Header list of 2ari.pdb file
Complete list - 9 20 Bytes
HEADER VIRAL PROTEIN 19-AUG-05 2ARI
TITLE SOLUTION STRUCTURE OF MICELLE-BOUND FUSION DOMAIN OF HIV-1 GP41
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ENVELOPE POLYPROTEIN GP160;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: 30 N-TERMINAL RESIDUES, TRANSMEMBRANE GLYCOPROTEIN (GP41);
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;
SOURCE 3 ORGANISM_TAXID: 11676;
SOURCE 4 GENE: ENV;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET28A(+)
KEYWDS HIV, GP41, FUSION, MEMBRANE, PROTEIN, MICELLE, VIRUS, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR C.P.JARONIEC,J.D.KAUFMAN,S.J.STAHL,M.VIARD,R.BLUMENTHAL,
AUTHOR 2 P.T.WINGFIELD,A.BAX
REVDAT 3 09-MAR-22 2ARI 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2ARI 1 VERSN
REVDAT 1 20-DEC-05 2ARI 0
JRNL AUTH C.P.JARONIEC,J.D.KAUFMAN,S.J.STAHL,M.VIARD,R.BLUMENTHAL,
JRNL AUTH 2 P.T.WINGFIELD,A.BAX
JRNL TITL STRUCTURE AND DYNAMICS OF MICELLE-ASSOCIATED HUMAN
JRNL TITL 2 IMMUNODEFICIENCY VIRUS GP41 FUSION DOMAIN.
JRNL REF BIOCHEMISTRY V. 44 16167 2005
JRNL REFN ISSN 0006-2960
JRNL PMID 16331977
JRNL DOI 10.1021/BI051672A
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, X-PLOR-NIH 2.9.4
REMARK 3 AUTHORS : BRUKER (XWINNMR), SCHWIETERS (X-PLOR-NIH)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 192 RESTRAINTS. 57 ARE
REMARK 3 RESIDUAL DIPOLAR COUPLING (RDC) RESTRAINTS, 74 ARE NOE-DERIVED
REMARK 3 DISTANCE RESTRAINTS, 38 ARE TALOS-DERIVED LOOSE (MINIMUM +/- 30
REMARK 3 DEGREES FROM TARGET VALUE) DIHEDRAL ANGLE RESTRAINTS, AND 23 ARE
REMARK 3 3J_HNHA RESTRAINTS. NOTE THAT RDC RESTRAINTS WERE INCLUDED ONLY
REMARK 3 FOR THE LEAST MOBILE RESIDUES ILE-4 TO MET-19 (WITH S2 > 0.65),
REMARK 3 DIHEDRAL RESTRAINTS WERE INCLUDED FOR RESIDUES ILE-4 TO ALA-22,
REMARK 3 NOE AND 3J_HNHA RESTRAINTS WERE INCLUDED FOR RESIDUES VAL-2 TO MET-
REMARK 3 24. ALSO NOTE THAT THE RESIDUE INDEX IN PDB AND CONSTRAINTS FILES
REMARK 3 IS SUCH THAT HIV-1 GP41 FUSION DOMAIN RESIDUE I IS ACTUALLY
REMARK 3 LABELED AS I+1.
REMARK 4
REMARK 4 2ARI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-SEP-05.
REMARK 100 THE DEPOSITION ID IS D_1000034227.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298
REMARK 210 PH : 6.5; 6.5
REMARK 210 IONIC STRENGTH : 75 MM SODIUM DODECYL SULFATE; 25
REMARK 210 MM SODIUM PHOSPHATE; 0.05% (W/V)
REMARK 210 SODIUM AZIDE; 75 MM SODIUM
REMARK 210 DODECYL SULFATE DEUTERATED; 25
REMARK 210 MM SODIUM PHOSPHATE; 0.05% (W/V)
REMARK 210 SODIUM AZIDE
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.7 MM HIV-1 GP41 FUSION DOMAIN
REMARK 210 U-2H, 13C, 15N; 75 MM SODIUM
REMARK 210 DODECYL SULFATE; 25 MM SODIUM
REMARK 210 PHOSPHATE BUFFER PH 6.5; 0.05%
REMARK 210 (W/V) SODIUM AZIDE; 93% H2O, 7%
REMARK 210 D2O; 0.7 MM HIV-1 GP41 FUSION
REMARK 210 DOMAIN U-15N; 75 MM SODIUM
REMARK 210 DODECYL SULFATE DEUTERATED; 25
REMARK 210 MM SODIUM PHOSPHATE BUFFER PH
REMARK 210 6.5; 0.05% (W/V) SODIUM AZIDE;
REMARK 210 93% H2O, 7% D2O; 0.7 MM HIV-1
REMARK 210 GP41 FUSION DOMAIN U-2H, 13C,
REMARK 210 15N; 75 MM SODIUM DODECYL
REMARK 210 SULFATE; 25 MM SODIUM PHOSPHATE
REMARK 210 BUFFER PH 6.5; 0.05% (W/V)
REMARK 210 SODIUM AZIDE; 93% H2O, 7% D2O;
REMARK 210 SAMPLE ALIGNED WITH RESPECT TO
REMARK 210 THE MAGNETIC FIELD USING A
REMARK 210 STRETCHED POLYACRYALMIDE GEL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_HNCO; 3D_HNCA; 3D_HN(CO)CA;
REMARK 210 3D_HN(CA)CB; 2D_HNCG; 3D_15N-
REMARK 210 SEPARATED_TOCSY; 3D_15N-
REMARK 210 SEPARATED_NOESY; 3D_HNHA; 2D_
REMARK 210 IPAP-HSQC_JNH; 3D_HNCO_JNH; 3D_
REMARK 210 QJ-HNCO_JNCO; 3D_HNCO_JCOCA; 3D_
REMARK 210 HN(CO)CA_JCACB
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.5, NMRPIPE 2.3, SPARKY
REMARK 210 3.11
REMARK 210 METHOD USED : SIMULATED ANNEALING MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY. RESIDUAL DIPOLAR COUPLINGS WERE MEASURED FOR A
REMARK 210 PEPTIDE-MICELLE COMPLEX ALIGNED WITH RESPECT TO THE MAGNETIC
REMARK 210 FIELD USING A STRETCHED POLYACRYAMIDE GEL.
