Header list of 2b9z.pdb file
Complete list - r 9 2 Bytes
HEADER VIRAL PROTEIN 13-OCT-05 2B9Z
TITLE SOLUTION STRUCTURE OF FHV B2, A VIRAL SUPPRESSOR OF RNAI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: B2 PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: FLOCK HOUSE VIRUS;
SOURCE 3 ORGANISM_TAXID: 12287;
SOURCE 4 GENE: B2;
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: PETM-11
KEYWDS SYMMETRIC ANTIPARALLEL HOMODIMER, ALL ALPHA-HELICAL, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR A.LINGEL,B.SIMON,E.IZAURRALDE,M.SATTLER
REVDAT 4 09-MAR-22 2B9Z 1 REMARK SEQADV
REVDAT 3 24-FEB-09 2B9Z 1 VERSN
REVDAT 2 27-DEC-05 2B9Z 1 JRNL
REVDAT 1 29-NOV-05 2B9Z 0
JRNL AUTH A.LINGEL,B.SIMON,E.IZAURRALDE,M.SATTLER
JRNL TITL THE STRUCTURE OF THE FLOCK HOUSE VIRUS B2 PROTEIN, A VIRAL
JRNL TITL 2 SUPPRESSOR OF RNA INTERFERENCE, SHOWS A NOVEL MODE OF
JRNL TITL 3 DOUBLE-STRANDED RNA RECOGNITION.
JRNL REF EMBO REP. V. 6 1149 2005
JRNL REFN ISSN 1469-221X
JRNL PMID 16270100
JRNL DOI 10.1038/SJ.EMBOR.7400583
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.5, CNS 1.1
REMARK 3 AUTHORS : BRUNGER ET AL. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE EXPERIMENTALLY DETERMINED DISTANCE,
REMARK 3 DIHEDRAL AND DIPOLAR COUPLING RESTRAINTS WERE APPLIED IN A
REMARK 3 SIMULATED ANNEALING PROTOCOL USING ARIA AND CNS. NON-
REMARK 3 CRYSTALLOGRAPHIC SYMMETRY (NCS) RESTRAINTS WERE USED TO ENFORCE
REMARK 3 THE DIMER SYMMETRY. THE FINAL ENSEMBLE OF NMR STRUCTURES WAS
REMARK 3 REFINED IN A SHELL OF WATER MOLECULES.
REMARK 4
REMARK 4 2B9Z COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB.
REMARK 100 THE DEPOSITION ID IS D_1000034860.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 295
REMARK 210 PH : 6.3
REMARK 210 IONIC STRENGTH : 50 MM NAPI, 50 MM NACL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 0.2 - 1 MM 15N, 13C/15N OR
REMARK 210 2H/13C/15N LABELLED B2 PROTEIN
REMARK 210 IN 50 MM SODIUM PHOSPHATE PH 6.3,
REMARK 210 50 MM SODIUM CHLORIDE, 1 MM DTT,
REMARK 210 90% H2O / 10% D2O; 0.2 - 1 MM
REMARK 210 13C/15N LABELLED B2 PROTEIN IN
REMARK 210 50 MM SODIUM PHOSPHATE PH 6.3,
REMARK 210 50 MM SODIUM CHLORIDE, 1 MM DTT,
REMARK 210 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 900 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, NMRVIEW 5, TALOS, ARIA
REMARK 210 1.2, CNS 1.1
REMARK 210 METHOD USED : MOLECULAR DYNAMICS, SIMULATED
REMARK 210 ANNEALING
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
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: DISTANCE RESTRAINTS WERE DERIVED FROM 15N- OR 13C-RESOLVED
REMARK 210 3D NOESY. HN-N RESIDUAL DIPOLAR COUPLINGS WERE MEASURED USING A
REMARK 210 SPIN-STATE-SELECTIVE 1H,15N CORRELATION EXPERIMENT IN DILUTE
REMARK 210 LIQUID CRYSTALLINE MEDIUM. RESTRAINTS FOR THE BACKBONE ANGLES
REMARK 210 PHI AND PSI WERE DERIVED FROM TALOS. STEREOSPECIFIC ASSIGNMENTS
REMARK 210 OF LEU, VAL METHYL GROUPS WERE OBTAINED USING A 10% FRACTIONALLY
REMARK 210 13C-LABELLED SAMPLE.
