Header list of 1hff.pdb file
Complete list - 25 20 Bytes
HEADER CHEMOKINE 01-DEC-00 1HFF TITLE NMR SOLUTION STRUCTURES OF THE VMIP-II 1-10 PEPTIDE FROM TITLE 2 KAPOSI'S SARCOMA-ASSOCIATED HERPESVIRUS. COMPND MOL_ID: 1; COMPND 2 MOLECULE: VIRAL MACROPHAGE INFLAMMATORY PROTEIN-II; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 1-10; COMPND 5 SYNONYM: VMIP-II, VMIP-1B SOURCE MOL_ID: 1; SOURCE 2 SYNTHETIC: YES; SOURCE 3 ORGANISM_SCIENTIFIC: HUMAN HERPESVIRUS 8; SOURCE 4 ORGANISM_TAXID: 37296 KEYWDS CHEMOKINE, CXCR4, ANATAGONIST, VMIP-II EXPDTA SOLUTION NMR NUMMDL 55 AUTHOR M.P.CRUMP,E.ELISSEEVA,J.H.GONG,I.CLARK-LEWIS,B.D.SYKES REVDAT 4 24-FEB-09 1HFF 1 VERSN REVDAT 3 06-FEB-07 1HFF 1 REVDAT DBREF MODEL REVDAT 2 19-FEB-01 1HFF 1 JRNL REMARK REVDAT 1 07-DEC-00 1HFF 0 JRNL AUTH M.P.CRUMP,E.ELISSEEVA,J.H.GONG,I.CLARK-LEWIS, JRNL AUTH 2 B.D.SYKES JRNL TITL STRUCTURE/FUNCTION OF HUMAN HERPESVIRUS-8 MIP-II JRNL TITL 2 (1-71) AND THE ANTAGONIST N-TERMINAL SEGMENT JRNL TITL 3 (1-10) JRNL REF FEBS LETT. V. 489 171 2001 JRNL REFN ISSN 0014-5793 JRNL PMID 11165244 JRNL DOI 10.1016/S0014-5793(00)02393-0 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : X-PLOR REMARK 3 AUTHORS : BRUNGER REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN REMARK 3 THE JOURNAL CITATION. REMARK 4 REMARK 4 1HFF COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-DEC-00. REMARK 100 THE PDBE ID CODE IS EBI-5613. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 281 REMARK 210 PH : 5.0 REMARK 210 IONIC STRENGTH : 20MM SODIUM ACETATE REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 20MM SODIUM ACETATE, REMARK 210 1-2MM PEPTIDE, 1MM SODIUM REMARK 210 AZIDE, 1MM DSS REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : DQF-COSY, TOCSY, NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 600 REMARK 210 SPECTROMETER MODEL : VARIAN UNITY REMARK 210 SPECTROMETER MANUFACTURER : VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : X-PLOR REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 55 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 55 REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL REMARK 210 REMARK 210 REMARK: SEE PAPER FOR FURTHER EXPERIMENTAL DETAILS. 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: 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 ALA A 3 -166.73 -127.78 REMARK 500 1 ARG A 7 155.14 88.29 REMARK 500 1 PRO A 8 45.83 -83.01 REMARK 500 1 ASP A 9 75.80 53.12 REMARK 500 2 HIS A 6 -67.33 -133.32 REMARK 500 2 ARG A 7 150.36 162.60 REMARK 500 3 ALA A 3 -173.61 60.71 REMARK 500 3 HIS A 6 -64.15 -108.68 REMARK 500 3 ARG A 7 149.88 155.77 REMARK 500 3 ASP A 9 49.20 -151.34 REMARK 500 4 SER A 4 120.89 63.23 REMARK 500 4 ARG A 7 140.91 86.17 REMARK 500 4 PRO A 8 46.80 -84.19 REMARK 500 5 ALA A 3 -165.48 60.71 REMARK 500 5 HIS A 6 -46.43 -135.24 REMARK 500 5 ASP A 9 156.09 61.46 REMARK 500 6 TRP A 