Header list of 1a6s.pdb file
Complete list - b 16 2 Bytes
HEADER VIRAL PROTEIN 02-MAR-98 1A6S TITLE M-DOMAIN FROM GAG POLYPROTEIN OF ROUS SARCOMA VIRUS, NMR, 20 TITLE 2 STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: GAG POLYPROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: M-DOMAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ROUS SARCOMA VIRUS - PRAGUE C; SOURCE 3 ORGANISM_TAXID: 11888; SOURCE 4 STRAIN: PRAGUE C; SOURCE 5 CELL_LINE: BL21; SOURCE 6 GENE: GAG; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3); SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PATV-8; SOURCE 11 EXPRESSION_SYSTEM_GENE: GAG KEYWDS CORE PROTEIN, VIRUS STRUCTURE, MEMBRANE BINDING, VIRAL PROTEIN EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR J.M.MCDONNELL,D.FUSHMAN,S.M.CAHILL,W.ZHOU,A.WOLVEN,C.B.WILSON, AUTHOR 2 T.D.NELLE,M.D.RESH,J.WILLS,D.COWBURN REVDAT 4 16-FEB-22 1A6S 1 REMARK REVDAT 3 24-FEB-09 1A6S 1 VERSN REVDAT 2 01-APR-03 1A6S 1 JRNL REVDAT 1 14-OCT-98 1A6S 0 JRNL AUTH J.M.MCDONNELL,D.FUSHMAN,S.M.CAHILL,W.ZHOU,A.WOLVEN, JRNL AUTH 2 C.B.WILSON,T.D.NELLE,M.D.RESH,J.WILLS,D.COWBURN JRNL TITL SOLUTION STRUCTURE AND DYNAMICS OF THE BIOACTIVE RETROVIRAL JRNL TITL 2 M DOMAIN FROM ROUS SARCOMA VIRUS JRNL REF J.MOL.BIOL. V. 279 921 1998 JRNL REFN ISSN 0022-2836 JRNL PMID 9642071 JRNL DOI 10.1006/JMBI.1998.1788 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH T.D.NELLE,J.W.WILLS REMARK 1 TITL A LARGE REGION WITHIN THE ROUS SARCOMA VIRUS MATRIX PROTEIN REMARK 1 TITL 2 IS DISPENSABLE FOR BUDDING AND INFECTIVITY REMARK 1 REF J.VIROL. V. 70 2269 1996 REMARK 1 REFN ISSN 0022-538X REMARK 1 REFERENCE 2 REMARK 1 AUTH A.M.CHRISTENSEN,M.A.MASSIAH,B.G.TURNER,W.I.SUNDQUIST, REMARK 1 AUTH 2 M.F.SUMMERS REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF THE HTLV-II MATRIX PROTEIN REMARK 1 TITL 2 AND COMPARATIVE ANALYSIS OF MATRIX PROTEINS FROM THE REMARK 1 TITL 3 DIFFERENT CLASSES OF PATHOGENIC HUMAN RETROVIRUSES REMARK 1 REF J.MOL.BIOL. V. 264 1117 1996 REMARK 1 REFN ISSN 0022-2836 REMARK 1 REFERENCE 3 REMARK 1 AUTH S.MATTHEWS,M.MIKHAILOV,A.BURNY,P.ROY REMARK 1 TITL THE SOLUTION STRUCTURE OF THE BOVINE LEUKAEMIA VIRUS MATRIX REMARK 1 TITL 2 PROTEIN AND SIMILARITY WITH LENTIVIRAL MATRIX PROTEINS REMARK 1 REF EMBO J. V. 15 3267 1996 REMARK 1 REFN ISSN 0261-4189 REMARK 1 REFERENCE 4 REMARK 1 AUTH Z.RAO,A.S.BELYAEV,E.FRY,P.ROY,I.M.JONES,D.I.STUART REMARK 1 TITL CRYSTAL STRUCTURE OF SIV MATRIX ANTIGEN AND IMPLICATIONS FOR REMARK 1 TITL 2 VIRUS ASSEMBLY REMARK 1 REF NATURE V. 378 743 1995 REMARK 1 REFN ISSN 0028-0836 