Header list of 1by6.pdb file
Complete list - 14 20 Bytes
HEADER SIGNALING PROTEIN 03-DEC-99 1BY6
TITLE PEPTIDE OF HUMAN APOLIPOPROTEIN C-II
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOLIPOPROTEIN C-II;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 44-79;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606;
SOURCE 6 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED ON AN ABI
SOURCE 7 430A SYNTHESIZER (PE APPLIED BIOSYSTEMS, FOSTER CITY, CA, USA) BY
SOURCE 8 THE SOLID PHASE METHOD USING T-BOC/BENZYL PROTECTING GROUPS AND A
SOURCE 9 PHENYL-ACETAMIDOMETHYL-POLYSTYRENE SUPPORT WITH FAST HBTU/HOBT
SOURCE 10 COUPLING. AFTER SYNTHESIS THE PEPTIDE WAS DEPROTECTED AND CLEAVED
SOURCE 11 FROM THE RESIN WITH TMSBR.
KEYWDS APOLIPOPROTEIN, AMPHIPATHIC HELIX, LIPID ASSOCIATION, LPL ACTIVATION,
KEYWDS 2 SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 19
AUTHOR R.STORJOHANN,A.ROZEK,J.T.SPARROW,R.J.CUSHLEY
REVDAT 3 14-MAR-18 1BY6 1 SOURCE REMARK
REVDAT 2 24-FEB-09 1BY6 1 VERSN
REVDAT 1 15-NOV-00 1BY6 0
JRNL AUTH R.STORJOHANN,A.ROZEK,J.T.SPARROW,R.J.CUSHLEY
JRNL TITL STRUCTURE OF A BIOLOGICALLY ACTIVE FRAGMENT OF HUMAN SERUM
JRNL TITL 2 APOLIPOPROTEIN C-II IN THE PRESENCE OF SODIUM DODECYL
JRNL TITL 3 SULFATE AND DODECYLPHOSPHOCHOLINE.
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1486 253 2000
JRNL REFN ISSN 0006-3002
JRNL PMID 10903476
JRNL DOI 10.1016/S1388-1981(00)00062-7
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE OF APOC-II(44-79) IN THE
REMARK 3 PRESENCE OF SODIUM DODECYL SULFATE WAS REFINED USING A
REMARK 3 RELAXATION MATRIX REFINEMENT PROTOCOL BASED ON 241 NOESY CROSS-
REMARK 3 PEAK INTENSITIES MEASURED AT SEVEN DIFFERENT NOESY MIXING TIMES
REMARK 3 BETWEEN 75 MS AND 300 MS. NO DIHEDRAL RESTRAINTS WERE USED. THIS
REMARK 3 ENTRY CONTAINS 19 ACCEPTED STRUCTURES. ONE CALCULATED STRUCTURE
REMARK 3 WAS REJECTED BECAUSE OF HIGH COVALENT ENERGY. STRUCTURE
REMARK 3 CALCULATIONS WERE PERFORMED WITH THE PROGRAM X-PLOR (AXEL
REMARK 3 BRUNGER) INCLUDING DISTANCE GEOMETRY CALCULATIONS, SIMULATED
REMARK 3 ANNEALING (BOTH UNDER THE ISOLATED SPIN PAIR APPROXIMATION AND
REMARK 3 COMPLETE RELAXATION MATRIX CALCULATIONS) AS WELL AS ENERGY
REMARK 3 MINIMIZATION WITH A CONJUGATED GRADIENT. THE CHARMM FORCEFIELD
REMARK 3 WAS USED. FOR DETAILS ON STRUCTURE CALCULATION PLEASE SEE
REMARK 3 REFERENCE CITED UNDER "JRNL".
REMARK 4
REMARK 4 1BY6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-DEC-99.
