Header list of 1cfp.pdb file
Complete list - b 16 2 Bytes
HEADER CALCIUM-BINDING PROTEIN 04-JUN-96 1CFP
TITLE S100B (S100BETA) NMR DATA WAS COLLECTED FROM A SAMPLE OF CALCIUM FREE
TITLE 2 PROTEIN AT PH 6.3 AND A TEMPERATURE OF 311 K AND 1.7-6.9 MM
TITLE 3 CONCENTRATION, 25 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: S100B;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: S100BETA, S-100B;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 GENE: S100B;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-12A-S100B;
SOURCE 9 OTHER_DETAILS: THE GENE IS A SYNTHETIC DNA FOR THE BOVINE SEQUENCE
SOURCE 10 WITH ESCHERICHIA COLI CODON USAGE
KEYWDS HELIX-LOOP-HELIX, CALCIUM-BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR P.M.KILBY,L.J.VANELDIK,G.C.K.ROBERTS
REVDAT 3 16-FEB-22 1CFP 1 REMARK
REVDAT 2 24-FEB-09 1CFP 1 VERSN
REVDAT 1 12-MAR-97 1CFP 0
JRNL AUTH P.M.KILBY,L.J.VAN ELDIK,G.C.ROBERTS
JRNL TITL THE SOLUTION STRUCTURE OF THE BOVINE S100B PROTEIN DIMER IN
JRNL TITL 2 THE CALCIUM-FREE STATE.
JRNL REF STRUCTURE V. 4 1041 1996
JRNL REFN ISSN 0969-2126
JRNL PMID 8805590
JRNL DOI 10.1016/S0969-2126(96)00111-6
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 1CFP 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_1000172297.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 314
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D NOESY-HMQC; 3D TOCSY-HMQC; 3D
REMARK 210 HMQC-NOESY-HMQC; 2D DOUBLE
REMARK 210 QUANTUM FILTERED COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX 600; DMX 500
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.841
REMARK 210 METHOD USED : DISTANCE GEOMETRY-SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 91
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : TOTAL ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: S100B (S100BETA) NMR DATA WAS COLLECTED FROM A OF CALCIUM
REMARK 210 FREE PROTEIN AT PH 6.3 AND A TEMPERATURE OF 311 K AND 1.7-6.9 MM
REMARK 210 CONCENTRATION IONIC_STRENGTH : 20 MM SODIUM SUCCINATE PRESSURE :
REMARK 210 ATMOSPHERIC SOLVENT SYSTEM : 90% H2O : 10% D2O SOFTWARE
REMARK 210 PROGRAM(S) USED TO DETERMINE THE STRUCTURE : X-PLOR 3.841 METHOD
REMARK 210 USED TO DETERMINE THE STRUCTURE : DISTANCE GEOMETRY-SIMULATED
REMARK 210 ANNEALING
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 B 14 H SER B 18 1.48
REMARK 500 O PHE A 14 H SER A 18 1.48
REMARK 500 OD2 ASP B 54 HZ3 LYS B 55 1.49
REMARK 500 OD2 ASP A 54 HZ3 LYS A 55 1.50
REMARK 500 O GLU A 45 H ILE A 47 1.55
REMARK 500 OD1 ASP A 69 H PHE A 70 1.55
REMARK 500 OD1 ASP B 69 H PHE B 70 1.56
REMARK 500 O GLU B 45 H ILE B 47 1.56
REMARK 500 O SER A 41 H LEU A 44 1.58
REMARK 500 O SER B 41 H LEU B 44 1.59
REMARK 500 O GLU A 49 H VAL A 53 1.59
REMARK 500 O GLU B 49 H VAL B 53 1.59
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 SER A 1 -29.80 -35.31
REMARK 500 1 GLU A 21 -48.19 -144.00
REMARK 500 1 LYS A 24 -92.16 -88.49
REMARK 500 1 HIS A 25 56.62 -115.48
REMARK 500 1 GLU A 46 -58.61 64.93
REMARK 500 1 VAL A 56 -38.48 -39.60
REMARK 500 1 ASP A 65 82.41 44.49
REMARK 500 1 PHE A 70 -78.54 -25.62
REMARK 500 1 ALA A 75 -73.20 -72.62
REMARK 500 1 ILE A 80 -72.60 -72.38
REMARK 500 1 CYS A 84 -100.50 -90.62
REMARK 500 1 GLU A 86 -163.63 -172.01
REMARK 500 1 PHE A 88 103.20 -32.49
