Header list of 1r6r.pdb file
Complete list - r 2 2 Bytes
HEADER VIRAL PROTEIN 16-OCT-03 1R6R
TITLE SOLUTION STRUCTURE OF DENGUE VIRUS CAPSID PROTEIN REVEALS A NEW FOLD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GENOME POLYPROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CAPSID PROTEIN C (RESIDUE 1-100);
COMPND 5 SYNONYM: CORE PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DENGUE VIRUS 2 PUERTO RICO/PR159-S1/1969;
SOURCE 3 ORGANISM_TAXID: 11066;
SOURCE 4 STRAIN: PR-159-S1;
SOURCE 5 GENE: CAPSID GENE;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)[RIL];
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET30A
KEYWDS ALPHA HELICAL, DIMER, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 21
MDLTYP MINIMIZED AVERAGE
AUTHOR L.MA,C.T.JONES,T.D.GROESCH,R.J.KUHN,C.B.POST
REVDAT 4 02-MAR-22 1R6R 1 REMARK
REVDAT 3 24-FEB-09 1R6R 1 VERSN
REVDAT 2 06-APR-04 1R6R 1 JRNL
REVDAT 1 17-FEB-04 1R6R 0
JRNL AUTH L.MA,C.T.JONES,T.D.GROESCH,R.J.KUHN,C.B.POST
JRNL TITL SOLUTION STRUCTURE OF DENGUE VIRUS CAPSID PROTEIN REVEALS
JRNL TITL 2 ANOTHER FOLD
JRNL REF PROC.NATL.ACAD.SCI.USA V. 101 3414 2004
JRNL REFN ISSN 0027-8424
JRNL PMID 14993605
JRNL DOI 10.1073/PNAS.0305892101
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.2, X-PLOR 3.8
REMARK 3 AUTHORS : DELAGIO, GRZESIEK, VUISTER, ZHU, PFEIFER, BAX
REMARK 3 (NMRPIPE), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1R6R COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-OCT-03.
REMARK 100 THE DEPOSITION ID IS D_1000020505.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300; 305
REMARK 210 PH : 6.0; 6.0
REMARK 210 IONIC STRENGTH : 50 MM SODIUM PHOSPHATE AND 200
REMARK 210 MM NACL; 50 MM SODIUM PHOSPHATE
REMARK 210 AND 200 MM NACL
REMARK 210 PRESSURE : 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.8 MM DEN2C PROTEIN U-15N, 13C;
REMARK 210 IN 90% H2O/10% D2O WITH 50 MM
REMARK 210 SODIUM PHOSPHATE AND 200 MM NACL
REMARK 210 AT PH 6.0. IN SHIGEMI TUBE; 1MM
REMARK 210 OR 2 MM DEN2C PROTEIN U-15N; IN
REMARK 210 90% H2O/10% D2O WITH 50 MM
REMARK 210 SODIUM PHOSPHATE AND 200 MM NACL
REMARK 210 AT PH 6.0. IN SHIGEMI TUBE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY 3
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 54
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : 20 ARBITRARILY SELECTED FROM
REMARK 210 53/54 CONFORMERS WITH NO
REMARK 210 CONSTRAINT VIOLATIONS LARGER
REMARK 210 THAN 0.3 ANGSTROM OR 5 DEGREES.
REMARK 210 MODEL 21 IS ENERGY MINIMIZED
REMARK 210 STRUCTURE AVERAGED OVER THE 53
REMARK 210 MODELS.
