HEADER METAL BINDING PROTEIN 27-SEP-01 1K2H
TITLE THREE-DIMENSIONAL SOLUTION STRUCTURE OF APO-S100A1.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: S-100 PROTEIN, ALPHA CHAIN;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: S100A1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: HMS174(DE3);
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-11B
KEYWDS NON-COVALENT HOMODIMER, X-TYPE FOUR-HELIX BUNDLE, METAL BINDING
KEYWDS 2 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR R.R.RUSTANDI,D.M.BALDISSERI,K.G.INMAN,P.NIZNER,S.M.HAMILTON,A.LANDAR,
AUTHOR 2 A.LANDAR,D.B.ZIMMER,D.J.WEBER
REVDAT 4 01-FEB-17 1K2H 1 AUTHOR VERSN
REVDAT 3 24-FEB-09 1K2H 1 VERSN
REVDAT 2 01-APR-03 1K2H 1 JRNL
REVDAT 1 13-FEB-02 1K2H 0
JRNL AUTH R.R.RUSTANDI,D.M.BALDISSERI,K.G.INMAN,P.NIZNER,S.M.HAMILTON,
JRNL AUTH 2 A.LANDAR,A.LANDAR,D.B.ZIMMER,D.J.WEBER
JRNL TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE
JRNL TITL 2 CALCIUM-SIGNALING PROTEIN APO-S100A1 AS DETERMINED BY NMR.
JRNL REF BIOCHEMISTRY V. 41 788 2002
JRNL REFN ISSN 0006-2960
JRNL PMID 11790100
JRNL DOI 10.1021/BI0118308
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CHARMM
REMARK 3 AUTHORS : HARVARD UNIVERSITY
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1K2H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-OCT-01.
REMARK 100 THE RCSB ID CODE IS RCSB014477.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 6.4
REMARK 210 IONIC STRENGTH : 25MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : SAMPLE 1: S100A1, U-15N; 12-15MM
REMARK 210 D11-TRIS, 1-2MM EGTA, 0.3MM NAN3,
REMARK 210 15-18MM NACL; PH 6.4, 95% H2O, 5%
REMARK 210 D2O. SAMPLE 2: S100A1, U-13C,15N;
REMARK 210 12-15MM D11-TRIS, 1-2MM EGTA,
REMARK 210 0.3MM NAN3, 15-18MM NACL; PH 6.4,
REMARK 210 95% H2O, 5% D2O.; S100A1, U-13C,
REMARK 210 15N; 12-15MM D11-TRIS, 1-2MM
REMARK 210 EGTA, 0.3MM NAN3, 15-18MM NACL;
REMARK 210 PH 6.4, 95% H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNHA;
REMARK 210 2D_1H-15N_HSQC; 3D_15N_SEPARATED_
REMARK 210 HOHAHA; 4D_13C-SEPARATED_NOESY;
REMARK 210 3D_HNCACB
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.6, NMRPIPE 1.8, X-PLOR
REMARK 210 3.851, CHARMM
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, DOCKING, MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 75
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 17
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING CONSTRAINTS GENERATED
REMARK 210 FROM HETERONUCLEAR, MULTI-DIMENSIONAL NMR EXPERIMENTS.
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 HE21 GLN A 72 HA ALA B 80 1.24
REMARK 500 HA ALA A 80 HE21 GLN B 72 1.26
REMARK 500 HG SER A 2 H GLU A 5 1.29
REMARK 500 HG SER B 2 H GLU B 5 1.33
REMARK 500 H LYS A 49 O ALA A 84 1.36
REMARK 500 H LYS B 49 O ALA B 84 1.36
REMARK 500 O PHE A 89 H GLU A 91 1.46
REMARK 500 O PHE B 89 H GLU B 91 1.46
REMARK 500 O LEU B 41 H PHE B 44 1.52
REMARK 500 O LEU A 41 H PHE A 44 1.52
REMARK 500 O ASN A 64 H GLY A 67 1.52
REMARK 500 O ASN B 64 H GLY B 67 1.52
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 GLU A 22 -21.25 85.62
REMARK 500 1 TYR A 26 172.99 -50.01
REMARK 500 1 LEU A 28 -176.06 81.61
REMARK 500 1 LEU A 41 39.24 -86.40
REMARK 500 1 VAL A 47 87.08 -166.24
REMARK 500 1 LYS A 49 -81.02 -108.97
REMARK 500 1 ASN A 64 56.76 -151.65
