Header list of 1uph.pdb file
Complete list - r 25 2 Bytes
HEADER VIRUS/VIRAL PROTEIN 01-OCT-03 1UPH TITLE HIV-1 MYRISTOYLATED MATRIX COMPND MOL_ID: 1; COMPND 2 MOLECULE: GAG POLYPROTEIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 1-131; COMPND 5 SYNONYM: MA, P17; COMPND 6 ENGINEERED: YES; COMPND 7 OTHER_DETAILS: MYRISTYL GROUP COVALENTLY ATTACHED TO THE COMPND 8 N-TERMINAL GLYCINE BY A PEPTIDE BOND SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 SOURCE 3 (CLONE 12); SOURCE 4 ORGANISM_COMMON: HIV-1; SOURCE 5 ORGANISM_TAXID: 11679; SOURCE 6 STRAIN: PNL4-3, SUBCLONE 4.20; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 10 EXPRESSION_SYSTEM_VARIANT: RIL CODON PLUS; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET19B/PET11A KEYWDS VIRUS/VIRAL PROTEIN, MYRISTYL, MYRISTOYLATED, KEYWDS 2 POST-TRANSLATIONAL MODIFICATION, MYRISTYL SWITCH, KEYWDS 3 POLYPROTEIN, PHOSPHORYLATION EXPDTA SOLUTION NMR NUMMDL 20 AUTHOR C.TANG,E.LOELIGER,P.LUNCSFORD,I.KINDE,D.BECKETT,M.F.SUMMERS REVDAT 2 24-FEB-09 1UPH 1 VERSN REVDAT 1 08-JAN-04 1UPH 0 JRNL AUTH C.TANG,E.LOELIGER,P.LUNCSFORD,I.KINDE,D.BECKETT, JRNL AUTH 2 M.F.SUMMERS JRNL TITL ENTROPIC SWITCH REGULATES MYRISTATE EXPOSURE IN JRNL TITL 2 THE HIV-1 MATRIX PROTEIN JRNL REF PROC.NATL.ACAD.SCI.USA V. 101 517 2004 JRNL REFN ISSN 0027-8424 JRNL PMID 14699046 JRNL DOI 10.1073/PNAS.0305665101 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : CYANA REMARK 3 AUTHORS : GUNTERT REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: SIMULATED ANNEALING WITH TORSION REMARK 3 ANGLE DYNAMICS FOLLOWED BY ENERGY MINIMIZATION REMARK 4 REMARK 4 1UPH COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-OCT-03. REMARK 100 THE PDBE ID CODE IS EBI-13611. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308 REMARK 210 PH : 5.5 REMARK 210 IONIC STRENGTH : 100MM NACL REMARK 210 PRESSURE : 1ATM REMARK 210 SAMPLE CONTENTS : NULL REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600; 800 REMARK 210 SPECTROMETER MODEL : DMX600; AVANCE800 REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CYANA REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 100 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20 REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST TARGET FUNCTION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING 2D HOMONUCLEAR REMARK 210 NOESY, 3D 13C-EDITED NOESY AND 4D 13C, 13C-EDITED NOESY REMARK 210 ON UNLABELED OR FULLY