Header list of 1i5j.pdb file
Complete list - b 23 2 Bytes
HEADER LIPID TRANSPORT 27-FEB-01 1I5J
TITLE NMR STRUCTURE OF HUMAN APOLIPOPROTEIN C-II IN THE PRESENCE OF SDS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: APOLIPOPROTEIN CII;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: APOC-II;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS PROTEIN-LIPID INTERACTION, AMPHIPATHIC ALPHA HELIX, LIPID TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR C.A.MACRAILD,D.M.HATTERS,G.J.HOWLETT,P.R.GOOLEY
REVDAT 3 23-FEB-22 1I5J 1 REMARK
REVDAT 2 24-FEB-09 1I5J 1 VERSN
REVDAT 1 16-MAY-01 1I5J 0
JRNL AUTH C.A.MACRAILD,D.M.HATTERS,G.J.HOWLETT,P.R.GOOLEY
JRNL TITL NMR STRUCTURE OF HUMAN APOLIPOPROTEIN C-II IN THE PRESENCE
JRNL TITL 2 OF SODIUM DODECYL SULFATE.
JRNL REF BIOCHEMISTRY V. 40 5414 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11331005
JRNL DOI 10.1021/BI002821M
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 1.7, CNS 0.9
REMARK 3 AUTHORS : DELAGLIO (NMRPIPE), BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1I5J COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAR-01.
REMARK 100 THE DEPOSITION ID IS D_1000012930.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : 20 MM SODIUM ACETATE, 220 MM
REMARK 210 SODIUM DODECY SULFATE
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.8 MM U-15N APOC-II; 220 MM
REMARK 210 SDS; 20 MM SODIUM ACETATE, PH5
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNHA;
REMARK 210 HMQC-NOESY-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XEASY 1.4, DYANA 1.5
REMARK 210 METHOD USED : TORSION ANGLE AND CARTESIAN
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH FAVOURABLE NON
REMARK 210 -BOND ENERGY AND MINIMAL
REMARK 210 CONSTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 5
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-25
REMARK 465 RES C SSSEQI
REMARK 465 THR A 1
REMARK 465 GLN A 2
REMARK 465 GLN A 3
REMARK 465 PRO A 4
REMARK 465 GLN A 5
REMARK 465 GLN A 6
REMARK 465 ASP A 7
REMARK 465 GLU A 8
REMARK 465 MET A 9
REMARK 465 PRO A 10
REMARK 465 SER A 11
REMARK 465 PRO A 12
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 PHE A 14 -60.99 -164.28
REMARK 500 1 TYR A 37 -78.02 -66.60
REMARK 500 1 GLU A 38 26.91 -163.70
REMARK 500 1 THR A 40 -21.35 -141.83
REMARK 500 1 LEU A 42 48.93 -152.51
REMARK 500 1 VAL A 45 -88.89 -146.87
REMARK 500 1 ASP A 46 98.65 66.19
REMARK 500 1 GLU A 47 -74.36 37.58
REMARK 500 1 LYS A 48 -33.90 -39.50
REMARK 500 1 ARG A 50 35.73 -96.77
REMARK 500 1 ASP A 51 -39.03 -130.07
REMARK 500 1 THR A 57 32.57 178.51
REMARK 500 1 ALA A 58 42.90 75.45
REMARK 500 2 TYR A 37 -7.78 -163.75
REMARK 500 2 LEU A 42 -61.20 -143.99
REMARK 500 2 ALA A 44 18.01 -155.23
REMARK 500 2 ARG A 50 97.00 -173.01
REMARK 500 2 ASP A 51 -44.80 -163.49
REMARK 500 2 LYS A 55 -50.34 -145.76
REMARK 500 3 PHE A 14 -15.91 67.06
REMARK 500 3 TYR A 37 -14.04 -173.75
REMARK 500 3 TYR A 41 -76.16 -57.90
REMARK 500 3 LEU A 42 56.15 -149.85
REMARK 500 3 PRO A 43 -70.45 -89.37
REMARK 500 3 ALA A 44 57.42 -173.12
REMARK 500 4 PHE A 14 -60.98 -150.54
REMARK 500 4 GLU A 38 -40.57 -141.53
REMARK 500 4 LEU A 42 -59.19 -142.74
REMARK 500 4 PRO A 43 48.94 -71.39
REMARK 500 4 ALA A 44 25.41 -177.23
REMARK 500 4 VAL A 45 -55.12 -142.62
REMARK 500 4 THR A 57 26.36 -174.80
REMARK 500 4 ALA A 58 39.91 81.27
REMARK 500 5 PHE A 14 -44.56 -143.16
REMARK 500 5 GLU A 38 -55.47 -139.77
REMARK 500 5 TYR A 41 -159.75 -67.38
REMARK 500 5 PRO A 43 19.62 -68.18
REMARK 500 5 ASP A 51 -49.27 -157.22
REMARK 500 5 ALA A 58 -46.43 -138.79
REMARK 500 6 GLU A 38 -62.39 -144.00
REMARK 500 6 PRO A 43 46.87 -76.67
REMARK 500 6 GLU A 47 46.23 -77.45
REMARK 500 6 LYS A 48 24.12 48.61
REMARK 500 6 VAL A 71 -66.42 -99.69
REMARK 500 6 LYS A 76 -67.60 -134.67
REMARK 500 6 GLU A 78 63.14 79.62
REMARK 500 7 TYR A 37 -75.06 -125.56
REMARK 500 7 THR A 40 -36.40 78.82
REMARK 500 7 TYR A 41 -49.86 -21.04
REMARK 500 7 LEU A 42 170.96 -58.27
REMARK 500
REMARK 500 THIS ENTRY HAS 175 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1I5J A 1 79 UNP P02655 APOC2_HUMAN 1 79
SEQRES 1 A 79 THR GLN GLN PRO GLN GLN ASP GLU MET PRO SER PRO THR
SEQRES 2 A 79 PHE LEU THR GLN VAL LYS GLU SER LEU SER SER TYR TRP
SEQRES 3 A 79 GLU SER ALA LYS THR ALA ALA GLN ASN LEU TYR GLU LYS
SEQRES 4 A 79 THR TYR LEU PRO ALA VAL ASP GLU LYS LEU ARG ASP LEU
SEQRES 5 A 79 TYR SER LYS SER THR ALA ALA MET SER THR TYR THR GLY
SEQRES 6 A 79 ILE PHE THR ASP GLN VAL LEU SER VAL LEU LYS GLY GLU
SEQRES 7 A 79 GLU
HELIX 1 1 PHE A 14 LEU A 36 1 23
HELIX 2 2 THR A 62 LYS A 76 1 15
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 23 2 Bytes