REMARK 500 1 ASP A 70 -154.74 -128.24
REMARK 500 1 ASN A 86 -0.55 -57.59
REMARK 500 1 TRP A 90 41.61 -63.63
REMARK 500 1 GLU B 22 -21.02 85.02
REMARK 500 1 TYR B 26 173.16 -49.96
REMARK 500 1 LEU B 28 -176.24 81.51
REMARK 500 1 LEU B 41 39.47 -86.76
REMARK 500 1 VAL B 47 87.16 -166.38
REMARK 500 1 LYS B 49 -80.89 -108.85
REMARK 500 1 ASN B 64 56.42 -151.56
REMARK 500 1 ASP B 70 -154.67 -128.24
REMARK 500 1 ASN B 86 -0.50 -57.83
REMARK 500 1 TRP B 90 40.86 -63.82
REMARK 500 2 TYR A 26 175.27 -49.30
REMARK 500 2 LYS A 27 -79.85 -57.63
REMARK 500 2 LEU A 28 -177.06 -173.48
REMARK 500 2 LEU A 41 33.02 -96.20
REMARK 500 2 ASN A 64 58.06 -155.35
REMARK 500 2 ASP A 70 -152.88 -128.84
REMARK 500 2 ASN A 86 56.24 -63.44
REMARK 500 2 PHE A 88 -69.92 -147.62
REMARK 500 2 TRP A 90 41.87 -94.60
REMARK 500 2 TYR B 26 175.02 -49.17
REMARK 500 2 LYS B 27 -80.37 -57.34
REMARK 500 2 LEU B 28 -177.12 -173.05
REMARK 500 2 LEU B 41 32.66 -96.17
REMARK 500 2 LYS B 49 -70.05 -80.47
REMARK 500 2 ASN B 64 58.03 -155.31
REMARK 500 2 ASP B 70 -152.84 -128.73
REMARK 500 2 ASN B 86 56.24 -63.52
REMARK 500 2 PHE B 88 -70.07 -147.44
REMARK 500 2 TRP B 90 41.10 -94.48
REMARK 500 3 LYS A 27 -80.33 -67.28
REMARK 500 3 LEU A 28 -178.20 -173.18
REMARK 500 3 VAL A 47 88.01 -152.09
REMARK 500 3 ASN A 64 45.59 -145.50
REMARK 500 3 ASP A 70 -158.44 -127.54
REMARK 500 3 ASN A 86 35.63 -67.42
REMARK 500 3 LYS B 27 -80.97 -68.35
REMARK 500 3 LEU B 28 -178.81 -171.23
REMARK 500 3 LEU B 41 32.84 -99.53
REMARK 500 3 VAL B 47 89.32 -151.84
REMARK 500 3 ASN B 64 45.41 -145.94
REMARK 500
REMARK 500 THIS ENTRY HAS 350 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR
REMARK 700
REMARK 700 SHEET
REMARK 700 DETERMINATION METHOD: AUTHOR
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4285 RELATED DB: BMRB
DBREF 1K2H A 1 93 UNP P35467 S10A1_RAT 1 93
DBREF 1K2H B 1 93 UNP P35467 S10A1_RAT 1 93
SEQRES 1 A 93 GLY SER GLU LEU GLU THR ALA MET GLU THR LEU ILE ASN
SEQRES 2 A 93 VAL PHE HIS ALA HIS SER GLY LYS GLU GLY ASP LYS TYR
SEQRES 3 A 93 LYS LEU SER LYS LYS GLU LEU LYS ASP LEU LEU GLN THR
SEQRES 4 A 93 GLU LEU SER SER PHE LEU ASP VAL GLN LYS ASP ALA ASP
SEQRES 5 A 93 ALA VAL ASP LYS ILE MET LYS GLU LEU ASP GLU ASN GLY
SEQRES 6 A 93 ASP GLY GLU VAL ASP PHE GLN GLU PHE VAL VAL LEU VAL
SEQRES 7 A 93 ALA ALA LEU THR VAL ALA CYS ASN ASN PHE PHE TRP GLU
SEQRES 8 A 93 ASN SER
SEQRES 1 B 93 GLY SER GLU LEU GLU THR ALA MET GLU THR LEU ILE ASN
SEQRES 2 B 93 VAL PHE HIS ALA HIS SER GLY LYS GLU GLY ASP LYS TYR
SEQRES 3 B 93 LYS LEU SER LYS LYS GLU LEU LYS ASP LEU LEU GLN THR
SEQRES 4 B 93 GLU LEU SER SER PHE LEU ASP VAL GLN LYS ASP ALA ASP
SEQRES 5 B 93 ALA VAL ASP LYS ILE MET LYS GLU LEU ASP GLU ASN GLY
SEQRES 6 B 93 ASP GLY GLU VAL ASP PHE GLN GLU PHE VAL VAL LEU VAL
SEQRES 7 B 93 ALA ALA LEU THR VAL ALA CYS ASN ASN PHE PHE TRP GLU
SEQRES 8 B 93 ASN SER
HELIX 1 1 GLU A 3 ALA A 17 1 15
HELIX 2 2 LYS A 30 GLN A 38 1 9
HELIX 3 3 ALA A 51 LEU A 61 1 11
HELIX 4 4 PHE A 71 ALA A 84 1 14
HELIX 5 5 GLU B 3 ALA B 17 1 15
HELIX 6 6 LYS B 30 GLN B 38 1 9
HELIX 7 7 ALA B 51 LEU B 61 1 11
HELIX 8 8 PHE B 71 ALA B 84 1 14
SHEET 1 A 2 LYS A 27 SER A 29 0
SHEET 2 A 2 GLU A 68 ASP A 70 -1 N VAL A 69 O LEU A 28
SHEET 1 B 2 LYS B 27 SER B 29 0
SHEET 2 B 2 GLU B 68 ASP B 70 -1 N VAL B 69 O LEU B 28
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
