Header list of 1x9v.pdb file
Complete list - r 2 2 Bytes
HEADER VIRAL PROTEIN 24-AUG-04 1X9V
TITLE DIMERIC STRUCTURE OF THE C-TERMINAL DOMAIN OF VPR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VPR PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: C-TERMINAL DOMAIN (RESIDUES 52-96);
COMPND 5 SYNONYM: VIRAL PROTEIN R;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED BY SOLID
SOURCE 4 PHASE. THE SEQUENCE OF THE PEPTIDE IS FOUND IN HUMAN
SOURCE 5 IMMUNODEFICIENCY VIRUS TYPE 1 (HIV-1)
KEYWDS ALPHA HELIX, ANTIPARALLEL HOMODIMER, LEUCINE-ZIPPER, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR S.BOURBIGOT,H.BELTZ,J.DENIS,N.MORELLET,B.P.ROQUES,Y.MELY,S.BOUAZIZ
REVDAT 3 02-MAR-22 1X9V 1 REMARK
REVDAT 2 24-FEB-09 1X9V 1 VERSN
REVDAT 1 14-JUN-05 1X9V 0
JRNL AUTH S.BOURBIGOT,H.BELTZ,J.DENIS,N.MORELLET,B.P.ROQUES,Y.MELY,
JRNL AUTH 2 S.BOUAZIZ
JRNL TITL THE C-TERMINAL DOMAIN OF THE HIV-1 REGULATORY PROTEIN VPR
JRNL TITL 2 ADOPTS AN ANTIPARALLEL DIMERIC STRUCTURE IN SOLUTION VIA ITS
JRNL TITL 3 LEUCINE-ZIPPER-LIKE DOMAIN
JRNL REF BIOCHEM.J. V. 387 333 2005
JRNL REFN ISSN 0264-6021
JRNL PMID 15571493
JRNL DOI 10.1042/BJ20041759
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.0, X-PLOR 3.851
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON 573 NOE
REMARK 3 -DERIVED DISTANCE CONSTRAINTS.
REMARK 4
REMARK 4 1X9V COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-AUG-04.
REMARK 100 THE DEPOSITION ID IS D_1000030121.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 3
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM VPR(52-96); 63% H2O, 7% D2O,
REMARK 210 30% CD3CN
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; DQF-COSY; 2D
REMARK 210 15N-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.0, FELIX 98.0
REMARK 210 METHOD USED : RESTRAINED SIMULATED ANNEALING,
REMARK 210 MOLECULAR DYNAMICS, ENERGY
REMARK 210 MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY, STRUCTURES WITH THE
REMARK 210 LEAST RESTRAINT VIOLATIONS
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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: 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 H2 ASP A 52 H THR A 53 1.33
REMARK 500 O ARG B 62 H GLN B 66 1.46
REMARK 500 O ARG A 62 H GLN A 66 1.46
REMARK 500 O TRP B 54 H VAL B 57 1.56
REMARK 500 O TRP A 54 H VAL A 57 1.56
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 THR A 53 -74.96 -47.50
REMARK 500 1 ARG A 77 35.61 -167.62
REMARK 500 1 ARG A 80 46.06 -90.91
REMARK 500 1 ILE A 84 71.50 46.85
REMARK 500 1 GLN A 86 75.24 -176.62
REMARK 500 1 THR A 89 38.90 38.26
REMARK 500 1 ARG A 90 -176.98 57.73
REMARK 500 1 ALA A 93 39.77 -99.26
REMARK 500 1 SER A 94 -160.85 53.64
REMARK 500 1 THR B 53 -74.98 -47.56
REMARK 500 1 ARG B 77 35.64 -167.65
REMARK 500 1 ARG B 80 45.92 -90.87
REMARK 500 1 ILE B 84 71.45 46.82
REMARK 500 1 GLN B 86 75.24 -176.61
REMARK 500 1 THR B 89 38.93 38.29
REMARK 500 1 ARG B 90 -176.96 57.63
REMARK 500 1 ALA B 93 39.81 -99.43
REMARK 500 1 SER B 94 -160.84 53.68
REMARK 500 2 ARG A 77 12.41 -140.39
REMARK 500 2 HIS A 78 145.77 67.72
REMARK 500 2 SER A 79 -145.46 -70.24
REMARK 500 2 ILE A 81 66.34 -69.62
REMARK 500 2 ILE A 83 -100.36 -72.08
REMARK 500 2 ILE A 84 -94.68 -134.16
REMARK 500 2 THR A 89 132.55 65.35
REMARK 500 2 ARG A 90 49.27 -85.69
REMARK 500 2 ASN A 91 85.32 -165.67
REMARK 500 2 ARG B 77 12.45 -140.44
REMARK 500 2 HIS B 78 145.69 67.79
REMARK 500 2 SER B 79 -145.47 -70.14
REMARK 500 2 ILE B 81 66.42 -69.55
REMARK 500 2 ILE B 83 -100.23 -72.08
REMARK 500 2 ILE B 84 -94.77 -134.25
REMARK 500 2 THR B 89 132.49 65.26
REMARK 500 2 ARG B 90 49.28 -85.64
REMARK 500 2 ASN B 91 85.39 -165.74
REMARK 500 3 ILE A 74 -34.69 -157.63
REMARK 500 3 ARG A 77 37.88 150.96
REMARK 500 3 ILE A 83 -86.17 -48.07
REMARK 500 3 ILE A 84 33.21 33.51
REMARK 500 3 GLN A 86 -168.92 44.15
REMARK 500 3 ARG A 88 54.69 -110.29
REMARK 500 3 THR A 89 -143.52 -133.94
REMARK 500 3 SER A 94 39.81 -155.35
REMARK 500 3 ILE B 74 -34.59 -157.62
REMARK 500 3 ARG B 77 37.79 151.03
REMARK 500 3 ILE B 83 -86.26 -48.07
REMARK 500 3 ILE B 84 33.23 33.55
REMARK 500 3 GLN B 86 -168.94 44.07
REMARK 500 3 ARG B 88 54.66 -110.31
REMARK 500
REMARK 500 THIS ENTRY HAS 156 RAMACHANDRAN OUTLIERS.