LABELED MATRIX 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 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT 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 LYS A 114 - HE21 GLN A 117 1.52 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 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 ARG A 4 51.94 -119.42 REMARK 500 1 ALA A 5 -176.20 48.85 REMARK 500 1 GLU A 17 32.74 -90.06 REMARK 500 1 ALA A 45 38.73 83.39 REMARK 500 1 ARG A 91 54.45 73.77 REMARK 500 1 LYS A 95 -47.17 -137.65 REMARK 500 1 SER A 129 135.91 -174.46 REMARK 500 1 GLN A 130 167.20 179.39 REMARK 500 1 ASN A 131 133.19 -177.51 REMARK 500 2 ALA A 3 -59.72 -122.16 REMARK 500 2 ALA A 5 -175.97 48.87 REMARK 500 2 SER A 6 56.44 -153.60 REMARK 500 2 VAL A 7 -81.81 -126.20 REMARK 500 2 LYS A 26 -60.21 161.09 REMARK 500 2 ARG A 91 61.80 64.19 REMARK 500 2 LYS A 95 -47.25 -146.27 REMARK 500 2 ASN A 124 165.90 174.46 REMARK 500 2 SER A 126 142.92 177.75 REMARK 500 2 GLN A 127 113.62 -165.49 REMARK 500 2 SER A 129 -58.55 -177.07 REMARK 500 2 ASN A 131 92.53 174.68 REMARK 500 3 SER A 6 -32.86 170.65 REMARK 500 3 LYS A 26 50.54 -143.23 REMARK 500 3 ALA A 45 38.52 83.54 REMARK 500 3 ASP A 93 106.86 -40.45 REMARK 500 3 LYS A 95 -40.22 -174.06 REMARK 500 3 SER A 129 -58.60 -165.78 REMARK 500 3 GLN A 130 91.55 43.46 REMARK 500 4 ARG A 4 101.59 169.82 REMARK 500 4 ALA A 45 42.28 76.99 REMARK 500 4 ARG A 91 65.81 76.76 REMARK 500 4 ASN A 124 159.84 174.58 REMARK 500 4 SER A 126 -58.46 -155.80 REMARK 500 4 GLN A 127 95.29 50.58 REMARK 500 4 SER A 129 143.72 67.01 REMARK 500 4 GLN A 130 74.03 -177.38 REMARK 500 4 ASN A 131 167.89 55.77 REMARK 500 5 ALA A 3 173.97 58.66 REMARK 500 5 ALA A 5 -176.64 -60.73 REMARK 500 5 SER A 6 50.59 -157.84 REMARK 500 5 VAL A 7 -68.03 -126.41 REMARK 500 5 GLU A 17 31.24 -90.72 REMARK 500 5 LYS A 26 -60.36 161.16 REMARK 500 5 LYS A 27 -176.49 -171.28 REMARK 500 5 TYR A 29 178.93 -59.41 REMARK 500 5 LYS A 30 175.76 177.35 REMARK 500 5 LYS A 95 -47.24 -146.39 REMARK 500 5 ASP A 121 71.15 -159.21 REMARK 500 5 ASN A 124 149.02 179.29 REMARK 500 5 VAL A 128 -50.20 -173.37 REMARK 500 5 GLN A 130 106.97 -172.88 REMARK 500 6 VAL A 7 -78.21 -125.89 REMARK 500 6 GLU A 17 30.58 -90.81 REMARK 500 6 LYS A 26 -60.52 161.73 REMARK 500 6 LYS A 30 -179.46 -175.63 REMARK 500 6 LYS A 95 -46.07 -130.51 REMARK 500 6 ASN A 124 -51.69 -147.81 REMARK 500 6 ASN A 125 165.31 174.85 REMARK 500 6 SER A 126 88.99 -159.74 