5 118.93 61.04 REMARK 500 6 HIS A 6 -61.44 -98.83 REMARK 500 6 ARG A 7 145.80 148.71 REMARK 500 7 SER A 4 136.22 -172.18 REMARK 500 7 HIS A 6 -48.17 -155.20 REMARK 500 7 ASP A 9 97.92 -175.23 REMARK 500 8 ALA A 3 -165.71 61.10 REMARK 500 8 HIS A 6 -47.32 -155.36 REMARK 500 9 ALA A 3 -178.21 -175.86 REMARK 500 9 HIS A 6 -45.41 -170.56 REMARK 500 9 ARG A 7 153.63 171.41 REMARK 500 9 PRO A 8 47.44 -86.07 REMARK 500 9 ASP A 9 81.48 60.10 REMARK 500 10 ASP A 9 64.34 -107.28 REMARK 500 11 HIS A 6 -46.84 -140.41 REMARK 500 11 ASP A 9 -176.50 57.24 REMARK 500 12 ARG A 7 147.39 82.02 REMARK 500 12 ASP A 9 95.65 41.94 REMARK 500 13 ALA A 3 162.28 60.82 REMARK 500 13 HIS A 6 -44.21 -170.10 REMARK 500 13 ARG A 7 158.09 179.77 REMARK 500 13 ASP A 9 68.45 64.31 REMARK 500 14 HIS A 6 -48.93 -132.80 REMARK 500 14 ARG A 7 157.43 172.14 REMARK 500 15 ALA A 3 -177.75 60.64 REMARK 500 15 HIS A 6 -55.69 -135.66 REMARK 500 15 ARG A 7 153.34 167.40 REMARK 500 15 ASP A 9 84.74 -169.42 REMARK 500 16 HIS A 6 -48.98 -140.66 REMARK 500 16 ARG A 7 157.27 178.87 REMARK 500 17 ARG A 7 158.85 176.74 REMARK 500 18 ARG A 7 146.89 91.89 REMARK 500 18 PRO A 8 47.59 -84.64 REMARK 500 19 ALA A 3 -174.52 -61.50 REMARK 500 19 SER A 4 126.21 63.12 REMARK 500 19 HIS A 6 -49.96 -153.14 REMARK 500 19 ARG A 7 153.14 168.74 REMARK 500 20 SER A 4 141.32 -174.23 REMARK 500 20 ARG A 7 143.28 87.26 REMARK 500 20 ASP A 9 103.86 57.71 REMARK 500 21 ALA A 3 -173.63 60.84 REMARK 500 21 ARG A 7 145.62 84.39 REMARK 500 21 PRO A 8 48.43 -85.00 REMARK 500 21 ASP A 9 156.65 61.10 REMARK 500 22 ALA A 3 -177.80 60.41 REMARK 500 22 HIS A 6 -63.24 -164.48 REMARK 500 22 ARG A 7 151.85 171.43 REMARK 500 22 PRO A 8 46.52 -87.02 REMARK 500 22 ASP A 9 88.98 57.32 REMARK 500 23 ALA A 3 160.50 60.24 REMARK 500 23 HIS A 6 -66.94 -123.03 REMARK 500 23 ARG A 7 143.21 149.24 REMARK 500 24 ARG A 7 160.33 173.31 REMARK 500 25 ALA A 3 -164.72 -178.11 REMARK 500 25 HIS A 6 -44.29 -130.76 REMARK 500 26 ALA A 3 47.89 -148.84 REMARK 500 26 SER A 4 96.46 61.07 REMARK 500 26 TRP A 5 137.55 -39.24 REMARK 500 26 HIS A 6 -48.75 -130.96 REMARK 500 26 ARG A 7 154.33 165.16 REMARK 500 26 ASP A 9 80.40 -154.69 REMARK 500 27 ALA A 3 40.06 -104.16 REMARK 500 27 ASP A 9 -170.85 44.57 REMARK 500 28 SER A 4 145.12 179.65 REMARK 500 28 HIS A 6 -48.60 -145.81 REMARK 500 28 ARG A 7 157.39 179.38 REMARK 500 29 ALA A 3 91.68 -178.40 REMARK 500 29 HIS A 6 -56.75 -169.68 REMARK 500 29 ARG A 7 151.37 169.43 REMARK 500 30 ARG A 7 158.44 170.77 REMARK 500 30 ASP A 9 86.19 54.64 REMARK 500 31 ALA A 3 -166.66 -172.64 REMARK 500 31 ARG A 7 155.29 167.37 REMARK 500 32 ALA A 3 83.81 60.95 REMARK 500 32 HIS A 6 -55.13 -143.70 REMARK 500 32 ARG A 7 151.73 165.33 REMARK 500 32 ASP A 9 144.81 -177.70 REMARK 500 33 ALA A 3 178.24 60.81 REMARK 500 33 HIS A 6 -52.51 -142.78 REMARK 500 33 ARG A 7 154.74 169.97 REMARK 500 34 ALA A 3 166.10 