Header list of 1hk6.pdb file
Complete list - r 28 2 Bytes
HEADER EXOCYTOSIS 05-MAR-03 1HK6
TITLE RAL BINDING DOMAIN FROM SEC5
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EXOCYST COMPLEX COMPONENT SEC5;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: IPT DOMAIN, RESIDUES 5-97;
COMPND 5 SYNONYM: SEC5L1;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: HIS-MET AT N-TERMINUS FROM CLONING
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR: PET16B
KEYWDS IPT RAL SEC5 EXOCYST, EXOCYTOSIS, PROTEIN TRANSPORT, IMMUNOGLOBULIN
KEYWDS 2 FOLD
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR H.R.MOTT,D.NIETLISPACH,L.J.HOPKINS,G.MIREY,J.H.CAMONIS,D.OWEN
REVDAT 4 28-MAR-18 1HK6 1 SOURCE JRNL
REVDAT 3 24-FEB-09 1HK6 1 VERSN
REVDAT 2 08-MAY-03 1HK6 1 JRNL
REVDAT 1 13-MAR-03 1HK6 0
JRNL AUTH H.R.MOTT,D.NIETLISPACH,L.J.HOPKINS,G.MIREY,J.H.CAMONIS,
JRNL AUTH 2 D.OWEN
JRNL TITL STRUCTURE OF THE GTPASE-BINDING DOMAIN OF SEC5 AND
JRNL TITL 2 ELUCIDATION OF ITS RAL BINDING SITE.
JRNL REF J. BIOL. CHEM. V. 278 17053 2003
JRNL REFN ISSN 0021-9258
JRNL PMID 12624092
JRNL DOI 10.1074/JBC.M300155200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL ABOVE
REMARK 4
REMARK 4 1HK6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1290012285.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 200
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS/ARIA1.1
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: STRUCTURE WAS DETERMINED USING 15N-LEBELLED AND 13C,15N
REMARK 210 -LABELLED SEC5
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 400
REMARK 400 COMPOUND
REMARK 400 PART OF THE EXOCYST COMPLEX INVOLVED IN THE DOCKING
REMARK 400 OF EXOCYSTIC VESICLES WITH FUSION SITES ON THE
REMARK 400 PLASMA MEMBRANE.
REMARK 400 THE EXOCYST COMPLEX IS COMPOSED OF VARIOUS SUBUNITS NAMED
REMARK 400 AS SEC3,SEC5,SEC6,SEC8,SEC10,SEC15,EXO70 AND EXO84.
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 THR A 11 52.47 -168.82
REMARK 500 1 PRO A 15 -160.14 -79.71
REMARK 500 1 ASN A 16 21.07 -173.22
REMARK 500 1 GLU A 17 127.45 177.78
REMARK 500 1 THR A 33 43.51 -94.97
REMARK 500 1 CYS A 48 41.87 -152.47
REMARK 500 1 MET A 55 -52.40 -136.36
REMARK 500 1 ALA A 57 41.67 -80.48
REMARK 500 1 SER A 58 -47.10 -175.27
REMARK 500 1 CYS A 62 143.82 -170.93
REMARK 500 1 LYS A 68 -43.90 -147.84
REMARK 500 1 ASN A 69 -123.40 -76.15
REMARK 500 1 ASP A 70 42.82 -170.41
REMARK 500 1 LYS A 71 -46.44 -164.55
REMARK 500 2 THR A 11 48.80 -171.05
