Header list of 1qce.pdb file
Complete list - ov 27 Bytes
HEADER VIRAL PROTEIN 30-APR-99 1QCE TITLE SOLUTION NMR STRUCTURE OF ECTODOMAIN OF SIV GP41, RESTRAINED TITLE 2 REGULARIZED MEAN STRUCTURE PLUS 29 SIMULATED ANNEALING STRUCTURES COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROTEIN (GP41); COMPND 3 CHAIN: A, B, C; COMPND 4 FRAGMENT: ECTODOMAIN, RESIDUES 27 - 149, NUMBERED 1 - 123 SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SIMIAN IMMUNODEFICIENCY VIRUS; SOURCE 3 ORGANISM_TAXID: 11723; SOURCE 4 STRAIN: SOOTEY MANGABEY KEYWDS VIRUS ENVELOPE PROTEIN, SIV GP41 ECTODOMAIN, VIRAL PROTEIN EXPDTA SOLUTION NMR NUMMDL 30 AUTHOR G.M.CLORE REVDAT 3 27-NOV-19 1QCE 1 JRNL REMARK SEQADV REVDAT 2 24-FEB-09 1QCE 1 VERSN REVDAT 1 18-JUL-99 1QCE 0 JRNL AUTH J.KUSZEWSKI,A.M.GRONENBORN,G.M.CLORE JRNL TITL MEASUREMENT OF RESIDUAL DIPOLAR COUPLINGS OF MACROMOLECULES JRNL TITL 2 ALIGNED IN THE NEMATIC PHASE OF ACOLLOIDAL SUSPENSION OF JRNL TITL 3 ROD-SHAPED VIRUSES JRNL REF J.AM.CHEM.SOC. V. 121 2337 1999 JRNL REFN ISSN 0002-7863 JRNL DOI 10.1021/JA9843730 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH M.CAFFREY,M.CAI,J.KAUFMAN,S.J.STAHL,P.T.WINGFIELD, REMARK 1 AUTH 2 D.G.COVELL,A.M.GRONENBORN,G.M.CLORE REMARK 1 TITL THREE-DIMENSIONAL SOLUTION STRUCTURE OF THE 44 KDA REMARK 1 TITL 2 ECTODOMAIN OF SIV GP41. REMARK 1 REF EMBO J. V. 17 4572 1998 REMARK 1 REFN ISSN 0261-4189 REMARK 1 PMID 9707417 REMARK 1 DOI 10.1093/EMBOJ/17.16.4572 REMARK 1 REFERENCE 2 REMARK 1 AUTH M.CAFFREY,M.CAI,J.KAUFMAN,S.J.STAHL,P.T.WINGFIELD, REMARK 1 AUTH 2 A.M.GRONENBORN,G.M.CLORE REMARK 1 TITL DETERMINATION OF THE SECONDARY STRUCTURE AND GLOBAL TOPOLOGY REMARK 1 TITL 2 OF THE 44 KDA ECTODOMAIN OF GP41 OF THE SIMIAN REMARK 1 TITL 3 IMMUNODEFICIENCY VIRUS BY MULTIDIMENSIONAL NUCLEAR MAGNETIC REMARK 1 TITL 4 RESONANCE SPECTROSCOPY. REMARK 1 REF J.MOL.BIOL. V. 271 819 1997 REMARK 1 REFN ISSN 0022-2836 REMARK 1 PMID 9299329 REMARK 1 DOI 10.1006/JMBI.1997.1217 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CNS/XPLOR REMARK 3 AUTHORS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REMARK 3 TERMS IN THE TARGET FUNCTION USED FOR SIMULATED ANNEALING: REMARK 3 NOE (SUM AVERAGING) AND TORSION ANGLE RESTRAINTS REMARK 3 3JHNALPHA COUPLING CONSTANT RESTRAINTS REMARK 3 AND THREE_BOND DEUTERIUMCALPHA(ND) ISOTOPE REMARK 3 RESTRAINTS (GARRETT ET AL REMARK 3 J. MAGN. RESON. B104, 99-103 (1994)). REMARK 3 13CALPHA AND 13CBETA CHEMISCAL SHIFT RESTRAINTS REMARK 3 (KUSZEWSKI ET AL J> MAGN RESON B106, 92-96 (1995)) REMARK 3 TERM FOR THE RADIUS OF GYRATION (KUSZEWSKI J, GRONENB REMARK 3 CLORE, GM J AM CHEM SOC 121, 2337-2338 (1999)) REMARK 3 TORSION ANGLE DATABASE POTENTIAL (KUSZEWSKI J, GRONEN REMARK 3 CLORE GM. PROTEIN SCI 5, 1067-1080 (1996); J. MAGN REMARK 3 125, 171-177 (1997)). REMARK 3 COVALENT GEOMETRY RESTRAINTS (BONDS, ANGLES, IMPROPER REMARK 3 QUARTIC VAN DER WAALS REPULSION TERM (NILGES. M, REMARK 3 GRONENBORN, A.M., BRUNGER, A.T., CLORE, G.M. (1988) REMARK 3 PROTEIN ENG. 2, 27-38). REMARK 4 REMARK 4 1QCE COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAY-99. REMARK 100 THE DEPOSITION ID IS D_1000000994. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 322.00 REMARK 210 PH : 3.00 REMARK 210 IONIC STRENGTH : NULL REMARK 210 PRESSURE : NULL REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : TRIPLE RESONANCE FOR ASSIGNMENT REMARK 210 OF PROTEIN: D-HNCA; D-HNCO; D- REMARK 210 HN(CO) CA; D-HN(CA)CO D-HNCACB; REMARK 210 D-HN(COCA)CB; D-HN(CA) CB; D- REMARK 210 C(CC)(CO)NH; HBHA(CO)NH; HCACO; REMARK 210 HNHA; HCCH-COSY; HCCH- TOCSY; 4D REMARK 210 HCCH 13C-13C NOE; QUANTITATIVE J REMARK 210 CORRELATION FOR COUPLING REMARK 210 CONSTANTS; 3D 15N- SEPARATED NOE REMARK 210 AND ROE; 3D 13C-SEPARATED NOE; REMARK 210 3D 13C-SEPARATED/12C_ FILTERED REMARK 210 NOE; 3D 13C- SEPARATED/15N- REMARK 210 FILTERED NOE; 3D 15N-SEPARATED/ REMARK 210 13C-FILTERED NOE; 4D 15N/15N- REMARK 210 SEPARATED NOE; 4D 15N/13C- REMARK 210 SEPARATED NOE AND 4D 13C/13C- REMARK 210 SEPARATED NOE EXPERIMENTS; 3D REMARK 210 HCA(CO)N FOR THREE-BOND AMIDE REMARK 210 DEUTERIUM ISOTOPE SHIFTS REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : DMX500; DMX600; DMX750 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XPLOR/CNS REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 30 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 OD1 ASN C 56 H VAL C 70 1.41 REMARK 500 OD1 ASN A 56 H VAL A 70 1.41 REMARK 500 OD1 ASN B 56 H VAL B 70 1.41 REMARK 500 O ASN A 37 HG1 THR A 40 1.51 REMARK 500 O ASN C 37 HG1 THR C 40 1.51 REMARK 500 O ASN B 37 HG1 THR B 40 1.51 REMARK 500 HD22 ASN A 37 OD1 ASN B 82 1.52 REMARK 500 OD1 ASN A 82 HD22 ASN C 37 1.52 REMARK 500 HD22 ASN B 37 OD1 ASN C 82 1.52 REMARK 500 O ALA A 107 H GLN A 111 1.53 REMARK 500 O ALA B 107 H GLN B 111 1.53 REMARK 500 O ALA C 107 H GLN C 111 1.53 REMARK 500 O ASN B 82 H TRP B 86 1.55 REMARK 500 O ASN C 82 H TRP C 86 1.55 REMARK 500 O ASN A 82 H TRP A 86 1.55 REMARK 500 O THR A 40 HG1 THR A 43 1.60 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 