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 1-30
REMARK 465 RES C SSSEQI
REMARK 465 PRO A 1
REMARK 465 ASP A 32
REMARK 465 TYR A 33
REMARK 465 LYS A 34
REMARK 465 ASP A 35
REMARK 465 ASP A 36
REMARK 465 ASP A 37
REMARK 465 ASP A 38
REMARK 465 LYS A 39
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 SER A 24 43.35 -80.12
REMARK 500 1 MET A 25 90.55 50.46
REMARK 500 1 THR A 26 7.06 -69.64
REMARK 500 1 LEU A 27 -80.19 -59.69
REMARK 500 1 THR A 28 -23.02 -164.90
REMARK 500 1 GLN A 30 -95.95 -67.27
REMARK 500 2 VAL A 3 -59.38 63.70
REMARK 500 2 ALA A 23 36.13 -72.74
REMARK 500 2 SER A 24 52.74 -160.08
REMARK 500 2 MET A 25 100.39 53.79
REMARK 500 2 THR A 26 -176.30 -57.37
REMARK 500 2 LEU A 27 -73.06 -67.80
REMARK 500 2 THR A 28 16.76 -172.97
REMARK 500 2 VAL A 29 176.97 -58.30
REMARK 500 3 VAL A 3 102.27 55.07
REMARK 500 3 SER A 24 45.16 -79.60
REMARK 500 3 MET A 25 84.39 51.51
REMARK 500 3 LEU A 27 90.66 -59.81
REMARK 500 3 VAL A 29 -163.72 -62.75
REMARK 500 3 GLN A 30 170.34 -59.16
REMARK 500 4 VAL A 3 -93.86 52.25
REMARK 500 4 SER A 24 39.35 -79.92
REMARK 500 4 VAL A 29 -164.62 -59.82
REMARK 500 5 VAL A 3 -95.78 52.31
REMARK 500 5 ILE A 5 20.27 -71.09
REMARK 500 5 SER A 24 42.49 -79.43
REMARK 500 5 MET A 25 92.84 53.10
REMARK 500 5 THR A 28 -147.80 53.03
REMARK 500 6 VAL A 3 -0.19 58.69
REMARK 500 6 SER A 24 40.30 -79.68
REMARK 500 6 MET A 25 -155.79 51.45
REMARK 500 6 THR A 26 85.73 -68.19
REMARK 500 6 LEU A 27 171.08 56.06
REMARK 500 6 VAL A 29 89.84 -67.81
REMARK 500 6 GLN A 30 82.77 -62.08
REMARK 500 7 VAL A 3 16.37 56.19
REMARK 500 7 MET A 20 23.72 -77.36
REMARK 500 7 SER A 24 35.52 -78.76
REMARK 500 7 MET A 25 88.15 51.56
REMARK 500 7 LEU A 27 -47.59 -170.10
REMARK 500 7 VAL A 29 85.36 -66.90
REMARK 500 7 GLN A 30 -158.28 52.38
REMARK 500 8 VAL A 3 124.74 59.50
REMARK 500 8 MET A 25 99.46 53.01
REMARK 500 8 THR A 26 -17.75 -164.51
REMARK 500 8 LEU A 27 -53.84 -169.54
REMARK 500 9 VAL A 3 147.50 60.27
REMARK 500 9 MET A 25 91.74 51.81
REMARK 500 9 GLN A 30 -7.70 -57.35
REMARK 500 10 SER A 24 31.01 -79.64
REMARK 500
REMARK 500 THIS ENTRY HAS 151 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2ARI A 2 31 UNP P03376 ENV_HV1PV 512 541
SEQADV 2ARI PRO A 1 UNP P03376 CLONING ARTIFACT
SEQADV 2ARI ASP A 32 UNP P03376 CLONING ARTIFACT
SEQADV 2ARI TYR A 33 UNP P03376 CLONING ARTIFACT
SEQADV 2ARI LYS A 34 UNP P03376 CLONING ARTIFACT
SEQADV 2ARI ASP A 35 UNP P03376 CLONING ARTIFACT
SEQADV 2ARI ASP A 36 UNP P03376 CLONING ARTIFACT
SEQADV 2ARI ASP A 37 UNP P03376 CLONING ARTIFACT
SEQADV 2ARI ASP A 38 UNP P03376 CLONING ARTIFACT
SEQADV 2ARI LYS A 39 UNP P03376 CLONING ARTIFACT
SEQRES 1 A 39 PRO ALA VAL GLY ILE GLY ALA LEU PHE LEU GLY PHE LEU
SEQRES 2 A 39 GLY ALA ALA GLY SER THR MET GLY ALA ALA SER MET THR
SEQRES 3 A 39 LEU THR VAL GLN ALA ASP TYR LYS ASP ASP ASP ASP LYS
HELIX 1 1 ILE A 5 GLY A 21 1 17
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 - 9 20 Bytes