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 2 MET A 1 101.46 54.27
REMARK 500 2 MET B 1 90.15 48.48
REMARK 500 3 SER A 26 -75.51 -67.06
REMARK 500 3 TYR A 27 -1.99 56.42
REMARK 500 3 PRO A 31 161.99 -46.80
REMARK 500 3 TYR B 27 8.89 49.97
REMARK 500 3 PRO B 31 152.36 -45.54
REMARK 500 4 ALA A 0 75.25 59.62
REMARK 500 4 ALA B 0 68.55 60.71
REMARK 500 4 GLU B 61 32.71 -97.44
REMARK 500 5 GLU A 61 36.57 -97.94
REMARK 500 5 PRO B 31 155.30 -46.64
REMARK 500 6 TYR A 27 6.99 55.16
REMARK 500 6 PRO A 31 157.30 -46.37
REMARK 500 6 ALA B 0 76.91 58.74
REMARK 500 6 TYR B 27 3.06 55.98
REMARK 500 6 PRO B 31 162.18 -46.22
REMARK 500 7 PRO A 31 150.35 -45.95
REMARK 500 8 ASP B 29 46.96 -85.93
REMARK 500 10 TYR A 27 6.14 55.04
REMARK 500 10 PRO A 31 153.49 -46.41
REMARK 500 10 TYR B 27 9.44 53.72
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2B9Z A 1 72 UNP P68831 B2_FHV 1 72
DBREF 2B9Z B 1 72 UNP P68831 B2_FHV 1 72
SEQADV 2B9Z GLY A -1 UNP P68831 CLONING ARTIFACT
SEQADV 2B9Z ALA A 0 UNP P68831 CLONING ARTIFACT
SEQADV 2B9Z GLY A 53 UNP P68831 SER 53 SEE REMARK 999
SEQADV 2B9Z GLY B -1 UNP P68831 CLONING ARTIFACT
SEQADV 2B9Z ALA B 0 UNP P68831 CLONING ARTIFACT
SEQADV 2B9Z GLY B 53 UNP P68831 SER 53 SEE REMARK 999
SEQRES 1 A 74 GLY ALA MET PRO SER LYS LEU ALA LEU ILE GLN GLU LEU
SEQRES 2 A 74 PRO ASP ARG ILE GLN THR ALA VAL GLU ALA ALA MET GLY
SEQRES 3 A 74 MET SER TYR GLN ASP ALA PRO ASN ASN VAL ARG ARG ASP
SEQRES 4 A 74 LEU ASP ASN LEU HIS ALA CYS LEU ASN LYS ALA LYS LEU
SEQRES 5 A 74 THR VAL GLY ARG MET VAL THR SER LEU LEU GLU LYS PRO
SEQRES 6 A 74 SER VAL VAL ALA TYR LEU GLU GLY LYS
SEQRES 1 B 74 GLY ALA MET PRO SER LYS LEU ALA LEU ILE GLN GLU LEU
SEQRES 2 B 74 PRO ASP ARG ILE GLN THR ALA VAL GLU ALA ALA MET GLY
SEQRES 3 B 74 MET SER TYR GLN ASP ALA PRO ASN ASN VAL ARG ARG ASP
SEQRES 4 B 74 LEU ASP ASN LEU HIS ALA CYS LEU ASN LYS ALA LYS LEU
SEQRES 5 B 74 THR VAL GLY ARG MET VAL THR SER LEU LEU GLU LYS PRO
SEQRES 6 B 74 SER VAL VAL ALA TYR LEU GLU GLY LYS
HELIX 1 1 SER A 3 GLY A 24 1 22
HELIX 2 2 SER A 26 ALA A 30 5 5
HELIX 3 3 PRO A 31 GLU A 61 1 31
HELIX 4 4 LYS A 62 GLY A 71 1 10
HELIX 5 5 SER B 3 GLY B 24 1 22
HELIX 6 6 PRO B 31 GLU B 61 1 31
HELIX 7 7 LYS B 62 GLY B 71 1 10
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 9 2 Bytes