REMARK 500 7 ARG A 4 151.91 63.10 REMARK 500 7 VAL A 7 -74.99 -94.23 REMARK 500 7 LYS A 26 -60.04 160.75 REMARK 500 7 ASP A 93 101.72 -52.62 REMARK 500 7 LYS A 95 23.24 -152.37 REMARK 500 7 GLN A 130 119.96 -175.53 REMARK 500 8 ARG A 4 101.50 -161.21 REMARK 500 8 SER A 6 53.22 -153.63 REMARK 500 8 VAL A 7 -79.32 -150.38 REMARK 500 8 GLU A 17 33.66 -90.14 REMARK 500 8 ALA A 45 41.02 81.64 REMARK 500 8 ARG A 91 52.58 78.90 REMARK 500 8 LYS A 95 -61.64 -146.03 REMARK 500 9 SER A 6 59.79 -147.81 REMARK 500 9 VAL A 7 -75.08 -134.41 REMARK 500 9 GLU A 17 31.05 -90.76 REMARK 500 9 LYS A 26 -60.17 161.04 REMARK 500 9 LYS A 95 -47.04 -137.29 REMARK 500 9 ASP A 121 -66.49 -97.66 REMARK 500 9 ASN A 131 148.46 63.63 REMARK 500 10 ALA A 3 -58.89 -125.91 REMARK 500 10 SER A 6 26.67 -147.05 REMARK 500 10 VAL A 7 -69.48 -104.57 REMARK 500 10 GLU A 17 31.00 -90.10 REMARK 500 10 LYS A 26 -60.50 161.45 REMARK 500 10 TYR A 29 177.95 -51.03 REMARK 500 10 ALA A 45 18.74 81.73 REMARK 500 10 LYS A 95 -43.90 -163.55 REMARK 500 10 ASN A 124 167.38 175.36 REMARK 500 10 GLN A 130 117.03 -169.33 REMARK 500 11 ALA A 3 154.66 62.09 REMARK 500 11 ARG A 4 94.97 57.41 REMARK 500 11 VAL A 7 -73.10 -121.31 REMARK 500 11 GLU A 17 40.48 -87.22 REMARK 500 11 ARG A 91 51.68 81.12 REMARK 500 11 LYS A 95 -47.25 -143.52 REMARK 500 11 ASN A 125 133.69 174.56 REMARK 500 11 ASN A 131 94.86 63.54 REMARK 500 12 ALA A 3 -63.17 -164.53 REMARK 500 12 ARG A 4 51.94 -111.29 REMARK 500 12 ALA A 5 -176.14 48.88 REMARK 500 12 SER A 6 60.22 -167.64 REMARK 500 12 VAL A 7 -51.09 -136.37 REMARK 500 12 GLU A 17 36.13 -89.95 REMARK 500 12 LYS A 26 -60.31 161.31 REMARK 500 12 ALA A 45 44.64 83.02 REMARK 500 12 ARG A 91 61.92 72.96 REMARK 500 12 LYS A 95 -45.71 -157.10 REMARK 500 12 ASP A 121 41.30 171.85 REMARK 500 12 ASN A 125 152.60 176.35 REMARK 500 12 SER A 129 112.63 66.77 REMARK 500 13 VAL A 7 -80.06 -147.42 REMARK 500 13 ARG A 91 63.93 62.71 REMARK 500 13 LYS A 95 -47.61 -142.79 REMARK 500 13 GLN A 130 96.97 50.06 REMARK 500 14 ARG A 4 159.96 57.41 REMARK 500 14 GLU A 17 31.87 -90.42 REMARK 500 14 ALA A 45 32.24 83.33 REMARK 500 14 ARG A 91 52.03 76.36 REMARK 500 14 LYS A 95 -46.62 -148.36 REMARK 500 14 ASN A 125 -55.44 -152.04 REMARK 500 14 SER A 126 96.72 53.36 REMARK 500 14 GLN A 127 126.21 -175.36 REMARK 500 15 ALA A 3 -70.77 -109.00 REMARK 500 15 SER A 6 64.86 -156.07 REMARK 500 15 VAL A 7 -81.20 -141.35 REMARK 500 15 GLU A 17 34.51 -88.76 REMARK 