REMARK 500 2 GLU A 17 132.24 179.73
REMARK 500 2 CYS A 48 38.03 -149.72
REMARK 500 2 MET A 55 -44.11 -143.12
REMARK 500 2 CYS A 62 136.67 -170.47
REMARK 500 2 VAL A 64 -143.61 -66.63
REMARK 500 2 ASN A 69 -127.30 -70.86
REMARK 500 2 ASP A 70 -53.90 -148.94
REMARK 500 2 SER A 86 127.81 -170.99
REMARK 500 3 MET A 4 139.49 -175.15
REMARK 500 3 ARG A 5 57.25 -171.16
REMARK 500 3 THR A 11 47.26 -153.70
REMARK 500 3 GLU A 17 131.30 177.57
REMARK 500 3 ILE A 39 -39.94 -143.57
REMARK 500 3 CYS A 48 40.03 -152.18
REMARK 500 3 MET A 55 -42.77 -149.83
REMARK 500 3 ALA A 57 34.39 -74.83
REMARK 500 3 SER A 58 30.13 -177.99
REMARK 500 3 LYS A 68 -50.01 -132.11
REMARK 500 3 ASP A 70 -47.03 -179.57
REMARK 500 3 LYS A 71 -126.68 -97.95
REMARK 500 3 THR A 87 40.75 -107.58
REMARK 500 4 THR A 11 44.51 -148.00
REMARK 500 4 ASN A 16 30.18 -92.93
REMARK 500 4 GLU A 17 131.21 178.08
REMARK 500 4 THR A 33 41.52 -90.03
REMARK 500 4 ILE A 39 20.71 -147.26
REMARK 500 4 CYS A 48 39.01 -153.09
REMARK 500 4 MET A 55 -48.37 -138.89
REMARK 500 4 ALA A 57 36.23 -78.52
REMARK 500 4 SER A 58 -43.10 -177.29
REMARK 500 4 LYS A 68 -48.91 -135.28
REMARK 500 4 ASN A 69 -118.91 -77.95
REMARK 500 4 ASP A 70 -44.09 -152.61
REMARK 500 5 MET A 4 139.90 -172.90
REMARK 500 5 THR A 11 41.18 -147.01
REMARK 500
REMARK 500 THIS ENTRY HAS 335 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 HIS A 3, INSERTION CLONING ARTEFACT
REMARK 999 MET A 4, INSERTION CLONING ARTEFACT
DBREF 1HK6 A 3 4 PDB 1HK6 1HK6 3 4
DBREF 1HK6 A 5 97 UNP Q9D4H1 SEC5_MOUSE 5 97
SEQRES 1 A 95 HIS MET ARG GLN PRO PRO LEU VAL THR GLY ILE SER PRO
SEQRES 2 A 95 ASN GLU GLY ILE PRO TRP THR LYS VAL THR ILE ARG GLY
SEQRES 3 A 95 GLU ASN LEU GLY THR GLY PRO THR ASP LEU ILE GLY LEU
SEQRES 4 A 95 THR ILE CYS GLY HIS ASN CYS LEU LEU THR ALA GLU TRP
SEQRES 5 A 95 MET SER ALA SER LYS ILE VAL CYS ARG VAL GLY GLN ALA
SEQRES 6 A 95 LYS ASN ASP LYS GLY ASP ILE ILE VAL THR THR LYS SER
SEQRES 7 A 95 GLY GLY LYS GLY THR SER THR VAL SER PHE LYS LEU LEU
SEQRES 8 A 95 LYS PRO GLU LYS
SHEET 1 AA 5 GLU A 53 TRP A 54 0
SHEET 2 AA 5 ILE A 60 ARG A 63 -1 O VAL A 61 N GLU A 53
SHEET 3 AA 5 LYS A 23 GLU A 29 -1 O VAL A 24 N CYS A 62
SHEET 4 AA 5 LEU A 9 ILE A 13 -1 O LEU A 9 N GLU A 29
SHEET 5 AA 5 THR A 85 SER A 86 1 O THR A 85 N VAL A 10
SHEET 1 AB 3 HIS A 46 ASN A 47 0
SHEET 2 AB 3 LEU A 41 ILE A 43 -1 O ILE A 43 N HIS A 46
SHEET 3 AB 3 ILE A 74 VAL A 76 -1 O ILE A 75 N THR A 42
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 - r 28 2 Bytes