Header list of 1sym.pdb file
Complete list - r 2 2 Bytes
HEADER CALCIUM-BINDING PROTEIN 29-MAY-96 1SYM
TITLE 3-D SOLUTION STRUCTURE OF REDUCED APO-S100B FROM RAT, NMR, 20
TITLE 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: S100B;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: S100B(BETABETA), S100BETA, S100(BETABETA);
COMPND 5 ENGINEERED: YES;
COMPND 6 OTHER_DETAILS: SYMMETRIC DIMER OF APO-S100BETA SUBUNITS, JOINED BY
COMPND 7 NONCOVALENT INTERACTION AT THE DIMER INTERFACE
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: NORWAY RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: S100BETA FROM RATTUS NORVEGICU;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HMS174;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET11B;
SOURCE 10 EXPRESSION_SYSTEM_GENE: S100BETA FROM RATTUS NORVEGICUS
KEYWDS METAL-BINDING, CALCIUM-BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR A.C.DROHAT,D.J.WEBER
REVDAT 3 02-MAR-22 1SYM 1 REMARK
REVDAT 2 24-FEB-09 1SYM 1 VERSN
REVDAT 1 07-DEC-96 1SYM 0
JRNL AUTH A.C.DROHAT,J.C.AMBURGEY,F.ABILDGAARD,M.R.STARICH,
JRNL AUTH 2 D.BALDISSERI,D.J.WEBER
JRNL TITL SOLUTION STRUCTURE OF RAT APO-S100B(BETA BETA) AS DETERMINED
JRNL TITL 2 BY NMR SPECTROSCOPY.
JRNL REF BIOCHEMISTRY V. 35 11577 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8794737
JRNL DOI 10.1021/BI9612226
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.C.AMBURGEY,F.ABILDGAARD,M.R.STARICH,S.SHAH,D.C.HILT,
REMARK 1 AUTH 2 D.J.WEBER
REMARK 1 TITL 1H, 13C AND 15N NMR ASSIGNMENTS AND SOLUTION SECONDARY
REMARK 1 TITL 2 STRUCTURE OF RAT APO-S100 BETA
REMARK 1 REF J.BIOMOL.NMR V. 6 171 1995
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: NULL
REMARK 4
REMARK 4 1SYM 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_1000176569.
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 : 20
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: 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 GLN A 16 -77.94 -95.17
REMARK 500 1 LYS A 24 20.94 -140.23
REMARK 500 1 HIS A 25 17.78 -153.95
REMARK 500 1 LEU A 40 -101.49 -73.68
REMARK 500 1 SER A 41 88.77 39.43
REMARK 500 1 HIS A 42 -59.56 -167.11
REMARK 500 1 GLU A 45 -78.05 -130.34
REMARK 500 1 ILE A 47 88.78 61.03
REMARK 500 1 ASP A 63 -60.34 -94.58
REMARK 500 1 ASP A 65 -7.54 -143.83
REMARK 500 1 ASP A 69 -163.60 -102.02
REMARK 500 1 HIS A 90 71.49 -119.33
REMARK 500 1 GLN B 16 -77.71 -95.27
REMARK 500 1 LYS B 24 20.79 -140.09
REMARK 500 1 HIS B 25 17.68 -153.93
REMARK 500 1 LEU B 40 -101.51 -73.75
REMARK 500 1 SER B 41 88.79 39.36
REMARK 500 1 HIS B 42 -59.66 -167.07
REMARK 500 1 GLU B 45 -78.12 -130.41
REMARK 500 1 ILE B 47 88.80 61.11
REMARK 500 1 ASP B 63 -60.44 -94.53
REMARK 500 1 ASP B 65 -7.53 -143.90
REMARK 500 1 ASP B 69 -163.59 -102.01
REMARK 500 1 HIS B 90 71.44 -119.16
REMARK 500 2 TYR A 17 33.02 -159.61
REMARK 500 2 GLU A 21 -158.10 -125.68
REMARK 500 2 LEU A 27 -158.29 -96.89
REMARK 500 2 SER A 41 97.23 -39.25
REMARK 500 2 HIS A 42 -34.04 -179.59
REMARK 500 2 GLU A 45 -75.18 -125.91
REMARK 500 2 ILE A 47 82.17 66.37
REMARK 500 2 ALA A 83 -71.63 -49.15
REMARK 500 2 CYS A 84 43.39 174.28
REMARK 500 2 GLU A 86 55.11 -95.35
REMARK 500 2 GLU A 89 -70.86 -111.35
REMARK 500 2 HIS A 90 24.55 -154.96
REMARK 500 2 TYR B 17 32.97 -159.57
REMARK 500 2 GLU B 21 -157.99 -125.65
REMARK 500 2 LEU B 27 -158.25 -96.87
REMARK 500 2 SER B 41 97.18 -39.20
REMARK 500 2 HIS B 42 -34.03 -179.58
