Header list of 2gji.pdb file
Complete list - r 9 2 Bytes
HEADER METAL BINDING PROTEIN 30-MAR-06 2GJI TITLE NMR SOLUTION STRUCTURE OF VP9 FROM WHITE SPOT SYNDROME VIRUS COMPND MOL_ID: 1; COMPND 2 MOLECULE: WSV230; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: VP9; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SHRIMP WHITE SPOT SYNDROME VIRUS; SOURCE 3 ORGANISM_TAXID: 92652; SOURCE 4 GENE: WSV230; 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: PET15B KEYWDS WSSV, FERREDOXIN FOLD, METAL BINDING, METAL BINDING PROTEIN EXPDTA SOLUTION NMR NUMMDL 10 AUTHOR Y.LIU,J.L.WU,J.X.SONG,J.SIVARAMAN,C.L.HEW REVDAT 4 09-MAR-22 2GJI 1 REMARK SEQADV REVDAT 3 24-FEB-09 2GJI 1 VERSN REVDAT 2 31-OCT-06 2GJI 1 JRNL REVDAT 1 19-SEP-06 2GJI 0 JRNL AUTH Y.LIU,J.L.WU,J.X.SONG,J.SIVARAMAN,C.L.HEW JRNL TITL IDENTIFICATION OF A NOVEL NONSTRUCTURAL PROTEIN, VP9, FROM JRNL TITL 2 WHITE SPOT SYNDROME VIRUS: ITS STRUCTURE REVEALS A JRNL TITL 3 FERREDOXIN FOLD WITH SPECIFIC METAL BINDING SITES JRNL REF J.VIROL. V. 80 10419 2006 JRNL REFN ISSN 0022-538X JRNL PMID 16956937 JRNL DOI 10.1128/JVI.00698-06 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : NMRPIPE 2004, CYANA 2.1 REMARK 3 AUTHORS : DELAGLIO, F. (NMRPIPE), GUNTERT, P. (CYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2GJI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-APR-06. REMARK 100 THE DEPOSITION ID IS D_1000037195. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6.72 REMARK 210 IONIC STRENGTH : 20MM PHOSPHATE BUFFER REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : 20MM PHOSPHATE BUFFER, 3MM VP9; REMARK 210 90% H2O, 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; HCCH-TOCSY; REMARK 210 HNCACB; CBCA(CO)NH; HSQC REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE; DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CYANA 2.1, NMRVIEW 5.2.2 REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10 REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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: 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 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 MODELS 1-10 REMARK 465 RES C SSSEQI REMARK 465 GLY A -2 REMARK 465 SER A -1 REMARK 465 HIS A 0 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 ASP A 7 40.36 -102.54 REMARK 500 1 GLN A 49 107.61 -54.23 REMARK 500 2 ASP A 7 43.71 -93.03 REMARK 500 2 LEU A 65 -74.08 -53.09 REMARK 500 3 ALA A 2 52.40 -110.14 REMARK 500 3 ASP A 7 44.06 -95.15 REMARK 500 3 ARG A 41 30.80 -95.67 REMARK 500 4 ARG A 41 30.15 -94.99 REMARK 500 4 GLN A 49 109.52 -56.84 REMARK 500 4 LEU A 65 -74.73 -59.64 REMARK 500 4 PRO A 79 -179.77 -69.80 REMARK 500 5 ALA A 2 66.79 -119.90 REMARK 500 5 ASP A 7 37.63 -95.07 REMARK 500 5 ASP A 16 73.85 51.99 REMARK 500 5 GLN A 49 109.59 -59.20 REMARK 500 5 LEU A 65 -74.29 -53.78 REMARK 500 6 ASP A 7 36.00 -97.73 REMARK 500 6 ARG A 41 30.34 -95.74 REMARK 500 6 LEU A 65 -73.79 -51.68 REMARK 500 7 ASP A 7 43.93 -93.16 REMARK 500 7 ARG A 41 30.73 -95.53 REMARK 500 8 ALA A 2 62.53 -107.21 REMARK 500 8 LEU A 65 -70.07 -54.98 REMARK 500 8 PRO A 79 74.48 -69.72 REMARK 500 8 THR A 80 83.49 47.65 REMARK 500 8 THR A 81 60.12 -161.32 REMARK 500 9 ALA A 2 64.64 -103.17 REMARK 500 9 THR A 3 146.11 -173.84 REMARK 500 9 ASP A 7 39.78 -94.95 REMARK 500 9 ASP A 16 75.12 54.15 REMARK 500 9 ARG A 41 32.18 -95.54 REMARK 500 9 THR A 80 43.51 37.33 REMARK 500 10 ASP A 7 43.40 -92.84 REMARK 500 10 LEU A 65 -71.05 -58.69 REMARK 500 10 PRO A 75 98.46 -69.75 REMARK 500 10 THR A 81 77.84 -116.14 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 2GJ2 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF THE SAME PROTEIN DBREF 2GJI A 1 82 UNP Q91LD0 Q91LD0_WSSV 1 82 SEQADV 2GJI GLY A -2 UNP Q91LD0 CLONING ARTIFACT SEQADV 2GJI SER A -1 UNP Q91LD0 CLONING ARTIFACT SEQADV 2GJI HIS A 0 UNP Q91LD0 CLONING ARTIFACT SEQRES 1 A 85 GLY SER HIS MET ALA THR PHE GLN THR ASP ALA ASP PHE SEQRES 2 A 85 LEU LEU VAL GLY ASP ASP THR SER ARG TYR GLU GLU VAL SEQRES 3 A 85 MET LYS THR PHE ASP THR VAL GLU ALA VAL ARG LYS SER SEQRES 4 A 85 ASP LEU ASP ASP ARG VAL TYR MET VAL CYS LEU LYS GLN SEQRES 5 A 85 GLY SER THR PHE VAL LEU ASN GLY GLY ILE GLU GLU LEU SEQRES 6 A 85 ARG LEU LEU THR GLY ASP SER THR LEU GLU ILE GLN PRO SEQRES 7 A 85 MET ILE VAL PRO THR THR GLU HELIX 1 1 ARG A 19 THR A 26 1 8 HELIX 2 2 GLY A 58 GLY A 67 1 10 SHEET 1 A 2 PHE A 4 THR A 6 0 SHEET 2 A 2 PHE A 53 LEU A 55 -1 O PHE A 53 N THR A 6 SHEET 1 B 4 VAL A 30 LYS A 35 0 SHEET 2 B 4 VAL A 42 LEU A 47 -1 O MET A 44 N ARG A 34 SHEET 3 B 4 PHE A 10 VAL A 13 -1 N PHE A 10 O VAL A 45 SHEET 4 B 4 GLU A 72 PRO A 75 -1 O GLN A 74 N LEU A 11 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