REMARK 1 REFERENCE 5 REMARK 1 AUTH M.A.MASSIAH,M.R.STARICH,C.PASCHALL,M.F.SUMMERS, REMARK 1 AUTH 2 A.M.CHRISTENSEN,W.I.SUNDQUIST REMARK 1 TITL THREE-DIMENSIONAL STRUCTURE OF THE HUMAN IMMUNODEFICIENCY REMARK 1 TITL 2 VIRUS TYPE 1 MATRIX PROTEIN REMARK 1 REF J.MOL.BIOL. V. 244 198 1994 REMARK 1 REFN ISSN 0022-2836 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA REMARK 3 AUTHORS : GUNTERT,WUTHRICH REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES WERE CALCULATED USING THE REMARK 3 DISTANCE GEOMETRY PROGRAM DYANA. NO FURTHER REFINEMENT WAS REMARK 3 PERFORMED. AN ANALYSIS OF THE QUALITY OF STRUCTURES PRODUCED WAS REMARK 3 CARRIED OUT USING PROCHECK-NMR. REMARK 4 REMARK 4 1A6S COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL. REMARK 100 THE DEPOSITION ID IS D_1000170463. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 6.0 REMARK 210 IONIC STRENGTH : 100 MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : H20 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 1H-15N)HSQC; (1H-13C)HSQC; HSQC REMARK 210 -J; 2D AND 3D 15N-NOESY-HMQC AND REMARK 210 TOCSY-HMQC; 13C-NOESY-HMQC; HCCH- REMARK 210 TOCSY; HNCA; HN(CO)CA; CBCANH; REMARK 210 CBCA(CO)NH; (1H)15N-NOE; H2O- REMARK 210 SELECTIVE 15N-EDITED NOESY AND REMARK 210 ROESY; HYDROGEN-DEUTERIUM REMARK 210 EXCHANGE REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ REMARK 210 SPECTROMETER MODEL : DMX500 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XWINNMR, XEASY, DIANA, DYANA, REMARK 210 THE ECEPP LIBRARY WAS USED USED REMARK 210 METHOD USED : DISTANCE GEOMETRY REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 1000 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: COORDINATES WERE CALCULATED FROM SOLUTION NMR DATA USING REMARK 210 THE PROGRAM DYANA. 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: 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 ALA A 11 HB2 TYR A 15 1.18 REMARK 500 HA VAL A 4 HB3 LEU A 45 1.29 REMARK 500 O LEU A 30 H GLN A 34 1.30 REMARK 500 O ALA A 3 H VAL A 7 1.30 REMARK 500 O SER A 10 H THR A 14 1.35 REMARK 500 O LYS A 6 H SER A 10 1.39 REMARK 500 O VAL A 7 H ALA A 11 1.42 REMARK 500 O TRP A 74 H LEU A 78 1.44 REMARK 500 O SER A 43 H TYR A 46 1.45 REMARK 500 O ALA A 28 H LEU A 32 1.53 REMARK 500 HZ2 LYS A 13 O SER A 20 1.58 REMARK 500 O ALA A 11 H TYR A 15 1.58 REMARK 500 O ALA A 11 CB TYR A 15 1.87 REMARK 500 O SER A 10 N THR A 14 1.92 REMARK 500 O LEU A 30 N GLN A 34 2.11 REMARK 500 O VAL A 7 N ALA A 11 2.12 REMARK 500 O SER A 31 CB LYS A 35 2.14 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 