500 15 ALA A 45 45.38 70.68 REMARK 500 15 ARG A 91 51.10 82.73 REMARK 500 15 LYS A 95 -46.95 -149.50 REMARK 500 15 ALA A 120 -60.62 -90.52 REMARK 500 15 GLN A 127 99.86 55.84 REMARK 500 15 SER A 129 167.16 179.23 REMARK 500 16 ALA A 3 170.32 60.40 REMARK 500 16 ALA A 5 -175.99 48.76 REMARK 500 16 SER A 6 60.59 -176.66 REMARK 500 16 GLU A 17 30.58 -89.36 REMARK 500 16 GLN A 69 -72.86 -33.77 REMARK 500 16 LYS A 95 -53.59 -145.36 REMARK 500 16 ASN A 131 148.84 -177.64 REMARK 500 17 ALA A 3 86.62 40.47 REMARK 500 17 ARG A 4 145.42 161.41 REMARK 500 17 ALA A 5 -171.68 46.90 REMARK 500 17 SER A 6 33.64 77.38 REMARK 500 17 LYS A 26 -60.16 160.88 REMARK 500 17 LYS A 30 -179.17 179.15 REMARK 500 17 ALA A 45 31.45 80.95 REMARK 500 17 ARG A 91 51.89 71.95 REMARK 500 17 LYS A 95 -47.32 -142.35 REMARK 500 17 ASP A 121 72.60 -164.41 REMARK 500 17 GLN A 127 120.35 179.18 REMARK 500 17 SER A 129 127.15 62.88 REMARK 500 18 ALA A 3 -84.89 -67.21 REMARK 500 18 VAL A 7 -56.75 -142.75 REMARK 500 18 GLU A 17 32.45 -89.83 REMARK 500 18 LYS A 26 -60.08 160.90 REMARK 500 18 ARG A 91 52.63 80.17 REMARK 500 18 LYS A 95 -46.88 -146.04 REMARK 500 18 SER A 126 168.69 62.63 REMARK 500 18 GLN A 127 -59.18 -141.19 REMARK 500 18 VAL A 128 102.75 60.98 REMARK 500 18 GLN A 130 144.32 -177.50 REMARK 500 19 ALA A 3 -40.43 -174.35 REMARK 500 19 SER A 6 -32.60 171.15 REMARK 500 19 GLU A 17 36.60 -86.58 REMARK 500 19 LYS A 26 -59.77 160.31 REMARK 500 19 ARG A 91 63.57 76.69 REMARK 500 19 LYS A 95 -46.25 -154.63 REMARK 500 19 SER A 126 146.41 -175.09 REMARK 500 19 GLN A 127 72.92 -178.24 REMARK 500 20 ALA A 5 -175.92 48.78 REMARK 500 20 SER A 6 49.44 -147.28 REMARK 500 20 VAL A 7 -79.06 -140.77 REMARK 500 20 LYS A 30 174.07 174.63 REMARK 500 20 ALA A 45 43.37 80.34 REMARK 500 20 ARG A 91 62.57 74.17 REMARK 500 20 ASN A 124 167.80 177.35 REMARK 500 20 ASN A 125 159.29 62.77 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1A43 RELATED DB: PDB REMARK 900 STRUCTURE OF THE HIV-1 CAPSID PROTEIN REMARK 900 DIMERIZATION DOMAINAT 2.6A RESOLUTION REMARK 900 RELATED ID: 1A8O RELATED DB: PDB REMARK 900 HIV CAPSID C-TERMINAL DOMAIN REMARK 900 RELATED ID: 1AFV RELATED DB: PDB REMARK 900 HIV-1 CAPSID PROTEIN (P24) COMPLEX WITH REMARK 900 FAB25.3 REMARK 900 RELATED ID: 1AK4 RELATED DB: PDB REMARK 900 HUMAN CYCLOPHILIN A BOUND TO THE AMINO- REMARK 900 TERMINAL DOMAIN OF HIV-1 CAPSID REMARK 900 RELATED ID: 1AUM RELATED DB: PDB REMARK 900 HIV CAPSID