Header list of 1u81.pdb file
Complete list - r 25 2 Bytes
HEADER PROTEIN TRANSPORT 04-AUG-04 1U81
TITLE DELTA-17 HUMAN ADP RIBOSYLATION FACTOR 1 COMPLEXED WITH GDP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADP-RIBOSYLATION FACTOR 1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ARF1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3
KEYWDS DELTA17ARF1, D17ARF1, ARF1, GDP-BINDING, MEMBRANE TRAFFICKING, RDC
KEYWDS 2 REFINEMENT, PROTEIN TRANSPORT
EXPDTA SOLUTION NMR
NUMMDL 11
AUTHOR R.D.SEIDEL,J.C.AMOR,R.A.KAHN,J.H.PRESTEGARD
REVDAT 5 15-SEP-10 1U81 1 JRNL AUTHOR
REVDAT 4 29-DEC-09 1U81 1 JRNL
REVDAT 3 24-FEB-09 1U81 1 VERSN
REVDAT 2 26-APR-05 1U81 1 JRNL
REVDAT 1 05-OCT-04 1U81 0
JRNL AUTH R.D.SEIDEL,J.C.AMOR,R.A.KAHN,J.H.PRESTEGARD
JRNL TITL CONFORMATIONAL CHANGES IN HUMAN ARF1 ON NUCLEOTIDE EXCHANGE
JRNL TITL 2 AND DELETION OF MEMBRANE-BINDING ELEMENTS.
JRNL REF J.BIOL.CHEM. V. 279 48307 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15308674
JRNL DOI 10.1074/JBC.M402109200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR-NIH 2.9.1
REMARK 3 AUTHORS : C.D.SCHWIETERS, J.J.KUSZEWSKI, N.TJANDRA, G.M.CLORE
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1U81 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-AUG-04.
REMARK 100 THE RCSB ID CODE IS RCSB023361.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 305; 301; 298
REMARK 210 PH : 7; 7; 7
REMARK 210 IONIC STRENGTH : 50MM SALT; 50MM SALT; 50MM SALT
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 10MM KPO4, 50MM NACL, 1MM MGCL2,
REMARK 210 5MM NAN3, 90% H2O, 10% D2O; 7.5%
REMARK 210 (W/V) ETHERBICELLE IN 10MM KPO4,
REMARK 210 50MM NACL, 1MM MGCL2, 90% H2O,
REMARK 210 10% D2O; 4% PENTAETHYLENE GLYCOL
REMARK 210 OCTYLETHER IN 10MM KPO4, 50MM
REMARK 210 NACL, 1MM MGCL2, 90% H2O, 10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : ASSIGNMENT SUITE; IPAP-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 600 MHZ; 300 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : CARTESIAN MIN (NO RDC), TORSION
REMARK 210 ANGLE MIN (RAMP RDC), CARTESIAN
REMARK 210 MIN (RAMP RDC), CARTESIAN MIN (RO
REMARK 210 RDC), TORSION ANGLE MIN (RDC)
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 11
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 11
REMARK 210 CONFORMERS, SELECTION CRITERIA : ALL CALCULATED STRUCTURES
REMARK 210 SUBMITTED
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-11
REMARK 470 RES CSSEQI ATOMS
REMARK 470 LYS A 181 O
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 MET A 22 89.33 -68.75
REMARK 500 1 LEU A 25 -159.95 -70.51
REMARK 500 1 LYS A 38 61.75 60.07
REMARK 500 1 GLU A 41 128.72 -24.46
REMARK 500 1 PRO A 47 -76.11 -59.11
REMARK 500 1 ILE A 49 87.31 -31.97
REMARK 500 1 THR A 55 64.96 -65.65
REMARK 500 1 LYS A 59 -143.64 74.45
REMARK 500 1 TRP A 66 -178.25 176.15
REMARK 500 1 GLN A 71 50.55 177.16
REMARK 500 1 ASP A 72 -148.84 51.85
REMARK 500 1 ILE A 74 81.05 45.86
REMARK 500 1 PRO A 76 11.37 -63.42
REMARK 500 1 LEU A 88 96.42 -178.36
REMARK 500 1 ASP A 93 85.06 -50.42
REMARK 500 1 ASP A 96 92.27 -46.72
