Header list of 1ioj.pdb file
Complete list - r 14 2 Bytes
HEADER APOLIPOPROTEIN 12-MAY-98 1IOJ
TITLE HUMAN APOLIPOPROTEIN C-I, NMR, 18 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOC-I;
COMPND 3 CHAIN: A;
COMPND 4 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
KEYWDS APOLIPOPROTEIN, AMPHIPATHIC HELIX, LIPID ASSOCIATION, LCAT ACTIVATION
EXPDTA SOLUTION NMR
NUMMDL 18
AUTHOR A.ROZEK,J.T.SPARROW,K.H.WEISGRABER,R.J.CUSHLEY
REVDAT 3 14-MAR-18 1IOJ 1 COMPND SOURCE REMARK
REVDAT 2 24-FEB-09 1IOJ 1 VERSN
REVDAT 1 12-AUG-98 1IOJ 0
JRNL AUTH A.ROZEK,J.T.SPARROW,K.H.WEISGRABER,R.J.CUSHLEY
JRNL TITL CONFORMATION OF HUMAN APOLIPOPROTEIN C-I IN A LIPID-MIMETIC
JRNL TITL 2 ENVIRONMENT DETERMINED BY CD AND NMR SPECTROSCOPY.
JRNL REF BIOCHEMISTRY V. 38 14475 1999
JRNL REFN ISSN 0006-2960
JRNL PMID 10545169
JRNL DOI 10.1021/BI982966H
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DGII, DISCOVER DISCOVER
REMARK 3 AUTHORS : MOLECULAR SIMULATIONS INC, SAN DIEGO
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE OF APOC-I(1-38) IN THE
REMARK 3 PRESENCE OF SODIUM DODECYL SULFATE WAS REFINED USING 685 NOE-
REMARK 3 BASED DISTANCE RESTRAINTS. NO DIHEDRAL RESTRAINTS AND NO H-BOND
REMARK 3 RESTRAINTS WERE USED. THIS ENTRY CONTAINS 18 ACCEPTED OUT OF 50
REMARK 3 CALCULATED STRUCTURES. STRUCTURE CALCULATIONS WERE PERFORMED
REMARK 3 WITH THE PROGRAMS DGII AND DISCOVER INCLUDING DISTANCE GEOMETRY
REMARK 3 CALCULATIONS, SIMULATED ANNEALING AND ENERGY MINIMIZATION WITH A
REMARK 3 CONJUGATED GRADIENT. THE CVFF FORCEFIELD WAS USED. ALL FORMAL
REMARK 3 CHARGES WERE SWITCHED OFF. THE DIELECTRIC CONSTANT WAS SET TO 1.
REMARK 3 THE LENNARD-JONES POTENTIAL WAS USED FOR NON-BOND INTERACTIONS
REMARK 3 (CUTOFF 12A). FOR DETAILS ON STRUCTURE CALCULATION, RMSDS AND
REMARK 3 FINAL ENERGIES PLEASE SEE REFERENCE CITED UNDER "JRNL".
REMARK 4
REMARK 4 1IOJ 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_1000174223.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 323
REMARK 210 PH : 4.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 5.8 MM NATIVE APOC-I,
REMARK 210 90%H2O/10%D2O, 232 MM SDS-D25; 5
REMARK 210 MM SELECTIVELY 15N-LABELED
REMARK 210 SYNTHETIC APOC-I, 90%H2O/10%D2O,
REMARK 210 200 MM SDS-D25
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D-NOESY; 2D-TOCSY; DQF-COSY; 2D
REMARK 210 -15N-FILTERED NOESY; 2D-15N-
REMARK 210 FILTERED TOCSY; 2D 1H-15N HSQC;
REMARK 210 3D-NOESY-HSQC; 3D-TOCSY-HSQC
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 : DGII AND DISCOVER DISCOVER
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18
REMARK 210 CONFORMERS, SELECTION CRITERIA : SELECTED STRUCTURES HAVE NO
REMARK 210 HELIX-HELIX CONTACTS <5 ANGSTROMS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 15
REMARK 210
REMARK 210 REMARK: USING WATERGATE FOR WATER SUPPRESSION, 2D-TOCSY USING MLEV
REMARK 210 -17 FOR MIXING, 3D-TOCSY USING DIPSY-2RC FOR MIXING. 15N-
REMARK 210 FILTERED NOESY AND TOCSY INCLUDE DIFFERENCE (SHOWING ONLY 15N
REMARK 210 LABELED RESIDUES) AND SUM SPECTRA (SHOWING ONLY UNLABELED
REMARK 210 RESIDUES).
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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 1 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 1 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 1 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 2 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 2 MET A 38 N - CA - CB ANGL. DEV. = -11.5 DEGREES
REMARK 500 2 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 3 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 3 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 3 GLU A 33 N - CA - CB ANGL. DEV. = 11.1 DEGREES
REMARK 500 3 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 4 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 4 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 4 MET A 38 N - CA - CB ANGL. DEV. = -12.2 DEGREES
REMARK 500 4 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 5 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 5 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 5 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 6 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 6 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 6 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 7 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 7 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 7 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 8 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 8 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 8 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 9 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 9 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 9 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 10 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 10 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 10 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 11 VAL A 4 CB - CA - C ANGL. DEV. = 11.6 DEGREES
REMARK 500 11 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 11 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 11 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 12 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 12 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 12 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 13 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 13 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 13 ALA A 36 N - CA - CB ANGL. DEV. = 11.0 DEGREES
REMARK 500 13 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 14 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 14 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 14 ARG A 39 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 14 GLU A 40 N - CA - CB ANGL. DEV. = 11.0 DEGREES
REMARK 500 15 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 15 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500
REMARK 500 THIS ENTRY HAS 61 ANGLE DEVIATIONS.