60.72 REMARK 500 34 HIS A 6 -49.34 -152.47 REMARK 500 34 ARG A 7 156.42 176.19 REMARK 500 35 HIS A 6 -48.61 -152.28 REMARK 500 35 ARG A 7 159.14 177.22 REMARK 500 35 ASP A 9 -170.53 44.36 REMARK 500 36 ARG A 7 148.17 94.57 REMARK 500 36 PRO A 8 48.86 -83.82 REMARK 500 37 ALA A 3 -175.60 60.50 REMARK 500 37 HIS A 6 -54.46 -143.54 REMARK 500 37 ARG A 7 154.14 171.53 REMARK 500 38 HIS A 6 -42.64 -173.89 REMARK 500 39 HIS A 6 -48.51 -159.90 REMARK 500 39 ARG A 7 157.70 175.16 REMARK 500 40 HIS A 6 -49.41 -146.64 REMARK 500 40 ARG A 7 157.34 176.09 REMARK 500 41 SER A 4 134.00 63.24 REMARK 500 41 ARG A 7 147.30 159.85 REMARK 500 41 ASP A 9 -173.53 177.73 REMARK 500 42 TRP A 5 118.88 61.29 REMARK 500 42 ARG A 7 151.57 158.92 REMARK 500 42 ASP A 9 80.28 59.49 REMARK 500 43 ALA A 3 -179.01 60.84 REMARK 500 43 SER A 4 117.39 62.28 REMARK 500 43 HIS A 6 -50.44 -152.04 REMARK 500 43 ARG A 7 153.97 168.68 REMARK 500 44 HIS A 6 -45.90 -166.37 REMARK 500 44 ARG A 7 153.38 176.33 REMARK 500 44 ASP A 9 161.42 59.48 REMARK 500 45 SER A 4 122.22 62.86 REMARK 500 45 HIS A 6 -51.37 -134.84 REMARK 500 45 ARG A 7 157.45 168.21 REMARK 500 46 ALA A 3 152.52 61.90 REMARK 500 46 ARG A 7 148.30 83.94 REMARK 500 46 ASP A 9 137.30 67.44 REMARK 500 47 ALA A 3 -169.12 61.01 REMARK 500 47 HIS A 6 -50.05 -143.01 REMARK 500 47 ARG A 7 155.82 173.51 REMARK 500 48 ALA A 3 134.88 -177.67 REMARK 500 48 HIS A 6 -49.44 -149.28 REMARK 500 48 ARG A 7 156.63 175.91 REMARK 500 49 ALA A 3 -179.84 -64.77 REMARK 500 49 HIS A 6 -51.01 -154.03 REMARK 500 49 ARG A 7 154.15 165.52 REMARK 500 49 ASP A 9 138.43 64.45 REMARK 500 50 ALA A 3 140.16 -172.09 REMARK 500 50 TRP A 5 117.81 61.42 REMARK 500 50 ARG A 7 153.65 162.43 REMARK 500 51 HIS A 6 -59.74 -143.75 REMARK 500 51 ARG A 7 153.49 172.79 REMARK 500 52 SER A 4 42.60 -97.31 REMARK 500 52 TRP A 5 -173.77 62.94 REMARK 500 52 HIS A 6 -45.11 174.24 REMARK 500 52 ARG A 7 154.40 164.29 REMARK 500 53 TRP A 5 145.21 -177.59 REMARK 500 53 HIS A 6 -51.12 -134.96 REMARK 500 53 ARG A 7 152.91 160.18 REMARK 500 54 ALA A 3 -179.22 60.59 REMARK 500 54 HIS A 6 -43.11 -176.63 REMARK 500 54 ARG A 7 154.26 173.84 REMARK 500 54 ASP A 9 44.81 -102.56 REMARK 500 55 HIS A 6 -64.99 -160.07 REMARK 500 55 ARG A 7 150.89 169.54 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1HFG RELATED DB: PDB REMARK 900 NMR SOLUTION STRUCTURES OF THE VMIP-II 1-71 PEPTIDE FROM REMARK 900 KAPOSI'S SARCOMA-ASSOCIATED HERPESVIRUS. REMARK 900 (RESIDUES 1-71, NMR, MINIMISED AVERAGE STRUCTURE) REMARK 900 RELATED ID: 1CM9 RELATED DB: PDB REMARK 900 CRYSTAL STRUCTURE OF VIRAL MACROPHAGE INFLAMMATORY PROTEIN-II REMARK 900 RELATED ID: 1VMP RELATED DB: PDB REMARK 900 STRUCTURE OF THE ANTI-HIV CHEMOKINE VMIP-II DBREF 1HFF A 1 10 UNP Q98157 VMI2_KSHV 24 33 SEQRES 1 A 10 LEU GLY ALA SER TRP HIS ARG PRO ASP LYS 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 - 25 20 Bytes