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 21
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY
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
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 VAL A 23 -26.00 -172.56
REMARK 500 1 MET A 37 -85.00 23.37
REMARK 500 1 ARG A 41 -146.17 56.76
REMARK 500 1 THR A 58 -8.68 -146.11
REMARK 500 1 PRO A 60 66.04 -104.70
REMARK 500 1 THR A 62 172.65 -57.96
REMARK 500 1 THR A 71 26.29 -163.68
REMARK 500 1 ILE A 72 -127.96 -114.80
REMARK 500 1 LYS A 74 -47.30 72.55
REMARK 500 1 ARG A 99 -62.14 68.41
REMARK 500 1 VAL B 23 -26.15 -172.53
REMARK 500 1 MET B 37 -77.32 -30.98
REMARK 500 1 ARG B 41 -147.85 56.85
REMARK 500 1 LEU B 44 19.79 56.92
REMARK 500 1 THR B 58 -8.68 -145.97
REMARK 500 1 PRO B 60 65.77 -104.87
REMARK 500 1 THR B 62 171.47 -57.85
REMARK 500 1 THR B 71 26.23 -163.75
REMARK 500 1 ILE B 72 -127.87 -114.92
REMARK 500 1 LYS B 74 -47.35 72.56
REMARK 500 1 ARG B 99 -62.31 68.38
REMARK 500 2 VAL A 23 -24.69 -169.09
REMARK 500 2 LEU A 35 30.37 -167.72
REMARK 500 2 ARG A 41 -99.14 54.00
REMARK 500 2 THR A 58 -9.73 -145.57
REMARK 500 2 PRO A 60 62.01 -105.35
REMARK 500 2 THR A 71 26.08 -164.22
REMARK 500 2 ILE A 72 -127.74 -104.19
REMARK 500 2 LYS A 74 -50.74 71.40
REMARK 500 2 VAL B 23 -24.23 -168.58
REMARK 500 2 LEU B 35 30.35 -167.46
REMARK 500 2 ARG B 41 -98.97 54.10
REMARK 500 2 THR B 58 -9.78 -145.18
REMARK 500 2 PRO B 60 62.27 -105.31
REMARK 500 2 THR B 71 26.23 -164.28
REMARK 500 2 ILE B 72 -127.88 -104.27
REMARK 500 2 LYS B 74 -50.91 71.26
REMARK 500 3 VAL A 23 -28.44 -172.35
REMARK 500 3 LEU A 35 55.81 -111.85
REMARK 500 3 ARG A 41 -97.80 52.36
REMARK 500 3 THR A 58 -8.96 -145.03
REMARK 500 3 PRO A 60 64.21 -105.09
REMARK 500 3 THR A 71 26.44 -167.12
REMARK 500 3 ILE A 72 -125.23 -98.32
REMARK 500 3 LYS A 74 -49.68 70.43
REMARK 500 3 ARG A 97 46.07 -95.63
REMARK 500 3 VAL B 23 -27.21 -171.77
REMARK 500 3 LEU B 35 30.77 -92.62
REMARK 500 3 MET B 37 -46.15 62.03
REMARK 500 3 ARG B 41 -97.31 52.44
REMARK 500
REMARK 500 THIS ENTRY HAS 364 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 22 0.25 SIDE CHAIN
REMARK 500 1 ARG A 32 0.22 SIDE CHAIN
REMARK 500 1 ARG A 41 0.29 SIDE CHAIN
REMARK 500 1 ARG A 55 0.28 SIDE CHAIN
REMARK 500 1 ARG A 68 0.21 SIDE CHAIN
REMARK 500 1 ARG A 82 0.23 SIDE CHAIN
REMARK 500 1 ARG A 85 0.31 SIDE CHAIN
REMARK 500 1 ARG A 90 0.25 SIDE CHAIN
REMARK 500 1 ARG A 97 0.32 SIDE CHAIN
REMARK 500 1 ARG A 98 0.21 SIDE CHAIN
REMARK 500 1 ARG A 99 0.29 SIDE CHAIN
REMARK 500 1 ARG A 100 0.29 SIDE CHAIN
REMARK 500 1 ARG B 22 0.25 SIDE CHAIN
REMARK 500 1 ARG B 32 0.22 SIDE CHAIN
REMARK 500 1 ARG B 41 0.29 SIDE CHAIN
REMARK 500 1 ARG B 55 0.28 SIDE CHAIN
REMARK 500 1 ARG B 68 0.21 SIDE CHAIN
REMARK 500 1 ARG B 82 0.22 SIDE CHAIN
REMARK 500 1 ARG B 85 0.31 SIDE CHAIN
REMARK 500 1 ARG B 90 0.25 SIDE CHAIN
REMARK 500 1 ARG B 97 0.32 SIDE CHAIN
REMARK 500 1 ARG B 98 0.21 SIDE CHAIN
REMARK 500 1 ARG B 99 0.29 SIDE CHAIN
