Header list of 1qa5.pdb file
Complete list - 21 20 Bytes
HEADER VIRAL PROTEIN 12-APR-99 1QA5
TITLE MYRISTOYLATED HIV-1 NEF ANCHOR DOMAIN, NMR, 2 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (MYRISTOYLATED HIV-1 NEF ANCHOR DOMAIN (MYRISTATE-
COMPND 3 GLY2 TO TRP57));
COMPND 4 CHAIN: A;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 (ISOLATE
SOURCE 4 NL4-3);
SOURCE 5 ORGANISM_COMMON: HIV-1;
SOURCE 6 ORGANISM_TAXID: 11676
KEYWDS HIV, AIDS, REGULATORY FACTOR, NEGATIVE FACTOR, NEF, MYRISTOYLATION,
KEYWDS 2 VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 2
AUTHOR M.GEYER,H.R.KALBITZER
REVDAT 5 21-DEC-22 1QA5 1 SEQADV
REVDAT 4 27-OCT-21 1QA5 1 SOURCE REMARK
REVDAT 3 27-NOV-19 1QA5 1 JRNL REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1QA5 1 VERSN
REVDAT 1 26-MAY-99 1QA5 0
JRNL AUTH M.GEYER,C.E.MUNTE,J.SCHORR,R.KELLNER,H.R.KALBITZER
JRNL TITL STRUCTURE OF THE ANCHOR-DOMAIN OF MYRISTOYLATED AND
JRNL TITL 2 NON-MYRISTOYLATED HIV-1 NEF PROTEIN.
JRNL REF J.MOL.BIOL. V. 289 123 1999
JRNL REFN ISSN 0022-2836
JRNL PMID 10339411
JRNL DOI 10.1006/JMBI.1999.2740
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.GRZESIEK,A.BAX,J.S.HU,J.KAUFMAN,I.PALMER,S.J.STAHL,
REMARK 1 AUTH 2 N.TJANDRA,P.T.WINGFIELD
REMARK 1 TITL REFINED SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF HIV-1
REMARK 1 TITL 2 NEF.
REMARK 1 REF PROTEIN SCI. V. 6 1248 1997
REMARK 1 REFN ISSN 0961-8368
REMARK 1 PMID 9194185
REMARK 1 DOI 10.1002/PRO.5560060613
REMARK 1 REFERENCE 2
REMARK 1 AUTH K.J.BARNHAM,S.A.MONKS,M.G.HINDS,A.A.AZAD,R.S.NORTON
REMARK 1 TITL SOLUTION STRUCTURE OF A POLYPEPTIDE FROM THE N TERMINUS OF
REMARK 1 TITL 2 THE HIV PROTEIN NEF.
REMARK 1 REF BIOCHEMISTRY V. 36 5970 1997
REMARK 1 REFN ISSN 0006-2960
REMARK 1 PMID 9166767
REMARK 1 DOI 10.1021/BI9629945
REMARK 1 REFERENCE 3
REMARK 1 AUTH S.AROLD,P.FRANKEN,M.P.STRUB,F.HOH,S.BENICHOU,R.BENAROUS,
REMARK 1 AUTH 2 C.DUMAS
REMARK 1 TITL THE CRYSTAL STRUCTURE OF HIV-1 NEF PROTEIN BOUND TO THE FYN
REMARK 1 TITL 2 KINASE SH3 DOMAIN SUGGESTS A ROLE FOR THIS COMPLEX IN
REMARK 1 TITL 3 ALTERED T CELL RECEPTOR SIGNALING.
REMARK 1 REF STRUCTURE V. 5 1361 1997
REMARK 1 REFN ISSN 0969-2126
REMARK 1 PMID 9351809
REMARK 1 DOI 10.1016/S0969-2126(97)00286-4
REMARK 1 REFERENCE 4
REMARK 1 AUTH C.H.LEE,K.SAKSELA,U.A.MIRZA,B.T.CHAIT,J.KURIYAN
REMARK 1 TITL CRYSTAL STRUCTURE OF THE CONSERVED CORE OF HIV-1 NEF
REMARK 1 TITL 2 COMPLEXED WITH A SRC FAMILY SH3 DOMAIN.
