Header list of 1r7f.pdb file
Complete list - r 2 2 Bytes
HEADER MEMBRANE PROTEIN 21-OCT-03 1R7F
TITLE NMR STRUCTURE OF THE MEMBRANE ANCHOR DOMAIN (1-31) OF THE
TITLE 2 NONSTRUCTURAL PROTEIN 5A (NS5A) OF HEPATITIS C VIRUS (ENSEMBLE OF 43
TITLE 3 STRUCTURES. SAMPLE IN 100MM SDS)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GENOME POLYPROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: NONSTRUCTURAL PROTEIN NS5A (P56)(RESIDUES 1973-2003 OF
COMPND 5 SWISS-PROT SEQUENCE P27958);
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 IS NATURALLY FOUND IN HEPATITIS C VIRUS.
KEYWDS MEMBRANE ANCHOR DOMAIN, HCV NS5A PROTEIN, PEPTIDE., MEMBRANE PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 43
AUTHOR F.PENIN,V.BRASS,N.APPEL,S.RAMBOARINA,R.MONTSERRET,D.FICHEUX,H.E.BLUM,
AUTHOR 2 R.BARTENSCHLAGER,D.MORADPOUR
REVDAT 5 02-MAR-22 1R7F 1 REMARK
REVDAT 4 24-FEB-09 1R7F 1 VERSN
REVDAT 3 28-SEP-04 1R7F 1 JRNL
REVDAT 2 07-SEP-04 1R7F 1 JRNL
REVDAT 1 10-AUG-04 1R7F 0
JRNL AUTH F.PENIN,V.BRASS,N.APPEL,S.RAMBOARINA,R.MONTSERRET,D.FICHEUX,
JRNL AUTH 2 H.E.BLUM,R.BARTENSCHLAGER,D.MORADPOUR
JRNL TITL STRUCTURE AND FUNCTION OF THE MEMBRANE ANCHOR DOMAIN OF
JRNL TITL 2 HEPATITIS C VIRUS NONSTRUCTURAL PROTEIN 5A.
JRNL REF J.BIOL.CHEM. V. 279 40835 2004
JRNL REFN ISSN 0021-9258
JRNL PMID 15247283
JRNL DOI 10.1074/JBC.M404761200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1, X-PLOR 3.85
REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1R7F COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-OCT-03.
REMARK 100 THE DEPOSITION ID IS D_1000020529.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 313
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.2MM NS5A[1-31], 10MM DTTD10
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY; DQF-COSY; 1H
REMARK 210 -13C HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR 6.1, X-PLOR 3.85
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING, MOLECULAR DYNAMICS,
REMARK 210 ENERGY MINIMIZATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 43
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
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 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 TRP A 4 -158.54 -169.01
REMARK 500 2 SER A 3 -81.85 -75.55
REMARK 500 4 TRP A 4 -177.71 60.86
REMARK 500 4 LEU A 5 -72.70 64.09
REMARK 500 5 LEU A 5 38.52 33.95
REMARK 500 5 GLN A 30 57.43 35.14
REMARK 500 6 SER A 3 -71.79 -125.30
REMARK 500 6 TRP A 4 -158.77 -158.96
REMARK 500 6 MET A 28 87.98 58.04
REMARK 500 7 SER A 3 -50.45 -168.18
REMARK 500 7 TRP A 4 -134.31 -77.67
REMARK 500 7 GLN A 30 76.04 51.80
REMARK 500 8 GLN A 30 74.35 51.78
REMARK 500 9 SER A 3 30.11 -99.78
REMARK 500 9 LEU A 27 96.65 67.10
REMARK 500 9 MET A 28 147.56 69.26
REMARK 500 10 SER A 3 53.07 -115.43
REMARK 500 10 LEU A 5 -62.26 66.29
REMARK 500 10 MET A 28 84.62 53.56
REMARK 500 10 GLN A 30 57.60 33.14
REMARK 500 11 SER A 3 -56.66 -131.40
REMARK 500 11 TRP A 4 -142.62 -165.46
REMARK 500 11 MET A 28 74.41 55.64
REMARK 500 11 GLN A 30 158.33 65.36
REMARK 500 12 SER A 3 -55.89 -132.90
REMARK 500 12 TRP A 4 63.37 30.56
REMARK 500 12 LEU A 27 99.93 64.00
REMARK 500 12 MET A 28 75.49 -119.20
REMARK 500 13 LEU A 27 -61.97 -123.42
REMARK 500 13 MET A 28 64.61 -162.46
REMARK 500 14 SER A 3 -81.78 -115.97
REMARK 500 14 TRP A 4 -68.59 64.37
REMARK 500 14 LEU A 27 109.01 68.14
REMARK 500 14 GLN A 30 36.92 -157.16
REMARK 500 15 TRP A 4 -166.35 -128.29
REMARK 500 16 SER A 3 -70.87 -121.70
REMARK 500 16 TRP A 4 -143.10 -156.59
