Header list of 1odr.pdb file
Complete list - 23 20 Bytes
HEADER LIPID TRANSPORT 02-MAR-96 1ODR
TITLE PEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH 6.0,
TITLE 2 37 DEGREES CELSIUS AND PEPTIDE:DPC MOLE RATIO OF 1:40
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOA-I PEPTIDE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 166 - 185;
COMPND 5 SYNONYM: APOA-I (166 - 185), APOLIPOPROTEIN A-I (166 - 185);
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS APOLIPOPROTEIN A-I, COFACTOR FOR LCAT ACTIVATION, LIPID TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 5
AUTHOR G.WANG,W.D.TRELEAVEN,R.J.CUSHLEY
REVDAT 3 23-FEB-22 1ODR 1 REMARK
REVDAT 2 24-FEB-09 1ODR 1 VERSN
REVDAT 1 10-JUN-96 1ODR 0
JRNL AUTH G.WANG,W.D.TRELEAVEN,R.J.CUSHLEY
JRNL TITL CONFORMATION OF HUMAN SERUM APOLIPOPROTEIN A-I(166-185) IN
JRNL TITL 2 THE PRESENCE OF SODIUM DODECYL SULFATE OR
JRNL TITL 3 DODECYLPHOSPHOCHOLINE BY 1H-NMR AND CD. EVIDENCE FOR
JRNL TITL 4 SPECIFIC PEPTIDE-SDS INTERACTIONS.
JRNL REF BIOCHIM.BIOPHYS.ACTA V.1301 174 1996
JRNL REFN ISSN 0006-3002
JRNL PMID 8664326
JRNL DOI 10.1016/0005-2760(96)00037-9
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DGII, DISCOVER
REMARK 3 AUTHORS : HAVEL (DGII), BIOSYM TECHNOLOGIES, INC. (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1ODR 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_1000175438.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 310
REMARK 210 PH : 6.0
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 : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 5
REMARK 210 CONFORMERS, SELECTION CRITERIA : MOST CLOSELY RESEMBLING THE
REMARK 210 AVERAGE STRUCTURE OF OF A
REMARK 210 CALCULATED SET OF 20 CONFORMERS
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: 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 LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 1 GLU A 4 CD GLU A 4 OE1 0.109
REMARK 500 1 GLU A 14 CD GLU A 14 OE2 0.110
REMARK 500 1 GLU A 18 CD GLU A 18 OE1 0.109
REMARK 500 2 GLU A 4 CD GLU A 4 OE2 0.110
REMARK 500 2 GLU A 14 CD GLU A 14 OE2 0.110
REMARK 500 2 GLU A 18 CD GLU A 18 OE2 0.111
REMARK 500 3 GLU A 4 CD GLU A 4 OE2 0.110
REMARK 500 3 GLU A 14 CD GLU A 14 OE1 0.110
REMARK 500 3 GLU A 18 CD GLU A 18 OE1 0.110
REMARK 500 4 GLU A 4 CD GLU A 4 OE1 0.110
REMARK 500 4 GLU A 14 CD GLU A 14 OE2 0.110
REMARK 500 4 GLU A 18 CD GLU A 18 OE1 0.110
REMARK 500 5 GLU A 4 CD GLU A 4 OE1 0.109
REMARK 500 5 GLU A 14 CD GLU A 14 OE2 0.109
REMARK 500 5 GLU A 18 CD GLU A 18 OE1 0.110
REMARK 500
REMARK 500 REMARK: NULL
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 ASP A 3 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 1 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 1 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 1 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 2 ASP A 3 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 2 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 2 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 2 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 3 ASP A 3 CB - CG - OD1 ANGL. DEV. = -5.5 DEGREES
REMARK 500 3 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 3 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 3 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 4 ASP A 3 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 4 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 4 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 4 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 5 ASP A 3 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 5 ARG A 6 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
REMARK 500 5 ARG A 8 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 5 ARG A 12 NE - CZ - NH1 ANGL. DEV. = 4.1 DEGREES
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 2 47.78 -174.33
REMARK 500 1 ASP A 3 22.79 -149.45
REMARK 500 1 GLU A 4 -53.20 -156.69
REMARK 500 1 ASN A 19 -44.88 -153.37
REMARK 500 2 ASP A 3 -46.40 -172.14
REMARK 500 2 GLU A 18 102.20 -56.11
REMARK 500 2 ASN A 19 -62.75 176.09
REMARK 500 3 ASP A 3 -38.46 -175.49
REMARK 500 3 ASN A 19 -55.16 -172.24
REMARK 500 4 ASP A 3 -40.51 -179.46
REMARK 500 4 LYS A 17 31.24 -96.95
REMARK 500 4 GLU A 18 38.16 -97.12
REMARK 500 4 ASN A 19 -69.56 -170.50
REMARK 500 5 SER A 2 66.00 -165.59
REMARK 500 5 ASN A 19 -54.76 -169.76
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ODP RELATED DB: PDB
REMARK 900 RELATED ID: 1ODQ RELATED DB: PDB
DBREF 1ODR A 1 20 UNP P02647 APOA1_HUMAN 190 209
SEQRES 1 A 20 TYR SER ASP GLU LEU ARG GLN ARG LEU ALA ALA ARG LEU
SEQRES 2 A 20 GLU ALA LEU LYS GLU ASN GLY
HELIX 1 1 LEU A 5 LEU A 16 1 12
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 - 23 20 Bytes