REMARK 500 1 ARG B 100 0.29 SIDE CHAIN
REMARK 500 2 ARG A 22 0.32 SIDE CHAIN
REMARK 500 2 ARG A 32 0.31 SIDE CHAIN
REMARK 500 2 ARG A 41 0.31 SIDE CHAIN
REMARK 500 2 ARG A 55 0.28 SIDE CHAIN
REMARK 500 2 ARG A 68 0.21 SIDE CHAIN
REMARK 500 2 ARG A 82 0.32 SIDE CHAIN
REMARK 500 2 ARG A 85 0.31 SIDE CHAIN
REMARK 500 2 ARG A 90 0.32 SIDE CHAIN
REMARK 500 2 ARG A 97 0.32 SIDE CHAIN
REMARK 500 2 ARG A 98 0.29 SIDE CHAIN
REMARK 500 2 ARG A 99 0.31 SIDE CHAIN
REMARK 500 2 ARG A 100 0.21 SIDE CHAIN
REMARK 500 2 ARG B 22 0.32 SIDE CHAIN
REMARK 500 2 ARG B 32 0.31 SIDE CHAIN
REMARK 500 2 ARG B 41 0.31 SIDE CHAIN
REMARK 500 2 ARG B 55 0.28 SIDE CHAIN
REMARK 500 2 ARG B 68 0.21 SIDE CHAIN
REMARK 500 2 ARG B 82 0.32 SIDE CHAIN
REMARK 500 2 ARG B 85 0.31 SIDE CHAIN
REMARK 500 2 ARG B 90 0.32 SIDE CHAIN
REMARK 500 2 ARG B 97 0.32 SIDE CHAIN
REMARK 500 2 ARG B 98 0.29 SIDE CHAIN
REMARK 500 2 ARG B 99 0.31 SIDE CHAIN
REMARK 500 2 ARG B 100 0.21 SIDE CHAIN
REMARK 500 3 ARG A 22 0.22 SIDE CHAIN
REMARK 500 3 ARG A 32 0.31 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 504 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5973 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFT DATA OF THE SAME PROTEIN
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE RESIDUES 1-20 ARE MISSING FROM ALL THE
REMARK 999 MODELS. THE NMR EXPERIMENTAL DATA WERE OBTAINED
REMARK 999 USING PROTEIN INCLUDING THE MISSING RESIDUES.
REMARK 999 SINCE THE N-TERMINAL 20 RESIDUES ARE USTRUCTURED,
REMARK 999 THEY WERE EXCLUDED FROM THE STRUCTURE REFINEMENT.
DBREF 1R6R A 1 100 UNP P12823 POLG_DEN2P 1 100
DBREF 1R6R B 1 100 UNP P12823 POLG_DEN2P 1 100
SEQRES 1 A 100 MET ASN ASP GLN ARG LYS LYS ALA ARG ASN THR PRO PHE
SEQRES 2 A 100 ASN MET LEU LYS ARG GLU ARG ASN ARG VAL SER THR VAL
SEQRES 3 A 100 GLN GLN LEU THR LYS ARG PHE SER LEU GLY MET LEU GLN
SEQRES 4 A 100 GLY ARG GLY PRO LEU LYS LEU PHE MET ALA LEU VAL ALA
SEQRES 5 A 100 PHE LEU ARG PHE LEU THR ILE PRO PRO THR ALA GLY ILE
SEQRES 6 A 100 LEU LYS ARG TRP GLY THR ILE LYS LYS SER LYS ALA ILE
SEQRES 7 A 100 ASN VAL LEU ARG GLY PHE ARG LYS GLU ILE GLY ARG MET
SEQRES 8 A 100 LEU ASN ILE LEU ASN ARG ARG ARG ARG
SEQRES 1 B 100 MET ASN ASP GLN ARG LYS LYS ALA ARG ASN THR PRO PHE
SEQRES 2 B 100 ASN MET LEU LYS ARG GLU ARG ASN ARG VAL SER THR VAL
SEQRES 3 B 100 GLN GLN LEU THR LYS ARG PHE SER LEU GLY MET LEU GLN
SEQRES 4 B 100 GLY ARG GLY PRO LEU LYS LEU PHE MET ALA LEU VAL ALA
SEQRES 5 B 100 PHE LEU ARG PHE LEU THR ILE PRO PRO THR ALA GLY ILE
SEQRES 6 B 100 LEU LYS ARG TRP GLY THR ILE LYS LYS SER LYS ALA ILE
SEQRES 7 B 100 ASN VAL LEU ARG GLY PHE ARG LYS GLU ILE GLY ARG MET
SEQRES 8 B 100 LEU ASN ILE LEU ASN ARG ARG ARG ARG
HELIX 1 1 VAL A 26 PHE A 33 1 8
HELIX 2 2 LEU A 44 THR A 58 1 15
HELIX 3 3 THR A 62 GLY A 70 1 9
HELIX 4 4 LYS A 74 ASN A 96 1 23
HELIX 5 5 VAL B 26 PHE B 33 1 8
HELIX 6 6 LEU B 44 THR B 58 1 15
HELIX 7 7 THR B 62 GLY B 70 1 9
HELIX 8 8 LYS B 74 ASN B 96 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