
REMARK 500 13 ARG A 20 0.32 SIDE CHAIN
REMARK 500 13 ARG B 20 0.25 SIDE CHAIN
REMARK 500 14 ARG A 20 0.15 SIDE CHAIN
REMARK 500 14 ARG B 20 0.12 SIDE CHAIN
REMARK 500 15 ARG A 20 0.29 SIDE CHAIN
REMARK 500 15 ARG B 20 0.31 SIDE CHAIN
REMARK 500 16 ARG B 20 0.25 SIDE CHAIN
REMARK 500 17 ARG A 20 0.25 SIDE CHAIN
REMARK 500 17 ARG B 20 0.29 SIDE CHAIN
REMARK 500 18 ARG A 20 0.21 SIDE CHAIN
REMARK 500 18 ARG B 20 0.29 SIDE CHAIN
REMARK 500 19 ARG A 20 0.21 SIDE CHAIN
REMARK 500 19 ARG B 20 0.11 SIDE CHAIN
REMARK 500 20 ARG A 20 0.30 SIDE CHAIN
REMARK 500 20 ARG B 20 0.17 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: CA1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: PSEUDO EF-HAND CALCIUM-BINDING SITE MONOMER A.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA3
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: PSEUDO EF-HAND CALCIUM-BINDING SITE MONOMER B.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CANONICAL EF-HAND CALCIUM-BINDING SITE MONOMER
REMARK 800 A.
REMARK 800
REMARK 800 SITE_IDENTIFIER: CA4
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: CANONICAL EF-HAND CALCIUM-BINDING SITE MONOMER
REMARK 800 B.
DBREF 1UWO A 1 91 UNP P04271 S100B_HUMAN 1 91
DBREF 1UWO B 1 91 UNP P04271 S100B_HUMAN 1 91
SEQRES 1 A 91 SER GLU LEU GLU LYS ALA MET VAL ALA LEU ILE ASP VAL
SEQRES 2 A 91 PHE HIS GLN TYR SER GLY ARG GLU GLY ASP LYS HIS LYS
SEQRES 3 A 91 LEU LYS LYS SER GLU LEU LYS GLU LEU ILE ASN ASN GLU
SEQRES 4 A 91 LEU SER HIS PHE LEU GLU GLU ILE LYS GLU GLN GLU VAL
SEQRES 5 A 91 VAL ASP LYS VAL MET GLU THR LEU ASP ASN ASP GLY ASP
SEQRES 6 A 91 GLY GLU CYS ASP PHE GLN GLU PHE MET ALA PHE VAL ALA
SEQRES 7 A 91 MET VAL THR THR ALA CYS HIS GLU PHE PHE GLU HIS GLU
SEQRES 1 B 91 SER GLU LEU GLU LYS ALA MET VAL ALA LEU ILE ASP VAL
SEQRES 2 B 91 PHE HIS GLN TYR SER GLY ARG GLU GLY ASP LYS HIS LYS
SEQRES 3 B 91 LEU LYS LYS SER GLU LEU LYS GLU LEU ILE ASN ASN GLU
SEQRES 4 B 91 LEU SER HIS PHE LEU GLU GLU ILE LYS GLU GLN GLU VAL
SEQRES 5 B 91 VAL ASP LYS VAL MET GLU THR LEU ASP ASN ASP GLY ASP
SEQRES 6 B 91 GLY GLU CYS ASP PHE GLN GLU PHE MET ALA PHE VAL ALA
SEQRES 7 B 91 MET VAL THR THR ALA CYS HIS GLU PHE PHE GLU HIS GLU
HELIX 1 1 GLU A 2 GLY A 19 1 18
HELIX 2 2 LYS A 29 ASN A 38 5 10
HELIX 3 3 VAL A 52 THR A 59 1 8
HELIX 4 4 PHE A 70 PHE A 88 1 19
HELIX 5 5 GLU B 2 GLY B 19 1 18
HELIX 6 6 LYS B 29 ASN B 38 1 10
HELIX 7 7 VAL B 52 THR B 59 1 8
HELIX 8 8 PHE B 70 PHE B 88 1 19
SITE 1 CA1 6 SER A 18 GLU A 21 ASP A 23 LYS A 26
SITE 2 CA1 6 LYS A 28 GLU A 31
SITE 1 CA3 6 SER B 18 GLU B 21 ASP B 23 LYS B 26
SITE 2 CA3 6 LYS B 28 GLU B 31
SITE 1 CA2 6 ASP A 61 ASP A 63 ASP A 65 GLU A 67
SITE 2 CA2 6 ASP A 69 GLU A 72
SITE 1 CA4 6 ASP B 61 ASP B 63 ASP B 65 GLU B 67
SITE 2 CA4 6 ASP B 69 GLU B 72
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
(ATOM LINES ARE NOT SHOWN.)
END