HEADER METAL BINDING PROTEIN 17-AUG-08 2K7O
TITLE CA2+-S100B, REFINED WITH RDCS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN S100-B;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: S100 CALCIUM-BINDING PROTEIN B, S-100 PROTEIN SUBUNIT BETA,
COMPND 5 S-100 PROTEIN BETA CHAIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: S100B;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET 11A
KEYWDS S100 PROTEIN, CALCIUM BINDING, EF-HAND, CALCIUM, CYTOPLASM, METAL-
KEYWDS 2 BINDING, NUCLEUS, ZINC, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.T.WRIGHT,K.G.INMAN,J.A.LEVINE,D.J.WEBER
REVDAT 3 16-MAR-22 2K7O 1 REMARK LINK
REVDAT 2 24-FEB-09 2K7O 1 VERSN
REVDAT 1 18-NOV-08 2K7O 0
JRNL AUTH N.T.WRIGHT,K.G.INMAN,J.A.LEVINE,B.R.CANNON,K.M.VARNEY,
JRNL AUTH 2 D.J.WEBER
JRNL TITL REFINEMENT OF THE SOLUTION STRUCTURE AND DYNAMIC PROPERTIES
JRNL TITL 2 OF CA(2+)-BOUND RAT S100B.
JRNL REF J.BIOMOL.NMR V. 42 279 2008
JRNL REFN ISSN 0925-2738
JRNL PMID 18949447
JRNL DOI 10.1007/S10858-008-9282-Y
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR NIH, X-PLOR NIH
REMARK 3 AUTHORS : SCHWIETERS, KUSZEWSKI, TJANDRA AND CLORE (X-PLOR
REMARK 3 NIH), SCHWIETERS, KUSZEWSKI, TJANDRA AND CLORE (X-
REMARK 3 PLOR NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2K7O COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-AUG-08.
REMARK 100 THE DEPOSITION ID IS D_1000100779.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 6.7
REMARK 210 IONIC STRENGTH : 50
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 400 UM [U-15N] S100B, 10 MM
REMARK 210 CACL2, 25 MM NACL, 10 MM [U-99%
REMARK 210 2H] MES, PH 6.7, 10 MM DTT, .1
REMARK 210 MM NAN3, 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : IPAP; HNCOCA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR NIH
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: 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 O PHE A 14 H SER A 18 1.46
REMARK 500 O PHE B 14 H SER B 18 1.47
REMARK 500 O ALA B 75 H MET B 79 1.51
REMARK 500 O ALA A 75 H MET A 79 1.52
REMARK 500 O VAL A 53 H MET A 57 1.60
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 1 HIS A 25 39.13 78.33
REMARK 500 1 GLU A 39 -74.96 -88.03
REMARK 500 1 SER A 41 -33.50 -145.46
REMARK 500 1 GLU A 45 -109.41 -125.08
REMARK 500 1 GLU A 46 -142.35 47.29
REMARK 500 1 HIS B 25 39.83 78.47
REMARK 500 1 GLU B 39 -75.37 -88.58
REMARK 500 1 SER B 41 -33.88 -144.80
REMARK 500 1 GLU B 45 -109.94 -125.28
REMARK 500 1 GLU B 46 -141.98 48.14
REMARK 500 2 LYS A 26 97.39 -169.68
REMARK 500 2 GLU A 39 -71.62 -84.01
REMARK 500 2 SER A 41 -48.54 -135.47
REMARK 500 2 GLU A 45 -133.69 -171.34
REMARK 500 2 LYS A 48 -79.53 -89.96
REMARK 500 2 LYS B 26 97.52 -169.80
REMARK 500 2 GLU B 39 -71.31 -83.99
REMARK 500 2 SER B 41 -48.33 -135.79
REMARK 500 2 GLU B 45 -133.58 -171.25
REMARK 500 2 LYS B 48 -79.47 -89.97
REMARK 500 3 GLU A 39 -75.27 -87.18
REMARK 500 3 SER A 41 -33.56 -147.29
REMARK 500 3 LEU A 44 -89.84 -110.08
REMARK 500 3 PHE A 87 95.38 -170.72
REMARK 500 3 PHE A 88 -76.93 -89.72
REMARK 500 3 GLU A 89 -130.06 40.72
REMARK 500 3 GLU B 39 -75.00 -86.81
REMARK 500 3 SER B 41 -33.00 -147.96
REMARK 500 3 LEU B 44 -89.99 -110.01
REMARK 500 3 PHE B 87 95.51 -170.37
REMARK 500 3 PHE B 88 -76.81 -89.75
REMARK 500 3 GLU B 89 -130.05 40.30
REMARK 500 4 HIS A 25 33.94 75.69
REMARK 500 4 GLU A 39 -75.11 -87.96
REMARK 500 4 SER A 41 -56.17 -124.94
REMARK 500 4 ASP A 61 48.69 -79.11
REMARK 500 4 ASP A 65 -29.23 -142.32
REMARK 500 4 HIS B 25 32.83 75.99
REMARK 500 4 GLU B 39 -74.80 -86.83
REMARK 500 4 SER B 41 -56.06 -125.14
REMARK 500 4 ASP B 61 49.70 -79.44
REMARK 500 4 ASP B 65 -28.88 -142.64
REMARK 500 5 ASP A 23 -140.29 48.85
REMARK 500 5 LYS A 24 -39.00 -131.17
REMARK 500 5 GLU A 39 -75.15 -88.45
REMARK 500 5 SER A 41 -49.57 -140.48
REMARK 500 5 LYS A 48 -72.23 -94.64
REMARK 500 5 ASP B 23 -140.09 48.82
REMARK 500 5 LYS B 24 -39.07 -131.31