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 85 931 1996
REMARK 1 REFN ISSN 0092-8674
REMARK 1 PMID 8681387
REMARK 1 DOI 10.1016/S0092-8674(00)81276-3
REMARK 1 REFERENCE 5
REMARK 1 AUTH S.GRZESIEK,A.BAX,G.M.CLORE,A.M.GRONENBORN,J.S.HU,J.KAUFMAN,
REMARK 1 AUTH 2 I.PALMER,S.J.STAHL,P.T.WINGFIELD
REMARK 1 TITL THE SOLUTION STRUCTURE OF HIV-1 NEF REVEALS AN UNEXPECTED
REMARK 1 TITL 2 FOLD AND PERMITS DELINEATION OF THE BINDING SURFACE FOR THE
REMARK 1 TITL 3 SH3 DOMAIN OF HCK TYROSINE PROTEIN KINASE.
REMARK 1 REF NAT.STRUCT.BIOL. V. 3 340 1996
REMARK 1 REFN ISSN 1072-8368
REMARK 1 PMID 8599760
REMARK 1 DOI 10.1038/NSB0496-340
REMARK 1 REFERENCE 6
REMARK 1 AUTH J.FREUND,R.KELLNER,J.KONVALINKA,V.WOLBER,H.G.KRAUSSLICH,
REMARK 1 AUTH 2 H.R.KALBITZER
REMARK 1 TITL A POSSIBLE REGULATION OF NEGATIVE FACTOR (NEF) ACTIVITY OF
REMARK 1 TITL 2 HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 BY THE VIRAL PROTEASE.
REMARK 1 REF EUR.J.BIOCHEM. V. 223 589 1994
REMARK 1 REFN ISSN 0014-2956
REMARK 1 PMID 8055930
REMARK 1 DOI 10.1111/J.1432-1033.1994.TB19029.X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES WERE CALCULATED WITH X-PLOR, V. 3.851 (BRUNGER,
REMARK 3 1992) USING A DISTANCE GEOMETRY/SIMULATED ANNEALING PROTOCOL
REMARK 3 (NILGES ET AL., FEBS LETT. 229, 317 (1988)). THE 3D STRUCTURE OF
REMARK 3 MYRISTOYLATED HIV-1 NEF ANCHOR
REMARK 3 DOMAIN (MYR-2-57) SOLVED BY TWO-DIMENSIONAL HOMONUCLEAR NMR
REMARK 3 SPECTROSCOPY IS BASED ON 540 EXPERIMENTAL RESTRAINTS:
REMARK 3 332 INTRARESIDUAL, 156 SEQUENTIAL AND MEDIUM RANGE (1<=|I-J|<=4),
REMARK 3 AND 10 LONG RANGE (|I-J|>=5) INTERPROTON
REMARK 3 DISTANCE RESTRAINTS; 42 TORSION ANGLE RESTRAINTS (PHI). NO
REMARK 3 RESTRAINTS FOR HYDROGEN BONDS WERE ADDED.
REMARK 4
REMARK 4 1QA5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-APR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000836.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 285
REMARK 210 PH : 4.6
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 1H
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; DMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AURELIA 2.0, X-PLOR 3.851
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 400
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 2
REMARK 210 CONFORMERS, SELECTION CRITERIA : TWO STRUCTURES WITH LOW TOTAL
REMARK 210 ENERGY WERE SELECTED SHOWING THE
REMARK 210 CONFORMATIONAL VARIETY OF THE
REMARK 210 FLEXIBLE DOMAIN
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK:
REMARK 210 THE COORDINATES OF 2 SIMULATED ANNEALING STRUCTURES ARE PRESENTED
REMARK 210 IN THIS ENTRY. THE STRUCTURE OF THE
REMARK 210 MYRISTOYLATED HIV-1 NEF ANCHOR DOMAIN IS HIGHLY FLEXIBLE AND NOT
REMARK 210 WELL DEFINED BY NMR RESTRAINTS. ONLY TWO
REMARK 210 SECONDARY STRUCTURE ELEMENTS CAN BE OBSERVED: A FIRST HELIX IN
REMARK 210 THE POSITIVE CLUSTER REGION FROM PRO14 TO ARG22
REMARK 210 AND A SECOND HELICAL REGION FROM ALA33 TO GLY41. ADDITIONALLY, THE
REMARK 210 N-TERMINAL MYRISTIC ACID RESIDUE
REMARK 210 CLOSELY INTERACTS WITH THE SIDE CHAIN OF TRP5 AND THEREBY FORMS A
REMARK 210 LOOP WITH GLY2, GLY3 AND LYS4 IN THE
REMARK 210 KINK REGION. TWO MODELS ARE PRESENTED TO DEMONSTRATE THE
REMARK 210 CONFORMATIONAL VARIETY OF THE STRUCTURES CALCULATED.