TYR A 15 -76.71 -69.70 REMARK 500 1 LYS A 18 96.91 -27.68 REMARK 500 1 THR A 19 -63.96 165.69 REMARK 500 1 SER A 22 59.76 159.19 REMARK 500 1 LYS A 24 12.14 -143.09 REMARK 500 1 GLU A 25 -89.81 -47.98 REMARK 500 1 LEU A 30 -60.55 -95.01 REMARK 500 1 GLN A 34 3.01 -68.88 REMARK 500 1 SER A 41 177.75 94.10 REMARK 500 1 TYR A 46 -4.50 -56.12 REMARK 500 1 ALA A 57 -71.80 -66.93 REMARK 500 1 ARG A 61 66.18 -164.41 REMARK 500 1 SER A 68 24.26 -155.88 REMARK 500 1 GLU A 70 -65.31 -177.96 REMARK 500 2 GLU A 2 -8.62 -58.94 REMARK 500 2 ILE A 5 -67.05 -92.42 REMARK 500 2 VAL A 7 -70.85 -67.64 REMARK 500 2 TYR A 15 -70.70 -60.61 REMARK 500 2 LYS A 18 -104.12 36.24 REMARK 500 2 SER A 20 95.58 -34.27 REMARK 500 2 SER A 22 -84.67 167.89 REMARK 500 2 LYS A 23 163.40 170.05 REMARK 500 2 LYS A 24 -0.56 77.41 REMARK 500 2 GLU A 25 -92.52 -47.22 REMARK 500 2 LEU A 30 -67.11 -95.23 REMARK 500 2 SER A 41 174.73 99.81 REMARK 500 2 ASP A 44 -36.06 -33.55 REMARK 500 2 ALA A 57 -75.71 -64.67 REMARK 500 2 ARG A 61 62.06 -159.16 REMARK 500 2 LEU A 65 -150.23 -103.33 REMARK 500 2 SER A 68 -19.98 -49.56 REMARK 500 2 GLU A 70 68.21 -172.11 REMARK 500 3 ILE A 5 -66.91 -92.17 REMARK 500 3 VAL A 7 -70.91 -65.99 REMARK 500 3 TYR A 15 -70.82 -69.58 REMARK 500 3 CYS A 16 46.70 -105.21 REMARK 500 3 LYS A 18 -99.00 35.46 REMARK 500 3 THR A 19 -29.58 -39.37 REMARK 500 3 SER A 20 131.28 -35.12 REMARK 500 3 SER A 22 34.30 177.49 REMARK 500 3 GLU A 25 -95.05 -46.58 REMARK 500 3 MET A 40 -26.05 -144.58 REMARK 500 3 SER A 41 162.00 158.08 REMARK 500 3 ALA A 57 -72.36 -65.31 REMARK 500 3 ARG A 61 66.31 -163.12 REMARK 500 3 LEU A 65 -146.36 -104.44 REMARK 500 3 LYS A 67 65.55 -117.84 REMARK 500 3 SER A 68 -95.55 35.92 REMARK 500 3 GLU A 70 64.86 -161.91 REMARK 500 4 TYR A 15 -74.45 -68.70 REMARK 500 REMARK 500 THIS ENTRY HAS 354 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1A6S A 2 87 UNP P03322 GAG_RSVP 2 87 SEQRES 1 A 87 GLY GLU ALA VAL ILE LYS VAL ILE SER SER ALA CYS LYS SEQRES 2 A 87 THR TYR CYS GLY LYS THR SER PRO SER LYS LYS GLU ILE SEQRES 3 A 87 GLY ALA MET LEU SER LEU LEU GLN LYS GLU GLY LEU LEU SEQRES 4 A 87 MET SER PRO SER ASP LEU TYR SER PRO GLY SER TRP ASP SEQRES 5 A 87 PRO ILE THR ALA ALA LEU SER GLN ARG ALA MET ILE LEU SEQRES 6 A 87 GLY LYS SER GLY GLU LEU LYS THR TRP GLY LEU VAL LEU SEQRES 7 A 87 GLY ALA LEU LYS ALA ALA ARG GLU GLU HELIX 1 H-E GLU A 70 GLU A 87 1 18 HELIX 2 H-D TRP A 51 ALA A 62 1 12 HELIX 3 H-B ILE A 26 GLY A 37 1 12 HELIX 4 H-A GLU A 2 CYS A 16 1 15 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 - b 16 2 Bytes