REMARK 500 2 GLU B 45 -75.11 -125.89
REMARK 500 2 ILE B 47 82.28 66.39
REMARK 500 2 ALA B 83 -71.60 -49.24
REMARK 500 2 CYS B 84 43.38 174.31
REMARK 500 2 GLU B 86 55.22 -95.43
REMARK 500 2 GLU B 89 -70.91 -111.26
REMARK 500 2 HIS B 90 24.53 -154.85
REMARK 500 3 GLU A 21 -163.19 41.30
REMARK 500 3 ASP A 23 -95.59 -57.55
REMARK 500
REMARK 500 THIS ENTRY HAS 552 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 0.19 SIDE CHAIN
REMARK 500 1 ARG B 20 0.19 SIDE CHAIN
REMARK 500 2 ARG A 20 0.22 SIDE CHAIN
REMARK 500 2 ARG B 20 0.22 SIDE CHAIN
REMARK 500 3 ARG A 20 0.25 SIDE CHAIN
REMARK 500 3 ARG B 20 0.25 SIDE CHAIN
REMARK 500 4 ARG A 20 0.32 SIDE CHAIN
REMARK 500 4 ARG B 20 0.32 SIDE CHAIN
REMARK 500 5 ARG A 20 0.24 SIDE CHAIN
REMARK 500 5 ARG B 20 0.24 SIDE CHAIN
REMARK 500 6 ARG A 20 0.31 SIDE CHAIN
REMARK 500 6 ARG B 20 0.31 SIDE CHAIN
REMARK 500 7 ARG A 20 0.21 SIDE CHAIN
REMARK 500 7 ARG B 20 0.21 SIDE CHAIN
REMARK 500 9 ARG A 20 0.17 SIDE CHAIN
REMARK 500 9 ARG B 20 0.17 SIDE CHAIN
REMARK 500 10 ARG A 20 0.31 SIDE CHAIN
REMARK 500 10 ARG B 20 0.31 SIDE CHAIN
REMARK 500 11 ARG A 20 0.31 SIDE CHAIN
REMARK 500 11 ARG B 20 0.31 SIDE CHAIN
REMARK 500 12 ARG A 20 0.23 SIDE CHAIN
REMARK 500 12 ARG B 20 0.23 SIDE CHAIN
REMARK 500 13 ARG A 20 0.32 SIDE CHAIN
REMARK 500 13 ARG B 20 0.32 SIDE CHAIN
REMARK 500 14 ARG A 20 0.26 SIDE CHAIN
REMARK 500 14 ARG B 20 0.26 SIDE CHAIN
REMARK 500 15 ARG A 20 0.20 SIDE CHAIN
REMARK 500 15 ARG B 20 0.19 SIDE CHAIN
REMARK 500 16 ARG A 20 0.27 SIDE CHAIN
REMARK 500 16 ARG B 20 0.27 SIDE CHAIN
REMARK 500 17 ARG A 20 0.27 SIDE CHAIN
REMARK 500 17 ARG B 20 0.27 SIDE CHAIN
REMARK 500 18 ARG A 20 0.27 SIDE CHAIN
REMARK 500 18 ARG B 20 0.27 SIDE CHAIN
REMARK 500 19 ARG A 20 0.28 SIDE CHAIN
REMARK 500 19 ARG B 20 0.28 SIDE CHAIN
REMARK 500 20 ARG A 20 0.32 SIDE CHAIN
REMARK 500 20 ARG B 20 0.32 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1SYM A 1 91 UNP P04631 S100B_RAT 1 91
DBREF 1SYM B 1 91 UNP P04631 S100B_RAT 1 91
SEQRES 1 A 92 MET SER GLU LEU GLU LYS ALA MET VAL ALA LEU ILE ASP
SEQRES 2 A 92 VAL PHE HIS GLN TYR SER GLY ARG GLU GLY ASP LYS HIS
SEQRES 3 A 92 LYS LEU LYS LYS SER GLU LEU LYS GLU LEU ILE ASN ASN
SEQRES 4 A 92 GLU LEU SER HIS PHE LEU GLU GLU ILE LYS GLU GLN GLU
SEQRES 5 A 92 VAL VAL ASP LYS VAL MET GLU THR LEU ASP GLU ASP GLY
SEQRES 6 A 92 ASP GLY GLU CYS ASP PHE GLN GLU PHE MET ALA PHE VAL
SEQRES 7 A 92 SER MET VAL THR THR ALA CYS HIS GLU PHE PHE GLU HIS
SEQRES 8 A 92 GLU
SEQRES 1 B 92 MET SER GLU LEU GLU LYS ALA MET VAL ALA LEU ILE ASP
SEQRES 2 B 92 VAL PHE HIS GLN TYR SER GLY ARG GLU GLY ASP LYS HIS
SEQRES 3 B 92 LYS LEU LYS LYS SER GLU LEU LYS GLU LEU ILE ASN ASN
SEQRES 4 B 92 GLU LEU SER HIS PHE LEU GLU GLU ILE LYS GLU GLN GLU
SEQRES 5 B 92 VAL VAL ASP LYS VAL MET GLU THR LEU ASP GLU ASP GLY
SEQRES 6 B 92 ASP GLY GLU CYS ASP PHE GLN GLU PHE MET ALA PHE VAL
SEQRES 7 B 92 SER MET VAL THR THR ALA CYS HIS GLU PHE PHE GLU HIS
SEQRES 8 B 92 GLU
HELIX 1 1 GLU A 2 TYR A 17 1 16
HELIX 2 2 LYS A 29 ASN A 38 1 10
HELIX 3 3 GLN A 50 ASP A 63 1 14
HELIX 4 4 PHE A 70 THR A 82 1 13
HELIX 5 5 GLU B 2 TYR B 17 1 16
HELIX 6 6 LYS B 29 ASN B 38 1 10
HELIX 7 7 GLN B 50 ASP B 63 1 14
HELIX 8 8 PHE B 70 THR B 82 1 13
SHEET 1 S1 2 LYS A 26 LYS A 28 0
SHEET 2 S1 2 GLU A 67 ASP A 69 -1 N CYS A 68 O LEU A 27
SHEET 1 S2 2 LYS B 26 LYS B 28 0
SHEET 2 S2 2 GLU B 67 ASP B 69 -1 N CYS B 68 O LEU B 27
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 - r 2 2 Bytes