ASN A 56 -67.80 -133.49 REMARK 500 1 ALA A 60 39.49 -72.01 REMARK 500 1 ALA A 61 115.67 -165.00 REMARK 500 1 VAL A 65 57.50 -105.83 REMARK 500 1 PRO A 73 145.61 -38.04 REMARK 500 1 ASN B 56 -67.78 -133.52 REMARK 500 1 ALA B 60 39.45 -72.02 REMARK 500 1 ALA B 61 115.74 -164.89 REMARK 500 1 VAL B 65 57.48 -105.81 REMARK 500 1 PRO B 73 145.58 -37.98 REMARK 500 1 ASN C 56 -67.81 -133.47 REMARK 500 1 ALA C 60 39.40 -71.97 REMARK 500 1 ALA C 61 115.66 -164.89 REMARK 500 1 VAL C 65 57.46 -105.74 REMARK 500 1 PRO C 73 145.62 -37.96 REMARK 500 2 ASN A 56 -61.95 -133.03 REMARK 500 2 ALA A 60 23.05 -71.74 REMARK 500 2 VAL A 65 60.34 -107.00 REMARK 500 2 TRP A 81 -70.01 -81.91 REMARK 500 2 ASN B 56 -61.95 -132.94 REMARK 500 2 ALA B 60 23.06 -72.03 REMARK 500 2 VAL B 65 59.89 -107.30 REMARK 500 2 ASN C 56 -62.22 -133.03 REMARK 500 2 ALA C 60 22.86 -71.98 REMARK 500 2 VAL C 65 60.11 -107.21 REMARK 500 3 ASN A 56 -69.29 -131.77 REMARK 500 3 ALA A 60 25.50 -78.04 REMARK 500 3 ARG A 63 22.48 -148.28 REMARK 500 3 VAL A 65 59.73 -110.78 REMARK 500 3 PRO A 73 147.80 -37.53 REMARK 500 3 ASN A 74 -58.25 -129.63 REMARK 500 3 ASN A 122 59.07 -119.70 REMARK 500 3 ASN B 56 -69.25 -131.66 REMARK 500 3 ALA B 60 25.26 -77.76 REMARK 500 3 ARG B 63 22.51 -148.42 REMARK 500 3 VAL B 65 59.52 -110.62 REMARK 500 3 PRO B 73 147.97 -37.50 REMARK 500 3 ASN B 74 -57.98 -129.90 REMARK 500 3 ASN B 122 59.12 -119.93 REMARK 500 3 ASN C 56 -69.22 -131.60 REMARK 500 3 ALA C 60 25.28 -77.96 REMARK 500 3 ARG C 63 22.35 -148.32 REMARK 500 3 VAL C 65 59.70 -110.60 REMARK 500 3 PRO C 73 148.02 -37.33 REMARK 500 3 ASN C 74 -58.45 -129.92 REMARK 500 4 ASN A 56 -69.94 -133.94 REMARK 500 4 VAL A 65 57.58 -103.73 REMARK 500 4 PRO A 73 146.02 -39.97 REMARK 500 4 TRP A 81 -70.33 -85.75 REMARK 500 4 ASN A 122 58.00 -119.21 REMARK 500 REMARK 500 THIS ENTRY HAS 436 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 63 0.27 SIDE CHAIN REMARK 500 1 ARG B 63 0.27 SIDE CHAIN REMARK 500 1 ARG C 63 0.27 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 999 REMARK 999 SEQUENCE REMARK 999 1QCE A GB 431487 1 - 551 NOT IN ATOMS LIST REMARK 999 1QCE A GB 431487 675 - 876 NOT IN ATOMS LIST REMARK 999 1QCE B GB 431487 1 - 551 NOT IN ATOMS LIST REMARK 999 1QCE B GB 431487 675 - 876 NOT IN ATOMS LIST REMARK 999 1QCE C GB 431487 1 - 551 NOT IN ATOMS LIST REMARK 999 1QCE C GB 431487 675 - 876 NOT IN ATOMS LIST DBREF 1QCE A 1 123 UNP Q88031 Q88031_SIVCZ 552 674 DBREF 1QCE B 1 123 UNP Q88031 Q88031_SIVCZ 552 674 DBREF 1QCE C 1 123 