Header list of 1cwx.pdb file
Complete list - 16 20 Bytes
HEADER VIRAL PROTEIN 27-AUG-99 1CWX
TITLE SOLUTION STRUCTURE OF THE HEPATITIS C VIRUS N-TERMINAL CAPSID PROTEIN
TITLE 2 2-45 [C-HCV(2-45)]
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HEPATITIS C VIRUS CAPSID PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: N-TERMINAL FRAGMENT;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THE PROTEIN WAS CHEMICALLY SYNTHESIZED. THIS SEQUENCE
SOURCE 4 OCCURS NATURALLY IN HEPATITIS C VIRUS (GENOTYPE 1A ISOLATE H77)..
KEYWDS HELIX-LOOP-HELIX, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 4
AUTHOR L.LADAVIERE,G.DELEAGE,R.MONTSERRET,P.DALBON,M.JOLIVET,F.PENIN
REVDAT 3 16-FEB-22 1CWX 1 REMARK
REVDAT 2 24-FEB-09 1CWX 1 VERSN
REVDAT 1 30-AUG-99 1CWX 0
JRNL AUTH L.LADAVIERE,G.DELEAGE,R.MONTSERRET,P.DALBON,M.JOLIVET,
JRNL AUTH 2 F.PENIN
JRNL TITL STRUCTURAL ANALYSIS OF THE IMMUNODOMINANT ANTIGENIC REGION
JRNL TITL 2 OF THE HEPATITIS C VIRUS CAPSID PROTEIN BY NMR
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 5.1, X-PLOR 3.1
REMARK 3 AUTHORS : VARIAN (VNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1CWX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-AUG-99.
REMARK 100 THE DEPOSITION ID IS D_1000009594.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 5.9
REMARK 210 IONIC STRENGTH : 0.1M NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 40% D2-TRIFLUOROETHANOL;0.01M
REMARK 210 SODIUM PHOSPHATE;0.1M NACL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY; 2D ROESY; 2D
REMARK 210 TOCSY
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 5.1, X-PLOR 3.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING MOLECULAR DYNAMICS
REMARK 210 MATRIX RELAXATION
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 4
REMARK 210 CONFORMERS, SELECTION CRITERIA : MOST CONVERGENT STRUCTURES AT
REMARK 210 THE LEVEL OF BOTH HELICES. NOTE
REMARK 210 THAT 23 STRUCTURES OVER 50 HAD
REMARK 210 NO RESTRAINT VIOLATION > 0.5
REMARK 210 ANGSTROM.
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 4
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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 THR A 2 89.37 -179.90
REMARK 500 1 LYS A 5 -51.52 164.29
REMARK 500 1 LYS A 9 -49.94 179.45
REMARK 500 1 THR A 10 -80.39 -85.71
REMARK 500 1 ARG A 12 -174.80 63.23
REMARK 500 1 ASN A 13 169.28 -45.02
REMARK 500 1 THR A 14 -38.29 -173.66
REMARK 500 1 ARG A 17 -45.57 120.76
REMARK 500 1 GLN A 19 41.26 -86.71
REMARK 500 1 ASP A 20 -43.16 -155.39
REMARK 500 1 GLN A 28 -10.28 -48.14
REMARK 500 1 ILE A 29 -6.72 80.37
REMARK 500 1 ARG A 39 94.09 -52.77
REMARK 500 2 THR A 2 -89.01 59.98
REMARK 500 2 ASN A 3 84.54 -164.66
REMARK 500 2 LYS A 9 149.65 -173.71