REMARK 500 1 VAL A 100 -54.08 -7.74
REMARK 500 1 MET A 110 13.68 -60.16
REMARK 500 1 GLU A 113 121.02 -29.35
REMARK 500 1 LEU A 116 56.69 -109.84
REMARK 500 1 ARG A 117 -74.58 -75.01
REMARK 500 1 ALA A 119 108.00 -28.66
REMARK 500 1 LYS A 127 25.35 81.91
REMARK 500 1 ASP A 129 3.89 -58.88
REMARK 500 1 ALA A 133 164.25 -37.44
REMARK 500 1 GLU A 138 1.59 -65.18
REMARK 500 1 ASP A 141 -86.11 -106.01
REMARK 500 1 LYS A 142 -5.49 -39.59
REMARK 500 1 ARG A 149 -169.34 -121.34
REMARK 500 1 HIS A 150 -44.65 70.37
REMARK 500 1 TYR A 154 137.05 -172.37
REMARK 500 2 ILE A 20 116.78 -160.26
REMARK 500 2 LEU A 25 -168.15 -62.79
REMARK 500 2 PRO A 47 -73.11 -59.13
REMARK 500 2 ILE A 49 101.72 -22.44
REMARK 500 2 THR A 55 72.50 -62.54
REMARK 500 2 TYR A 58 134.99 -170.01
REMARK 500 2 LYS A 59 -137.65 66.70
REMARK 500 2 SER A 62 73.68 -150.14
REMARK 500 2 TRP A 66 -179.79 163.85
REMARK 500 2 GLN A 71 49.90 177.10
REMARK 500 2 ASP A 72 -153.95 55.36
REMARK 500 2 ILE A 74 76.25 46.99
REMARK 500 2 PRO A 76 22.61 -67.22
REMARK 500 2 ASN A 84 34.55 -144.75
REMARK 500 2 LEU A 88 90.13 -179.91
REMARK 500 2 ASP A 93 94.03 -43.42
REMARK 500 2 ASP A 96 88.27 -47.86
REMARK 500 2 VAL A 100 -30.18 -37.74
REMARK 500 2 ARG A 104 -26.72 -34.79
REMARK 500
REMARK 500 THIS ENTRY HAS 343 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 1
DBREF 1U81 A 18 181 UNP P84077 ARF1_HUMAN 17 180
SEQRES 1 A 164 MET ARG ILE LEU MET VAL GLY LEU ASP ALA ALA GLY LYS
SEQRES 2 A 164 THR THR ILE LEU TYR LYS LEU LYS LEU GLY GLU ILE VAL
SEQRES 3 A 164 THR THR ILE PRO THR ILE GLY PHE ASN VAL GLU THR VAL
SEQRES 4 A 164 GLU TYR LYS ASN ILE SER PHE THR VAL TRP ASP VAL GLY
SEQRES 5 A 164 GLY GLN ASP LYS ILE ARG PRO LEU TRP ARG HIS TYR PHE
SEQRES 6 A 164 GLN ASN THR GLN GLY LEU ILE PHE VAL VAL ASP SER ASN
SEQRES 7 A 164 ASP ARG GLU ARG VAL ASN GLU ALA ARG GLU GLU LEU MET
SEQRES 8 A 164 ARG MET LEU ALA GLU ASP GLU LEU ARG ASP ALA VAL LEU
SEQRES 9 A 164 LEU VAL PHE ALA ASN LYS GLN ASP LEU PRO ASN ALA MET
SEQRES 10 A 164 ASN ALA ALA GLU ILE THR ASP LYS LEU GLY LEU HIS SER
SEQRES 11 A 164 LEU ARG HIS ARG ASN TRP TYR ILE GLN ALA THR CYS ALA
SEQRES 12 A 164 THR SER GLY ASP GLY LEU TYR GLU GLY LEU ASP TRP LEU
SEQRES 13 A 164 SER ASN GLN LEU ARG ASN GLN LYS
HET MG A 2 1
HET GDP A 1 28
HETNAM MG MAGNESIUM ION
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
FORMUL 2 MG MG 2+
FORMUL 3 GDP C10 H15 N5 O11 P2
HELIX 1 1 GLY A 29 LYS A 38 1 10
HELIX 2 2 PRO A 76 THR A 85 1 10
HELIX 3 3 ASN A 101 MET A 108 1 8
HELIX 4 4 ALA A 137 ASP A 141 5 5
HELIX 5 5 GLY A 165 LYS A 181 1 17
SHEET 1 A 4 MET A 22 GLY A 24 0
SHEET 2 A 4 ILE A 89 VAL A 91 1 O VAL A 91 N VAL A 23
SHEET 3 A 4 LEU A 121 ALA A 125 1 O PHE A 124 N PHE A 90
SHEET 4 A 4 TRP A 153 ALA A 157 1 O TYR A 154 N VAL A 123
SHEET 1 B 2 GLU A 54 TYR A 58 0
SHEET 2 B 2 ILE A 61 VAL A 65 -1 O PHE A 63 N VAL A 56
LINK MG MG A 2 OE2 GLU A 54 1555 1555 2.23
SITE 1 AC1 1 GLU A 54
SITE 1 AC2 9 LEU A 25 ALA A 27 ALA A 28 GLY A 29
SITE 2 AC2 9 LYS A 30 THR A 31 THR A 32 ASN A 126
SITE 3 AC2 9 LYS A 127
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 25 2 Bytes