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 5 73.21 -152.38
REMARK 500 1 ALA A 7 -66.32 -121.58
REMARK 500 1 GLU A 24 -62.76 169.28
REMARK 500 1 ARG A 28 -53.52 141.66
REMARK 500 1 ILE A 29 -81.65 -76.36
REMARK 500 1 SER A 32 -97.41 -117.90
REMARK 500 1 SER A 35 -110.03 -87.03
REMARK 500 1 ALA A 36 -68.92 70.23
REMARK 500 1 GLU A 44 -63.73 175.10
REMARK 500 1 LEU A 53 -128.48 -103.17
REMARK 500 1 LYS A 54 -113.97 59.10
REMARK 500 1 ILE A 55 -67.91 -92.18
REMARK 500 1 ASP A 56 -87.18 -140.65
REMARK 500 2 VAL A 4 -121.72 -128.94
REMARK 500 2 ALA A 7 -56.67 -130.80
REMARK 500 2 LYS A 12 -76.00 70.37
REMARK 500 2 LEU A 18 46.10 -98.72
REMARK 500 2 GLU A 19 52.18 -117.51
REMARK 500 2 ASP A 20 -55.63 -171.27
REMARK 500 2 ARG A 23 -60.35 -122.33
REMARK 500 2 ILE A 29 -70.44 -100.72
REMARK 500 2 LEU A 53 -68.64 -100.29
REMARK 500 2 ILE A 55 89.18 65.33
REMARK 500 3 VAL A 4 -148.00 -100.56
REMARK 500 3 SER A 6 -70.41 -172.90
REMARK 500 3 ALA A 7 -33.45 76.62
REMARK 500 3 ILE A 29 -82.55 -68.05
REMARK 500 3 GLN A 31 74.18 54.14
REMARK 500 3 SER A 32 153.54 71.95
REMARK 500 3 GLU A 33 -42.01 127.44
REMARK 500 3 SER A 35 -110.49 -79.97
REMARK 500 3 ALA A 36 -66.48 71.18
REMARK 500 3 MET A 38 0.61 -68.95
REMARK 500 3 ARG A 39 -63.37 -122.57
REMARK 500 3 GLU A 44 -69.46 171.52
REMARK 500 3 PHE A 46 -64.00 -91.37
REMARK 500 3 LYS A 54 -173.17 55.92
REMARK 500 3 ILE A 55 -79.17 -113.74
REMARK 500 3 ASP A 56 -80.07 -87.83
REMARK 500 4 ASP A 3 146.70 177.22
REMARK 500 4 VAL A 4 -129.93 -114.94
REMARK 500 4 ALA A 7 -44.39 -137.92
REMARK 500 4 LYS A 12 -76.44 68.75
REMARK 500 4 ILE A 29 -93.63 -78.49
REMARK 500 4 LYS A 30 2.87 56.35
REMARK 500 4 GLN A 31 -8.02 -161.23
REMARK 500 4 GLU A 33 -9.07 69.06
REMARK 500 4 SER A 35 105.57 -161.02
REMARK 500 4 LYS A 54 96.98 91.25
REMARK 500 5 ASP A 3 -92.84 71.25
REMARK 500
REMARK 500 THIS ENTRY HAS 198 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 LEU A 18 GLU A 19 2 137.49
REMARK 500 GLU A 33 LEU A 34 2 149.05
REMARK 500 GLU A 33 LEU A 34 4 141.07
REMARK 500 GLU A 33 LEU A 34 5 144.46
REMARK 500 GLY A 15 ASN A 16 6 141.49
REMARK 500 LEU A 34 SER A 35 6 148.72
REMARK 500 SER A 35 ALA A 36 6 -149.07
REMARK 500 GLU A 33 LEU A 34 7 149.44
REMARK 500 GLU A 33 LEU A 34 11 142.74
REMARK 500 SER A 35 ALA A 36 12 147.59
REMARK 500 GLU A 33 LEU A 34 13 146.65
REMARK 500 SER A 35 ALA A 36 13 -144.54
REMARK 500 GLU A 33 LEU A 34 17 143.35
REMARK 500 SER A 35 ALA A 36 17 138.60
REMARK 500 LEU A 34 SER A 35 18 -127.19
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1IOJ A 1 57 UNP P02654 APOC1_HUMAN 27 83
SEQRES 1 A 57 THR PRO ASP VAL SER SER ALA LEU ASP LYS LEU LYS GLU
SEQRES 2 A 57 PHE GLY ASN THR LEU GLU ASP LYS ALA ARG GLU LEU ILE
SEQRES 3 A 57 SER ARG ILE LYS GLN SER GLU LEU SER ALA LYS MET ARG
SEQRES 4 A 57 GLU TRP PHE SER GLU THR PHE GLN LYS VAL LYS GLU LYS
SEQRES 5 A 57 LEU LYS ILE ASP SER
HELIX 1 1 LEU A 8 LEU A 11 1 4
HELIX 2 2 PHE A 14 ILE A 29 1 16
HELIX 3 3 LYS A 37 LYS A 50 1 14
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
ORIGX1 1.000000 0.000000 0.000000 -1.00000
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 14 2 Bytes