C-TERMINAL DOMAIN (CAC146) REMARK 900 RELATED ID: 1BAJ RELATED DB: PDB REMARK 900 HIV-1 CAPSID PROTEIN C-TERMINAL FRAGMENT REMARK 900 PLUS GAG P2 DOMAIN REMARK 900 RELATED ID: 1GDS RELATED DB: PDB REMARK 900 HIV-1 CAPSID PROTEIN, AMINO-TERMINAL CORE REMARK 900 DOMAIN RESIDUES1 - 151, NMR: MODELS 1 - 17 REMARK 900 OF A 50 MODEL SET REMARK 900 RELATED ID: 1GDY RELATED DB: PDB REMARK 900 HIV-1 CAPSID PROTEIN, AMINO-TERMINAL CORE REMARK 900 DOMAIN RESIDUES1 - 151, NMR: MODELS 18 - 34 REMARK 900 OF A 50 MODEL SET REMARK 900 RELATED ID: 1GDZ RELATED DB: PDB REMARK 900 HIV-1 CAPSID PROTEIN, AMINO-TERMINAL CORE REMARK 900 DOMAIN RESIDUES1 - 151, NMR: MODELS 35 - 50 REMARK 900 OF A 50 MODEL SET REMARK 900 RELATED ID: 1GWP RELATED DB: PDB REMARK 900 STRUCTURE OF THE N-TERMINAL DOMAIN OF THE REMARK 900 MATURE HIV-1 CAPSID PROTEIN REMARK 900 RELATED ID: 1HIW RELATED DB: PDB REMARK 900 TRIMERIC HIV-1 MATRIX PROTEIN REMARK 900 RELATED ID: 1L6N RELATED DB: PDB REMARK 900 STRUCTURE OF THE N-TERMINAL 283-RESIDUE REMARK 900 FRAGMENT OF THE HIV-1 GAG POLYPROTEIN REMARK 900 RELATED ID: 2HMX RELATED DB: PDB REMARK 900 HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 MATRIX REMARK 900 PROTEIN 2HMX 3 REMARK 999 REMARK 999 SEQUENCE REMARK 999 RESIDUE 1-132 OF GAG, MET 1 REMOVED BY AMIONPEPTIDASE DBREF 1UPH A 1 1 PDB 1UPH 1UPH 1 1 DBREF 1UPH A 2 132 UNP P12493 GAG_HV1N5 1 131 SEQRES 1 A 132 MYR GLY ALA ARG ALA SER VAL LEU SER GLY GLY GLU LEU SEQRES 2 A 132 ASP LYS TRP GLU LYS ILE ARG LEU ARG PRO GLY GLY LYS SEQRES 3 A 132 LYS GLN TYR LYS LEU LYS HIS ILE VAL TRP ALA SER ARG SEQRES 4 A 132 GLU LEU GLU ARG PHE ALA VAL ASN PRO GLY LEU LEU GLU SEQRES 5 A 132 THR SER GLU GLY CYS ARG GLN ILE LEU GLY GLN LEU GLN SEQRES 6 A 132 PRO SER LEU GLN THR GLY SER GLU GLU LEU ARG SER LEU SEQRES 7 A 132 TYR ASN THR ILE ALA VAL LEU TYR CYS VAL HIS GLN ARG SEQRES 8 A 132 ILE ASP VAL LYS ASP THR LYS GLU ALA LEU ASP LYS ILE SEQRES 9 A 132 GLU GLU GLU GLN ASN LYS SER LYS LYS LYS ALA GLN GLN SEQRES 10 A 132 ALA ALA ALA ASP THR GLY ASN ASN SER GLN VAL SER GLN SEQRES 11 A 132 ASN TYR HET MYR A 1 42 HETNAM MYR MYRISTIC ACID FORMUL 2 MYR C14 H28 O2 HELIX 1 1 SER A 9 GLU A 17 1 9 HELIX 2 2 LYS A 30 ALA A 45 1 16 HELIX 3 3 PRO A 48 GLU A 52 5 5 HELIX 4 4 THR A 53 THR A 70 1 18 HELIX 5 5 SER A 72 ARG A 91 1 20 HELIX 6 6 ASP A 96 THR A 122 1 27 LINK C1 MYR A 1 N GLY A 2 1555 1555 1.33 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 25 2 Bytes