REMARK 500 2 LYS A 11 -53.35 -173.05
REMARK 500 2 ARG A 12 129.09 61.86
REMARK 500 2 THR A 14 -43.55 -170.67
REMARK 500 2 ASN A 15 116.25 -164.65
REMARK 500 2 ARG A 17 -57.26 161.42
REMARK 500 2 GLN A 19 43.99 -91.27
REMARK 500 2 ASP A 20 -39.98 -151.52
REMARK 500 2 PRO A 24 -72.97 -77.21
REMARK 500 2 ILE A 29 -12.09 83.26
REMARK 500 2 ARG A 38 39.25 -87.58
REMARK 500 3 ASN A 3 96.18 -176.65
REMARK 500 3 LYS A 9 -90.03 -150.93
REMARK 500 3 THR A 10 -73.36 79.96
REMARK 500 3 LYS A 11 127.95 62.59
REMARK 500 3 ARG A 12 -179.69 50.47
REMARK 500 3 ASN A 13 -66.37 -149.98
REMARK 500 3 ARG A 17 -57.96 147.93
REMARK 500 3 GLN A 19 40.60 -89.49
REMARK 500 3 ASP A 20 -43.06 -153.89
REMARK 500 3 ARG A 39 96.19 -50.06
REMARK 500 4 THR A 2 -74.63 -157.98
REMARK 500 4 LYS A 5 79.68 61.44
REMARK 500 4 GLN A 7 -90.04 -75.83
REMARK 500 4 ARG A 8 99.75 -174.09
REMARK 500 4 LYS A 9 -88.10 -163.13
REMARK 500 4 THR A 10 172.92 174.71
REMARK 500 4 LYS A 11 177.77 -58.20
REMARK 500 4 ASN A 15 92.84 -47.39
REMARK 500 4 ARG A 17 -47.50 124.49
REMARK 500 4 GLN A 19 44.80 -89.37
REMARK 500 4 ASP A 20 -41.81 -157.26
REMARK 500 4 GLN A 28 -33.67 -135.95
REMARK 500 4 ILE A 29 -12.95 85.34
REMARK 500 4 PRO A 37 -100.62 -77.22
REMARK 500
REMARK 500 THIS ENTRY HAS 52 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 8 0.32 SIDE CHAIN
REMARK 500 1 ARG A 12 0.31 SIDE CHAIN
REMARK 500 1 ARG A 16 0.29 SIDE CHAIN
REMARK 500 1 ARG A 17 0.24 SIDE CHAIN
REMARK 500 1 ARG A 38 0.30 SIDE CHAIN
REMARK 500 1 ARG A 39 0.24 SIDE CHAIN
REMARK 500 1 ARG A 42 0.28 SIDE CHAIN
REMARK 500 2 ARG A 8 0.31 SIDE CHAIN
REMARK 500 2 ARG A 12 0.27 SIDE CHAIN
REMARK 500 2 ARG A 16 0.08 SIDE CHAIN
REMARK 500 2 ARG A 17 0.26 SIDE CHAIN
REMARK 500 2 ARG A 38 0.30 SIDE CHAIN
REMARK 500 2 ARG A 39 0.20 SIDE CHAIN
REMARK 500 2 ARG A 42 0.30 SIDE CHAIN
REMARK 500 3 ARG A 8 0.25 SIDE CHAIN
REMARK 500 3 ARG A 12 0.23 SIDE CHAIN
REMARK 500 3 ARG A 16 0.31 SIDE CHAIN
REMARK 500 3 ARG A 17 0.19 SIDE CHAIN
REMARK 500 3 ARG A 38 0.27 SIDE CHAIN
REMARK 500 3 ARG A 39 0.20 SIDE CHAIN
REMARK 500 3 ARG A 42 0.32 SIDE CHAIN
REMARK 500 4 ARG A 8 0.32 SIDE CHAIN
REMARK 500 4 ARG A 12 0.31 SIDE CHAIN
REMARK 500 4 ARG A 17 0.23 SIDE CHAIN
REMARK 500 4 ARG A 38 0.32 SIDE CHAIN
REMARK 500 4 ARG A 39 0.29 SIDE CHAIN
REMARK 500 4 ARG A 42 0.25 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1CWX A 1 44 UNP P27958 POLG_HCVH 2 45
SEQRES 1 A 44 SER THR ASN PRO LYS PRO GLN ARG LYS THR LYS ARG ASN
SEQRES 2 A 44 THR ASN ARG ARG PRO GLN ASP VAL LYS PHE PRO GLY GLY
SEQRES 3 A 44 GLY GLN ILE VAL GLY GLY VAL TYR LEU LEU PRO ARG ARG
SEQRES 4 A 44 GLY PRO ARG LEU GLY
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 - 16 20 Bytes