REMARK 500 1 HIS A 90 -76.57 62.66
REMARK 500 1 SER B 1 -29.95 -35.08
REMARK 500 1 GLU B 21 -48.42 -143.54
REMARK 500 1 LYS B 24 -92.16 -88.84
REMARK 500 1 HIS B 25 56.73 -115.31
REMARK 500 1 GLU B 46 -59.15 65.13
REMARK 500 1 VAL B 56 -38.57 -39.29
REMARK 500 1 ASP B 65 82.07 44.05
REMARK 500 1 PHE B 70 -78.34 -25.85
REMARK 500 1 GLN B 71 -9.77 -59.85
REMARK 500 1 ALA B 75 -72.57 -72.57
REMARK 500 1 ILE B 80 -72.91 -72.23
REMARK 500 1 CYS B 84 -100.84 -90.39
REMARK 500 1 GLU B 86 -163.20 -171.12
REMARK 500 1 PHE B 88 103.89 -33.49
REMARK 500 1 HIS B 90 -76.62 62.51
REMARK 500 2 ARG A 20 70.87 -63.50
REMARK 500 2 GLU A 21 122.58 58.10
REMARK 500 2 ASP A 23 -164.05 41.95
REMARK 500 2 LYS A 24 -82.42 -117.76
REMARK 500 2 HIS A 25 57.69 -109.69
REMARK 500 2 GLU A 46 -55.56 65.40
REMARK 500 2 ILE A 47 -30.86 -38.14
REMARK 500 2 ASP A 63 95.53 -37.65
REMARK 500 2 ASP A 65 125.13 -20.37
REMARK 500 2 PHE A 70 -81.94 -21.24
REMARK 500 2 CYS A 84 -95.37 -84.17
REMARK 500 2 HIS A 85 -147.65 -152.48
REMARK 500 2 GLU A 86 -158.46 54.36
REMARK 500 2 PHE A 88 108.01 -39.06
REMARK 500 2 GLU A 89 -150.30 -153.75
REMARK 500 2 ARG B 20 70.80 -64.16
REMARK 500 2 GLU B 21 122.51 58.21
REMARK 500 2 ASP B 23 -164.16 41.84
REMARK 500 2 LYS B 24 -82.37 -117.60
REMARK 500 2 HIS B 25 57.89 -109.96
REMARK 500 2 GLU B 46 -55.28 65.70
REMARK 500
REMARK 500 THIS ENTRY HAS 819 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 0.31 SIDE CHAIN
REMARK 500 1 ARG B 20 0.31 SIDE CHAIN
REMARK 500 2 ARG A 20 0.26 SIDE CHAIN
REMARK 500 2 ARG B 20 0.26 SIDE CHAIN
REMARK 500 3 ARG A 20 0.24 SIDE CHAIN
REMARK 500 3 ARG B 20 0.24 SIDE CHAIN
REMARK 500 4 ARG A 20 0.25 SIDE CHAIN
REMARK 500 4 ARG B 20 0.25 SIDE CHAIN
REMARK 500 5 ARG A 20 0.15 SIDE CHAIN
REMARK 500 5 ARG B 20 0.15 SIDE CHAIN
REMARK 500 6 ARG A 20 0.21 SIDE CHAIN
REMARK 500 6 ARG B 20 0.21 SIDE CHAIN
REMARK 500 7 ARG A 20 0.18 SIDE CHAIN
REMARK 500 7 ARG B 20 0.18 SIDE CHAIN
REMARK 500 8 ARG A 20 0.22 SIDE CHAIN
REMARK 500 8 ARG B 20 0.22 SIDE CHAIN
REMARK 500 9 ARG A 20 0.19 SIDE CHAIN
REMARK 500 9 ARG B 20 0.19 SIDE CHAIN
REMARK 500 10 ARG A 20 0.32 SIDE CHAIN
REMARK 500 10 ARG B 20 0.32 SIDE CHAIN
REMARK 500 11 ARG A 20 0.30 SIDE CHAIN
REMARK 500 11 ARG B 20 0.30 SIDE CHAIN
REMARK 500 12 ARG A 20 0.32 SIDE CHAIN
REMARK 500 12 ARG B 20 0.32 SIDE CHAIN
REMARK 500 14 ARG A 20 0.22 SIDE CHAIN
REMARK 500 14 ARG B 20 0.22 SIDE CHAIN
REMARK 500 15 ARG A 20 0.29 SIDE CHAIN
REMARK 500 15 ARG B 20 0.29 SIDE CHAIN
REMARK 500 16 ARG A 20 0.19 SIDE CHAIN
REMARK 500 16 ARG B 20 0.18 SIDE CHAIN
REMARK 500 17 ARG A 20 0.18 SIDE CHAIN
REMARK 500 17 ARG B 20 0.18 SIDE CHAIN
REMARK 500 19 ARG A 20 0.27 SIDE CHAIN
REMARK 500 19 ARG B 20 0.27 SIDE CHAIN
REMARK 500 20 ARG A 20 0.32 SIDE CHAIN
REMARK 500 20 ARG B 20 0.32 SIDE CHAIN
REMARK 500 21 ARG A 20 0.27 SIDE CHAIN
REMARK 500 21 ARG B 20 0.28 SIDE CHAIN
REMARK 500 22 ARG A 20 0.27 SIDE CHAIN
REMARK 500 22 ARG B 20 0.27 SIDE CHAIN
REMARK 500 23 ARG A 20 0.19 SIDE CHAIN
REMARK 500 23 ARG B 20 0.19 SIDE CHAIN
REMARK 500 24 ARG A 20 0.27 SIDE CHAIN
REMARK 500 24 ARG B 20 0.27 SIDE CHAIN
REMARK 500 25 ARG A 20 0.14 SIDE CHAIN
REMARK 500 25 ARG B 20 0.14 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: LOW AFFINITY HELIX-LOOP-HELIX CALCIUM BINDING
REMARK 800 LOOP.