REMARK 500 5 GLU B 39 -75.17 -88.74
REMARK 500
REMARK 500 THIS ENTRY HAS 207 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 101 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 18 O
REMARK 620 2 GLU A 21 O 96.9
REMARK 620 3 LYS A 26 O 141.5 115.1
REMARK 620 4 GLU A 31 OE2 91.8 110.7 95.9
REMARK 620 5 GLU A 31 OE1 138.9 87.6 66.9 49.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 103 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 61 OD1
REMARK 620 2 ASP A 63 OD1 133.0
REMARK 620 3 ASP A 65 OD2 109.7 84.4
REMARK 620 4 ASP A 65 OD1 84.3 74.3 45.9
REMARK 620 5 GLU A 67 O 59.3 131.2 53.4 59.2
REMARK 620 6 GLU A 72 OE2 147.8 74.9 85.5 123.9 118.5
REMARK 620 7 GLU A 72 OE1 108.7 81.0 138.4 154.4 146.4 53.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 102 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 18 O
REMARK 620 2 GLU B 21 O 97.9
REMARK 620 3 LYS B 26 O 123.3 128.0
REMARK 620 4 GLU B 31 OE2 84.5 121.7 94.8
REMARK 620 5 GLU B 31 OE1 135.3 103.4 70.3 50.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 104 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 61 OD1
REMARK 620 2 ASP B 63 OD1 140.5
REMARK 620 3 ASP B 65 OD2 111.1 89.5
REMARK 620 4 ASP B 65 OD1 88.1 81.9 47.2
REMARK 620 5 GLU B 67 O 61.4 137.4 51.6 59.7
REMARK 620 6 GLU B 72 OE2 137.1 75.9 84.3 126.6 111.2
REMARK 620 7 GLU B 72 OE1 103.7 82.2 133.6 164.1 135.5 49.3
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 102
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 103
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 104
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1QLK RELATED DB: PDB
REMARK 900 CA2+-S100B, NO RDC
REMARK 900 RELATED ID: 1B4C RELATED DB: PDB
REMARK 900 APO-S100B
DBREF 2K7O A 1 91 UNP P04631 S100B_RAT 2 92
DBREF 2K7O B 1 91 UNP P04631 S100B_RAT 2 92
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 GLU ASP GLY ASP
SEQRES 6 A 91 GLY GLU CYS ASP PHE GLN GLU PHE MET ALA PHE VAL SER
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 GLU ASP GLY ASP
SEQRES 6 B 91 GLY GLU CYS ASP PHE GLN GLU PHE MET ALA PHE VAL SER
SEQRES 7 B 91 MET VAL THR THR ALA CYS HIS GLU PHE PHE GLU HIS GLU
HET CA A 101 1
HET CA A 103 1
HET CA B 102 1
HET CA B 104 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 4(CA 2+)
HELIX 1 1 SER A 1 GLY A 19 1 19
HELIX 2 2 LYS A 28 GLU A 39 1 12
HELIX 3 3 GLU A 49 ASP A 61 1 13
HELIX 4 4 ASP A 69 CYS A 84 1 16
HELIX 5 5 SER B 1 GLY B 19 1 19
HELIX 6 6 LYS B 28 GLU B 39 1 12
HELIX 7 7 GLU B 49 ASP B 61 1 13
HELIX 8 8 ASP B 69 CYS B 84 1 16
LINK O SER A 18 CA CA A 101 1555 1555 2.40
LINK O GLU A 21 CA CA A 101 1555 1555 2.98
LINK O LYS A 26 CA CA A 101 1555 1555 2.76
LINK OE2 GLU A 31 CA CA A 101 1555 1555 2.66
LINK OE1 GLU A 31 CA CA A 101 1555 1555 2.51
LINK OD1 ASP A 61 CA CA A 103 1555 1555 2.81
LINK OD1 ASP A 63 CA CA A 103 1555 1555 2.76
LINK OD2 ASP A 65 CA CA A 103 1555 1555 2.99
LINK OD1 ASP A 65 CA CA A 103 1555 1555 2.27
LINK O GLU A 67 CA CA A 103 1555 1555 2.67
LINK OE2 GLU A 72 CA CA A 103 1555 1555 2.36
LINK OE1 GLU A 72 CA CA A 103 1555 1555 2.46
LINK O SER B 18 CA CA B 102 1555 1555 2.76
LINK O GLU B 21 CA CA B 102 1555 1555 2.63
LINK O LYS B 26 CA CA B 102 1555 1555 2.76
LINK OE2 GLU B 31 CA CA B 102 1555 1555 2.69
LINK OE1 GLU B 31 CA CA B 102 1555 1555 2.22
LINK OD1 ASP B 61 CA CA B 104 1555 1555 2.87
LINK OD1 ASP B 63 CA CA B 104 1555 1555 2.58
LINK OD2 ASP B 65 CA CA B 104 1555 1555 2.94
LINK OD1 ASP B 65 CA CA B 104 1555 1555 2.02
LINK O GLU B 67 CA CA B 104 1555 1555 2.71
LINK OE2 GLU B 72 CA CA B 104 1555 1555 2.54
LINK OE1 GLU B 72 CA CA B 104 1555 1555 2.62
SITE 1 AC1 5 SER A 18 GLU A 21 ASP A 23 LYS A 26
SITE 2 AC1 5 GLU A 31
SITE 1 AC2 5 SER B 18 GLU B 21 ASP B 23 LYS B 26
SITE 2 AC2 5 GLU B 31
SITE 1 AC3 5 ASP A 61 ASP A 63 ASP A 65 GLU A 67
SITE 2 AC3 5 GLU A 72
SITE 1 AC4 5 ASP B 61 ASP B 63 ASP B 65 GLU B 67
SITE 2 AC4 5 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