REMARK 500 17 LEU A 27 115.32 64.84
REMARK 500 18 LEU A 5 -66.80 65.95
REMARK 500 18 LEU A 27 -82.00 -80.35
REMARK 500 18 MET A 28 113.25 -171.86
REMARK 500 19 SER A 3 54.12 -117.59
REMARK 500 19 TRP A 4 -142.45 -89.04
REMARK 500 20 SER A 3 -50.57 -147.70
REMARK 500 20 TRP A 4 -145.41 -75.13
REMARK 500 20 LEU A 27 72.50 57.19
REMARK 500 21 SER A 3 -71.98 -130.66
REMARK 500 22 TRP A 4 -139.85 -90.24
REMARK 500 22 PRO A 29 -167.36 -74.92
REMARK 500 23 TRP A 4 142.68 66.99
REMARK 500
REMARK 500 THIS ENTRY HAS 100 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 6 0.23 SIDE CHAIN
REMARK 500 2 ARG A 6 0.31 SIDE CHAIN
REMARK 500 3 ARG A 6 0.30 SIDE CHAIN
REMARK 500 4 ARG A 6 0.29 SIDE CHAIN
REMARK 500 5 ARG A 6 0.30 SIDE CHAIN
REMARK 500 6 ARG A 6 0.31 SIDE CHAIN
REMARK 500 7 ARG A 6 0.28 SIDE CHAIN
REMARK 500 8 ARG A 6 0.29 SIDE CHAIN
REMARK 500 9 ARG A 6 0.31 SIDE CHAIN
REMARK 500 10 ARG A 6 0.30 SIDE CHAIN
REMARK 500 11 ARG A 6 0.32 SIDE CHAIN
REMARK 500 12 ARG A 6 0.32 SIDE CHAIN
REMARK 500 13 ARG A 6 0.32 SIDE CHAIN
REMARK 500 14 ARG A 6 0.32 SIDE CHAIN
REMARK 500 15 ARG A 6 0.31 SIDE CHAIN
REMARK 500 16 ARG A 6 0.31 SIDE CHAIN
REMARK 500 17 ARG A 6 0.31 SIDE CHAIN
REMARK 500 18 ARG A 6 0.30 SIDE CHAIN
REMARK 500 19 ARG A 6 0.32 SIDE CHAIN
REMARK 500 20 ARG A 6 0.31 SIDE CHAIN
REMARK 500 21 ARG A 6 0.31 SIDE CHAIN
REMARK 500 22 ARG A 6 0.32 SIDE CHAIN
REMARK 500 23 ARG A 6 0.32 SIDE CHAIN
REMARK 500 24 ARG A 6 0.31 SIDE CHAIN
REMARK 500 25 ARG A 6 0.32 SIDE CHAIN
REMARK 500 26 ARG A 6 0.32 SIDE CHAIN
REMARK 500 27 ARG A 6 0.32 SIDE CHAIN
REMARK 500 28 ARG A 6 0.30 SIDE CHAIN
REMARK 500 29 ARG A 6 0.32 SIDE CHAIN
REMARK 500 30 ARG A 6 0.31 SIDE CHAIN
REMARK 500 31 ARG A 6 0.32 SIDE CHAIN
REMARK 500 32 ARG A 6 0.32 SIDE CHAIN
REMARK 500 33 ARG A 6 0.32 SIDE CHAIN
REMARK 500 34 ARG A 6 0.30 SIDE CHAIN
REMARK 500 35 ARG A 6 0.30 SIDE CHAIN
REMARK 500 36 ARG A 6 0.29 SIDE CHAIN
REMARK 500 37 ARG A 6 0.27 SIDE CHAIN
REMARK 500 38 ARG A 6 0.32 SIDE CHAIN
REMARK 500 39 ARG A 6 0.31 SIDE CHAIN
REMARK 500 40 ARG A 6 0.32 SIDE CHAIN
REMARK 500 41 ARG A 6 0.32 SIDE CHAIN
REMARK 500 42 ARG A 6 0.31 SIDE CHAIN
REMARK 500 43 ARG A 6 0.30 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1R7C RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE MEMBRANE ANCHOR DOMAIN (1-31) OF THE
REMARK 900 NONSTRUCTURAL PROTEIN 5A (NS5A) OF HEPATITIS C VIRUS. (MINIMIZED
REMARK 900 AVERAGE STRUCTURE, SAMPLE IN 50% TFE)
REMARK 900 RELATED ID: 1R7D RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE MEMBRANE ANCHOR DOMAIN (1-31) OF THE
REMARK 900 NONSTRUCTURAL PROTEIN 5A (NS5A) OF HEPATITIS C VIRUS. (ENSEMBLE OF
REMARK 900 51 STRUCTURES, SAMPLE IN 50% TFE)
REMARK 900 RELATED ID: 1R7E RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE MEMBRANE ANCHOR DOMAIN (1-31) OF THE
REMARK 900 NONSTRUCTURAL PROTEIN 5A (NS5A) OF HEPATITIS C VIRUS. (MINIMIZED
REMARK 900 AVERAGE STRUCTURE, SAMPLE IN 100MM SDS.)
REMARK 900 RELATED ID: 1R7G RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE MEMBRANE ANCHOR DOMAIN (1-31) OF THE
REMARK 900 NONSTRUCTURAL PROTEIN 5A (NS5A) OF HEPATITIS C VIRUS. (MINIMIZED
REMARK 900 AVERAGE STRUCTURE, SAMPLE IN 100MM DPC)
DBREF 1R7F A 1 31 UNP P27958 POLG_HCVH 1973 2003
SEQRES 1 A 31 SER GLY SER TRP LEU ARG ASP ILE TRP ASP TRP ILE CYS
SEQRES 2 A 31 GLU VAL LEU SER ASP PHE LYS THR TRP LEU LYS ALA LYS
SEQRES 3 A 31 LEU MET PRO GLN LEU
HELIX 1 1 ASP A 7 GLU A 14 1 8
HELIX 2 2 VAL A 15 MET A 28 1 14
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