REMARK 800
REMARK 800 SITE_IDENTIFIER: LOB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: HIGH AFFINITY HELIX-LOOP-HELIX CALCIUM BINDING
REMARK 800 LOOP.
REMARK 800
REMARK 800 SITE_IDENTIFIER: LOC
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: LOW AFFINITY HELIX-LOOP-HELIX CALCIUM BINDING
REMARK 800 LOOP.
REMARK 800
REMARK 800 SITE_IDENTIFIER: LOD
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: HIGH AFFINITY HELIX-LOOP-HELIX CALCIUM BINDING
REMARK 800 LOOP.
DBREF 1CFP A 1 91 UNP P02638 S100B_BOVIN 1 91
DBREF 1CFP B 1 91 UNP P02638 S100B_BOVIN 1 91
SEQRES 1 A 92 MET SER GLU LEU GLU LYS ALA VAL 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 SER ASP GLY
SEQRES 6 A 92 ASP GLY GLU CYS ASP PHE GLN GLU PHE MET ALA PHE VAL
SEQRES 7 A 92 ALA MET ILE 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 VAL 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 SER ASP GLY
SEQRES 6 B 92 ASP GLY GLU CYS ASP PHE GLN GLU PHE MET ALA PHE VAL
SEQRES 7 B 92 ALA MET ILE THR THR ALA CYS HIS GLU PHE PHE GLU HIS
SEQRES 8 B 92 GLU
HELIX 1 1A SER A 1 TYR A 17 1 17
HELIX 2 2A LYS A 29 GLU A 39 1 11
HELIX 3 3A SER A 41 GLU A 45 1 5
HELIX 4 4A GLN A 50 SER A 62 1 13
HELIX 5 5A PHE A 70 ALA A 83 1 14
HELIX 6 1B SER B 1 TYR B 17 1 17
HELIX 7 2B LYS B 29 GLU B 39 1 11
HELIX 8 3B SER B 41 GLU B 45 1 5
HELIX 9 4B GLN B 50 SER B 62 1 13
HELIX 10 5B PHE B 70 ALA B 83 1 14
SITE 1 LOA 14 SER A 18 GLY A 19 ARG A 20 GLU A 21
SITE 2 LOA 14 GLY A 22 ASP A 23 LYS A 24 HIS A 25
SITE 3 LOA 14 LYS A 26 LEU A 27 LYS A 28 LYS A 29
SITE 4 LOA 14 SER A 30 GLU A 31
SITE 1 LOB 12 ASP A 61 SER A 62 ASP A 63 GLY A 64
SITE 2 LOB 12 ASP A 65 GLY A 66 GLU A 67 CYS A 68
SITE 3 LOB 12 ASP A 69 PHE A 70 GLN A 71 GLU A 72
SITE 1 LOC 14 SER B 18 GLY B 19 ARG B 20 GLU B 21
SITE 2 LOC 14 GLY B 22 ASP B 23 LYS B 24 HIS B 25
SITE 3 LOC 14 LYS B 26 LEU B 27 LYS B 28 LYS B 29
SITE 4 LOC 14 SER B 30 GLU B 31
SITE 1 LOD 12 ASP B 61 SER B 62 ASP B 63 GLY B 64
SITE 2 LOD 12 ASP B 65 GLY B 66 GLU B 67 CYS B 68
SITE 3 LOD 12 ASP B 69 PHE B 70 GLN B 71 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
Complete list - b 16 2 Bytes