UNP Q88031 Q88031_SIVCZ 552 674 SEQADV 1QCE ALA A 60 UNP Q88031 CYS 611 CONFLICT SEQADV 1QCE ALA A 66 UNP Q88031 CYS 617 CONFLICT SEQADV 1QCE ALA B 60 UNP Q88031 CYS 611 CONFLICT SEQADV 1QCE ALA B 66 UNP Q88031 CYS 617 CONFLICT SEQADV 1QCE ALA C 60 UNP Q88031 CYS 611 CONFLICT SEQADV 1QCE ALA C 66 UNP Q88031 CYS 617 CONFLICT SEQRES 1 A 123 ALA GLN SER ARG THR LEU LEU ALA GLY ILE VAL GLN GLN SEQRES 2 A 123 GLN GLN GLN LEU LEU ASP VAL VAL LYS ARG GLN GLN GLU SEQRES 3 A 123 LEU LEU ARG LEU THR VAL TRP GLY THR LYS ASN LEU GLN SEQRES 4 A 123 THR ARG VAL THR ALA ILE GLU LYS TYR LEU LYS ASP GLN SEQRES 5 A 123 ALA GLN LEU ASN ALA TRP GLY ALA ALA PHE ARG GLN VAL SEQRES 6 A 123 ALA HIS THR THR VAL PRO TRP PRO ASN ALA SER LEU THR SEQRES 7 A 123 PRO LYS TRP ASN ASN GLU THR TRP GLN GLU TRP GLU ARG SEQRES 8 A 123 LYS VAL ASP PHE LEU GLU GLU ASN ILE THR ALA LEU LEU SEQRES 9 A 123 GLU GLU ALA GLN ILE GLN GLN GLU LYS ASN MET TYR GLU SEQRES 10 A 123 LEU GLN LYS LEU ASN SER SEQRES 1 B 123 ALA GLN SER ARG THR LEU LEU ALA GLY ILE VAL GLN GLN SEQRES 2 B 123 GLN GLN GLN LEU LEU ASP VAL VAL LYS ARG GLN GLN GLU SEQRES 3 B 123 LEU LEU ARG LEU THR VAL TRP GLY THR LYS ASN LEU GLN SEQRES 4 B 123 THR ARG VAL THR ALA ILE GLU LYS TYR LEU LYS ASP GLN SEQRES 5 B 123 ALA GLN LEU ASN ALA TRP GLY ALA ALA PHE ARG GLN VAL SEQRES 6 B 123 ALA HIS THR THR VAL PRO TRP PRO ASN ALA SER LEU THR SEQRES 7 B 123 PRO LYS TRP ASN ASN GLU THR TRP GLN GLU TRP GLU ARG SEQRES 8 B 123 LYS VAL ASP PHE LEU GLU GLU ASN ILE THR ALA LEU LEU SEQRES 9 B 123 GLU GLU ALA GLN ILE GLN GLN GLU LYS ASN MET TYR GLU SEQRES 10 B 123 LEU GLN LYS LEU ASN SER SEQRES 1 C 123 ALA GLN SER ARG THR LEU LEU ALA GLY ILE VAL GLN GLN SEQRES 2 C 123 GLN GLN GLN LEU LEU ASP VAL VAL LYS ARG GLN GLN GLU SEQRES 3 C 123 LEU LEU ARG LEU THR VAL TRP GLY THR LYS ASN LEU GLN SEQRES 4 C 123 THR ARG VAL THR ALA ILE GLU LYS TYR LEU LYS ASP GLN SEQRES 5 C 123 ALA GLN LEU ASN ALA TRP GLY ALA ALA PHE ARG GLN VAL SEQRES 6 C 123 ALA HIS THR THR VAL PRO TRP PRO ASN ALA SER LEU THR SEQRES 7 C 123 PRO LYS TRP ASN ASN GLU THR TRP GLN GLU TRP GLU ARG SEQRES 8 C 123 LYS VAL ASP PHE LEU GLU GLU ASN ILE THR ALA LEU LEU SEQRES 9 C 123 GLU GLU ALA GLN ILE GLN GLN GLU LYS ASN MET TYR GLU SEQRES 10 C 123 LEU GLN LYS LEU ASN SER HELIX 1 1 ARG A 4 GLN A 54 1 51 HELIX 2 2 TRP A 81 LEU A 121 1 41 HELIX 3 3 ARG B 4 GLN B 54 1 51 HELIX 4 4 TRP B 81 LEU B 121 1 41 HELIX 5 5 ARG C 4 GLN C 54 1 51 HELIX 6 6 TRP C 81 LEU C 121 1 41 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 - ov 27 Bytes