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: 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 6 86.30 50.18
REMARK 500 1 VAL A 11 154.70 58.08
REMARK 500 1 TRP A 13 81.03 -159.42
REMARK 500 1 PRO A 14 45.22 -80.66
REMARK 500 1 ARG A 22 -76.13 -87.45
REMARK 500 1 ALA A 23 -84.36 155.77
REMARK 500 1 GLU A 24 112.44 176.77
REMARK 500 1 ASP A 28 71.65 47.03
REMARK 500 1 ALA A 33 -79.78 -76.14
REMARK 500 1 SER A 34 -77.52 -87.89
REMARK 500 1 ARG A 35 -98.68 -100.32
REMARK 500 1 ASP A 36 -62.71 -125.66
REMARK 500 1 ALA A 49 -129.50 53.28
REMARK 500 1 ALA A 50 -153.65 53.36
REMARK 500 1 ASN A 52 85.54 44.17
REMARK 500 1 ALA A 54 -167.66 57.99
REMARK 500 2 LYS A 4 104.63 53.38
REMARK 500 2 GLU A 18 -70.47 -53.72
REMARK 500 2 ALA A 23 -170.89 52.57
REMARK 500 2 ALA A 27 -156.00 -125.90
REMARK 500 2 ALA A 32 135.89 168.35
REMARK 500 2 SER A 34 -89.29 -85.44
REMARK 500 2 ARG A 35 -91.89 -108.26
REMARK 500 2 SER A 46 78.66 -160.78
REMARK 500 2 ALA A 49 -145.86 50.32
REMARK 500 2 ALA A 50 128.07 61.89
REMARK 500 2 ASN A 51 -111.58 -131.34
REMARK 500 2 ALA A 53 -122.50 -170.65
REMARK 500 2 ALA A 54 148.20 63.88
REMARK 500 2 CYS A 55 128.67 -178.53
REMARK 500 2 ALA A 56 172.56 171.61
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 1 ARG A 17 0.31 SIDE CHAIN
REMARK 500 1 ARG A 19 0.30 SIDE CHAIN
REMARK 500 1 ARG A 21 0.31 SIDE CHAIN
REMARK 500 1 ARG A 22 0.32 SIDE CHAIN
REMARK 500 1 ARG A 35 0.32 SIDE CHAIN
REMARK 500 2 ARG A 17 0.32 SIDE CHAIN
REMARK 500 2 ARG A 19 0.32 SIDE CHAIN
REMARK 500 2 ARG A 21 0.31 SIDE CHAIN
REMARK 500 2 ARG A 22 0.30 SIDE CHAIN
REMARK 500 2 ARG A 35 0.32 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1QA5 A 2 57 UNP P04324 NEF_HV112 2 57
SEQADV 1QA5 MYR A 1 P04324 MODIFIED RESIDUE
SEQADV 1QA5 NH2 A 58 P04324 AMIDATION
SEQRES 1 A 58 MYR GLY GLY LYS TRP SER LYS SER SER VAL VAL GLY TRP
SEQRES 2 A 58 PRO ALA VAL ARG GLU ARG MET ARG ARG ALA GLU PRO ALA
SEQRES 3 A 58 ALA ASP GLY VAL GLY ALA ALA SER ARG ASP LEU GLU LYS
SEQRES 4 A 58 HIS GLY ALA ILE THR SER SER ASN THR ALA ALA ASN ASN
SEQRES 5 A 58 ALA ALA CYS ALA TRP NH2
HET MYR A 1 42
HET NH2 A 58 3
HETNAM MYR MYRISTIC ACID
HETNAM NH2 AMINO GROUP
FORMUL 1 MYR C14 H28 O2
FORMUL 1 NH2 H2 N
HELIX 1 1 VAL A 16 ARG A 22 1 7
HELIX 2 2 LEU A 37 GLY A 41 1 5
LINK C1 MYR A 1 N GLY A 2 1555 1555 1.31
LINK C TRP A 57 N NH2 A 58 1555 1555 1.30
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 - 21 20 Bytes