REMARK 100 THE DEPOSITION ID IS D_1000010133.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 4.1
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : PERDEUTERATED SODIUM DODECYL
REMARK 210 SULFATE (SDS) IN 160 FOLD MOLAR
REMARK 210 EXCESS RELATIVE TO PEPTIDE
REMARK 210 CONCENTRATION
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D-TOCSY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX 600
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY/SIMULATED
REMARK 210 ANNEALING/RELAXATION MATRIX
REMARK 210 REFINEMENT
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 19
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 19
REMARK 210
REMARK 210 REMARK: USING WATERGATE FOR WATER SUPPRESSION
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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
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 VAL A 45 77.58 -117.75
REMARK 500 1 LYS A 48 -50.80 -135.63
REMARK 500 1 ARG A 50 117.06 56.87
REMARK 500 1 LYS A 55 -37.92 -177.49
REMARK 500 1 ALA A 59 45.97 72.52
REMARK 500 1 SER A 61 25.69 44.90
REMARK 500 1 TYR A 63 70.02 -102.25
REMARK 500 1 ILE A 66 61.27 -178.90
REMARK 500 1 ASP A 69 176.89 52.75
REMARK 500 1 GLN A 70 -92.58 45.33
REMARK 500 1 SER A 73 40.10 -149.40
REMARK 500 1 GLU A 78 36.87 -178.77
REMARK 500 2 ASP A 46 56.19 -160.77
REMARK 500 2 GLU A 47 106.73 64.62
REMARK 500 2 LEU A 49 -172.44 50.66
REMARK 500 2 ASP A 51 -39.02 -137.53
REMARK 500 2 SER A 54 37.58 -91.11
REMARK 500 2 LYS A 55 -150.23 -77.82
REMARK 500 2 MET A 60 74.99 -175.80
REMARK 500 2 SER A 61 73.65 40.76
REMARK 500 2 ILE A 66 57.23 -151.37
REMARK 500 2 ASP A 69 -57.40 67.63
REMARK 500 2 GLN A 70 -76.02 -20.38
REMARK 500 2 VAL A 74 -48.73 -132.56
REMARK 500 2 LYS A 76 47.61 -144.20
REMARK 500 2 GLU A 78 21.99 -140.46
REMARK 500 3 LYS A 48 83.39 63.64
REMARK 500 3 SER A 56 -53.65 -134.60
REMARK 500 3 MET A 60 95.24 -41.72
REMARK 500 3 SER A 61 -92.12 52.35
REMARK 500 3 THR A 64 -60.35 -95.02
REMARK 500 3 ILE A 66 85.92 -156.66
REMARK 500 3 THR A 68 69.55 63.75
REMARK 500 3 ASP A 69 -28.20 -35.39
REMARK 500 3 SER A 73 32.60 -152.01
REMARK 500 3 LEU A 75 45.32 -85.90
REMARK 500 3 GLU A 78 115.46 65.98
REMARK 500 4 GLU A 47 78.89 -176.84
REMARK 500 4 LYS A 48 -82.91 -100.52
REMARK 500 4 ARG A 50 119.64 54.33
REMARK 500 4 ASP A 51 50.06 -98.70
REMARK 500 4 LYS A 55 -47.44 174.98
REMARK 500 4 SER A 56 -172.86 -171.46
REMARK 500 4 THR A 57 -54.03 64.22
REMARK 500 4 ALA A 58 -24.48 -39.95
REMARK 500 4 ALA A 59 49.94 77.01
REMARK 500 4 MET A 60 -72.36 -143.89
REMARK 500 4 SER A 61 -75.78 -42.70
REMARK 500 4 TYR A 63 110.73 175.77
REMARK 500 4 THR A 64 -51.01 -162.19
REMARK 500
REMARK 500 THIS ENTRY HAS 288 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 2 ARG A 50 0.28 SIDE CHAIN
REMARK 500 3 ARG A 50 0.08 SIDE CHAIN
REMARK 500 4 ARG A 50 0.08 SIDE CHAIN
REMARK 500 5 ARG A 50 0.19 SIDE CHAIN
REMARK 500 7 ARG A 50 0.09 SIDE CHAIN
REMARK 500 8 ARG A 50 0.15 SIDE CHAIN
REMARK 500 10 ARG A 50 0.11 SIDE CHAIN
REMARK 500 13 ARG A 50 0.18 SIDE CHAIN
REMARK 500 14 ARG A 50 0.13 SIDE CHAIN
REMARK 500 15 ARG A 50 0.27 SIDE CHAIN
REMARK 500 16 ARG A 50 0.10 SIDE CHAIN
REMARK 500 17 ARG A 50 0.19 SIDE CHAIN
REMARK 500 18 ARG A 50 0.08 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1BY6 A 44 79 UNP P02655 APOC2_HUMAN 66 101
SEQRES 1 A 36 ALA VAL ASP GLU LYS LEU ARG ASP LEU TYR SER LYS SER
SEQRES 2 A 36 THR ALA ALA MET SER THR TYR THR GLY ILE PHE THR ASP
SEQRES 3 A 36 GLN VAL LEU SER VAL LEU LYS GLY GLU GLU
HELIX 1 1 ASP A 69 SER A 73 5 5
HELIX 2 2 VAL A 74 GLU A 78 5 5
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 - 14 20 Bytes