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 62 0.16 SIDE CHAIN
REMARK 500 1 ARG A 73 0.26 SIDE CHAIN
REMARK 500 1 ARG A 77 0.16 SIDE CHAIN
REMARK 500 1 ARG A 80 0.25 SIDE CHAIN
REMARK 500 1 ARG A 87 0.24 SIDE CHAIN
REMARK 500 1 ARG A 88 0.21 SIDE CHAIN
REMARK 500 1 ARG A 90 0.26 SIDE CHAIN
REMARK 500 1 ARG B 62 0.16 SIDE CHAIN
REMARK 500 1 ARG B 73 0.26 SIDE CHAIN
REMARK 500 1 ARG B 77 0.16 SIDE CHAIN
REMARK 500 1 ARG B 80 0.26 SIDE CHAIN
REMARK 500 1 ARG B 87 0.24 SIDE CHAIN
REMARK 500 1 ARG B 88 0.21 SIDE CHAIN
REMARK 500 1 ARG B 90 0.26 SIDE CHAIN
REMARK 500 2 ARG A 73 0.29 SIDE CHAIN
REMARK 500 2 ARG A 77 0.32 SIDE CHAIN
REMARK 500 2 ARG A 80 0.16 SIDE CHAIN
REMARK 500 2 ARG A 87 0.24 SIDE CHAIN
REMARK 500 2 ARG A 88 0.31 SIDE CHAIN
REMARK 500 2 ARG A 90 0.30 SIDE CHAIN
REMARK 500 2 ARG B 73 0.29 SIDE CHAIN
REMARK 500 2 ARG B 77 0.32 SIDE CHAIN
REMARK 500 2 ARG B 80 0.16 SIDE CHAIN
REMARK 500 2 ARG B 87 0.24 SIDE CHAIN
REMARK 500 2 ARG B 88 0.31 SIDE CHAIN
REMARK 500 2 ARG B 90 0.30 SIDE CHAIN
REMARK 500 3 ARG A 62 0.27 SIDE CHAIN
REMARK 500 3 ARG A 73 0.15 SIDE CHAIN
REMARK 500 3 ARG A 77 0.21 SIDE CHAIN
REMARK 500 3 ARG A 80 0.21 SIDE CHAIN
REMARK 500 3 ARG A 87 0.17 SIDE CHAIN
REMARK 500 3 ARG A 88 0.27 SIDE CHAIN
REMARK 500 3 ARG A 90 0.30 SIDE CHAIN
REMARK 500 3 ARG B 62 0.27 SIDE CHAIN
REMARK 500 3 ARG B 73 0.15 SIDE CHAIN
REMARK 500 3 ARG B 77 0.21 SIDE CHAIN
REMARK 500 3 ARG B 80 0.21 SIDE CHAIN
REMARK 500 3 ARG B 87 0.17 SIDE CHAIN
REMARK 500 3 ARG B 88 0.27 SIDE CHAIN
REMARK 500 3 ARG B 90 0.30 SIDE CHAIN
REMARK 500 4 ARG A 62 0.32 SIDE CHAIN
REMARK 500 4 ARG A 73 0.31 SIDE CHAIN
REMARK 500 4 ARG A 77 0.27 SIDE CHAIN
REMARK 500 4 ARG A 80 0.30 SIDE CHAIN
REMARK 500 4 ARG A 87 0.29 SIDE CHAIN
REMARK 500 4 ARG A 88 0.31 SIDE CHAIN
REMARK 500 4 ARG A 90 0.32 SIDE CHAIN
REMARK 500 4 ARG B 62 0.32 SIDE CHAIN
REMARK 500 4 ARG B 73 0.31 SIDE CHAIN
REMARK 500 4 ARG B 77 0.27 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 136 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1X9V A 52 96 UNP Q73369 Q73369_9HIV1 52 96
DBREF 1X9V B 52 96 UNP Q73369 Q73369_9HIV1 52 96
SEQRES 1 A 45 ASP THR TRP THR GLY VAL GLU ALA LEU ILE ARG ILE LEU
SEQRES 2 A 45 GLN GLN LEU LEU PHE ILE HIS PHE ARG ILE GLY CYS ARG
SEQRES 3 A 45 HIS SER ARG ILE GLY ILE ILE GLN GLN ARG ARG THR ARG
SEQRES 4 A 45 ASN GLY ALA SER LYS SER
SEQRES 1 B 45 ASP THR TRP THR GLY VAL GLU ALA LEU ILE ARG ILE LEU
SEQRES 2 B 45 GLN GLN LEU LEU PHE ILE HIS PHE ARG ILE GLY CYS ARG
SEQRES 3 B 45 HIS SER ARG ILE GLY ILE ILE GLN GLN ARG ARG THR ARG
SEQRES 4 B 45 ASN GLY ALA SER LYS SER
HELIX 1 1 TRP A 54 CYS A 76 1 23
HELIX 2 2 TRP B 54 CYS B 76 1 23
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 2 2 Bytes