Header list of 2abo.pdb file
Complete list - 9 20 Bytes
HEADER VIRAL PROTEIN 15-JUL-05 2ABO TITLE NMR STRUCTURE OF GAMMA HERPESVIRUS 68 A VIRAL BCL-2 HOMOLOG COMPND MOL_ID: 1; COMPND 2 MOLECULE: BCL-2 HOMOLOG; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: TRUNCATED BCL-2 HOMOLOG; COMPND 5 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MURID HERPESVIRUS 4; SOURCE 3 ORGANISM_COMMON: MURINE HERPESVIRUS 68; SOURCE 4 ORGANISM_TAXID: 33708; SOURCE 5 GENE: GAMMA HV68; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET21D(+) KEYWDS VIRAL BCL-2 HOMOLOG, MURINE GAMMA HERPES VIRUS, VIRAL PROTEIN EXPDTA SOLUTION NMR MDLTYP MINIMIZED AVERAGE AUTHOR J.LOH,Q.HUANG,A.M.PETROS,D.NETTESHEIM,L.F.VAN DYK,L.LABRADA, AUTHOR 2 S.H.SPECK,B.LEVINE,E.T.OLEJNICZAK,H.W.VIRGIN REVDAT 3 09-MAR-22 2ABO 1 REMARK REVDAT 2 24-FEB-09 2ABO 1 VERSN REVDAT 1 16-MAY-06 2ABO 0 JRNL AUTH J.LOH,Q.HUANG,A.M.PETROS,D.NETTESHEIM,L.F.VAN DYK,L.LABRADA, JRNL AUTH 2 S.H.SPECK,B.LEVINE,E.T.OLEJNICZAK,H.W.VIRGIN JRNL TITL A SURFACE GROOVE ESSENTIAL FOR VIRAL BCL-2 FUNCTION DURING JRNL TITL 2 CHRONIC INFECTION IN VIVO. JRNL REF PLOS PATHOG. V. 1 E10 2005 JRNL REFN ISSN 1553-7366 JRNL PMID 16201011 JRNL DOI 10.1371/JOURNAL.PPAT.0010010 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 2ABO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUL-05. REMARK 100 THE DEPOSITION ID IS D_1000033716. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 303 REMARK 210 PH : 7.8 REMARK 210 IONIC STRENGTH : 20MM TRIS REMARK 210 PRESSURE : AMBIENT REMARK 210 SAMPLE CONTENTS : .1 MM HV68-VIRAL BCL2 U-15N, REMARK 210 13C, 20MM TRIS; 90% H2O, 10% D2O; REMARK 210 .5 MM HV68-VIRAL BCL2 U-15N, REMARK 210 13C, 75% 2H ; 20MM TRIS; 90% H2O, REMARK 210 10% D2O REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : DRX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : NULL REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 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 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 RES C SSSEQI REMARK 465 MET A 1 REMARK 465 SER A 2 REMARK 465 HIS A 3 REMARK 465 LYS A 4 REMARK 465 LYS A 5 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 O ASN A 126 H LEU A 128 1.01 REMARK 500 O ASN A 126 N LEU A 128 1.88 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 LYS A 23 92.35 42.26 REMARK 500 GLU A 25 26.58 45.19 REMARK 500 GLU A 26 96.34 68.60 REMARK 500 ASP A 28 53.75 -98.43 REMARK 500 CYS A 29 55.75 -147.78 REMARK 500 ALA A 58 -75.98 -39.16 REMARK 500 ASP A 59 49.67 -157.71 REMARK 500 TYR A 60 46.75 -107.90 REMARK 500 ASP A 70 62.47 -150.01 REMARK 500 ASP A 81 -54.62 -151.03 REMARK 500 GLU A 101 -44.30 177.92 REMARK 500 PRO A 105 -169.99 -73.43 REMARK 500 SER A 107 132.23 -174.43 REMARK 500 THR A 109 163.84 -44.86 REMARK 500 ASN A 127 5.08 -20.43 REMARK 500 MET A 129 -33.68 -38.85 REMARK 500 PRO A 133 94.80 -39.05 REMARK 500 LEU A 134 41.53 -143.99 REMARK 500 REMARK 500 REMARK: NULL DBREF 2ABO A 1 136 UNP P89884 P89884_MHV68 1 136 SEQRES 1 A 136 MET SER HIS LYS LYS SER GLY THR TYR TRP ALA THR LEU SEQRES 2 A 136 ILE THR ALA PHE LEU LYS THR VAL SER LYS VAL GLU GLU SEQRES 3 A 136 LEU ASP CYS VAL ASP SER ALA VAL LEU VAL ASP VAL SER SEQRES 4 A 136 LYS ILE ILE THR LEU THR GLN GLU PHE ARG ARG HIS TYR SEQRES 5 A 136 ASP SER VAL TYR ARG ALA ASP TYR GLY PRO ALA LEU LYS SEQRES 6 A 136 ASN TRP LYS ARG ASP LEU SER LYS LEU PHE THR SER LEU SEQRES 7 A 136 PHE VAL ASP VAL ILE ASN SER GLY ARG ILE VAL GLY PHE SEQRES 8 A 136 PHE ASP VAL GLY ARG TYR VAL CYS GLU GLU VAL LEU CYS SEQRES 9 A 136 PRO GLY SER TRP THR GLU ASP HIS GLU LEU LEU ASN ASP SEQRES 10 A 136 CYS MET THR HIS PHE PHE ILE GLU ASN ASN LEU MET ASN SEQRES 11 A 136 HIS PHE PRO LEU GLU ASP HELIX 1 1 THR A 8 SER A 22 1 15 HELIX 2 2 ALA A 33 TYR A 52 1 20 HELIX 3 3 SER A 54 ALA A 58 5 5 HELIX 4 4 PRO A 62 ASN A 66 5 5 HELIX 5 5 LEU A 71 THR A 76 1 6 HELIX 6 6 ASN A 84 GLU A 100 1 17 HELIX 7 7 THR A 109 ASN A 126 1 18 HELIX 8 8 ASN A 127 HIS A 131 5 5 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
Complete list - 9 20 Bytes