Header list of 1hhv.pdb file
Complete list - n 24 2 Bytes
HEADER VIRAL PROTEIN 06-DEC-98 1HHV
TITLE SOLUTION STRUCTURE OF VIRUS CHEMOKINE VMIP-II
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VIRUS CHEMOKINE VMIP-II;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ORF K4; VMIP-II; MACROPHAGE INFLAMMATORY PROTEIN 1-ALPHA
COMPND 5 HOMOLOG;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: SEQUENCE FROM HUMAN HERPESVIRUS 8
KEYWDS VMIP-II, VIRUS CHEMOKINE, KSHV(HUMAN HERPESVIRUS 8), RECEPTOR
KEYWDS 2 BINDING, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR W.SHAO,E.FERNANDEZ,J.M.NAVENOT,J.WILKEN,D.A.THOMPSON,S.PEPIPER,
AUTHOR 2 B.I.SCHWEITZER,E.LOLIS
REVDAT 3 24-JAN-18 1HHV 1 JRNL REMARK
REVDAT 2 24-FEB-09 1HHV 1 VERSN
REVDAT 1 16-SEP-03 1HHV 0
JRNL AUTH W.SHAO,E.FERNANDEZ,A.SACHPATZIDIS,J.WILKEN,D.A.THOMPSON,
JRNL AUTH 2 B.I.SCHWEITZER,E.LOLIS
JRNL TITL CCR2 AND CCR5 RECEPTOR-BINDING PROPERTIES OF HERPESVIRUS-8
JRNL TITL 2 VMIP-II BASED ON SEQUENCE ANALYSIS AND ITS SOLUTION
JRNL TITL 3 STRUCTURE
JRNL REF EUR.J.BIOCHEM. V. 268 2948 2001
JRNL REFN ISSN 0014-2956
JRNL PMID 11358512
JRNL DOI 10.1046/J.1432-1327.2001.02184.X
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH W.SHAO,E.FERNANDEZ,J.WILKEN,D.A.THOMPSON,M.A.SIANI,J.WEST,
REMARK 1 AUTH 2 E.LOLIS,B.I.SCHWEITZER
REMARK 1 TITL ACCESSIBILITY OF SELENOMETHIONINE PROTEINS BY TOTAL CHEMICAL
REMARK 1 TITL 2 SYNTHESIS: STRUCTURAL STUDIES OF HUMAN HERPESVIRUS-8 MIP-II
REMARK 1 REF FEBS LETT. V. 441 77 1998
REMARK 1 REFN ISSN 0014-5793
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1HHV COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-DEC-98.
REMARK 100 THE DEPOSITION ID IS D_1000000228.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 3.25
REMARK 210 IONIC STRENGTH : 50 MM
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NOESY; TOCSY; HSQC; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR 3.851
REMARK 210 METHOD USED : TORSIONAL ANGLE MOLECULAR
REMARK 210 DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 80
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
REMARK 210 CONFORMERS, SELECTION CRITERIA : LEAST RESTRAINT VIOLATION AND
REMARK 210 LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK:
REMARK 210 THE STRUCTURES WERE DETERMINED USING TWO- DIMENSIONAL HOMO- AND
REMARK 210 HETERO-NUCLEAR
REMARK 210 NMR SPECTROSCOPY.
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 MODELS 1-25
REMARK 470 RES CSSEQI ATOMS
REMARK 470 ARG A 74 O
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 H GLN A 19 O CYS A 54 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 ASP A 2 -50.72 -158.87
REMARK 500 1 THR A 3 -147.67 48.57
REMARK 500 1 LEU A 4 -86.88 -98.59
REMARK 500 1 ALA A 6 109.79 -58.03
REMARK 500 1 SER A 7 -33.83 -144.64
REMARK 500 1 TRP A 8 -169.77 -77.10
REMARK 500 1 ARG A 10 82.20 56.68
REMARK 500 1 PRO A 11 -159.56 -74.42
REMARK 500 1 ASP A 12 -98.10 -163.75
REMARK 500 1 CYS A 14 -33.60 -158.31
REMARK 500 1 CYS A 15 -176.79 -171.57
REMARK 500 1 TYR A 18 126.65 178.64
REMARK 500 1 SER A 29 -73.95 -96.10
REMARK 500 1 TYR A 32 134.64 -170.35
REMARK 500 1 LYS A 40 96.20 -169.12
REMARK 500 1 THR A 47 -156.72 -61.52
REMARK 500 1 ARG A 49 -82.17 -122.36
REMARK 500 1 VAL A 71 80.89 -69.71
REMARK 500 1 THR A 72 160.90 -38.10
REMARK 500 1 ALA A 73 174.47 176.30
REMARK 500 2 ASP A 2 -79.32 -57.18
REMARK 500 2 THR A 3 175.32 51.06
REMARK 500 2 SER A 7 -86.21 -69.39
REMARK 500 2 CYS A 14 -159.50 -160.84
REMARK 500 2 CYS A 15 177.17 -44.55
REMARK 500 2 LEU A 16 21.84 -76.95
REMARK 500 2 SER A 29 -69.31 -96.07
REMARK 500 2 SER A 35 -139.17 -86.04
REMARK 500 2 GLN A 36 23.63 -143.52
REMARK 500 2 CYS A 38 -166.89 -57.70
REMARK 500 2 THR A 47 -150.57 -63.77
REMARK 500 2 ARG A 49 -77.82 -124.52
REMARK 500 2 VAL A 71 79.39 -59.96
REMARK 500 2 THR A 72 135.73 -38.57
REMARK 500 3 ASP A 2 72.11 54.89
REMARK 500 3 THR A 3 103.13 -165.46
REMARK 500 3 LEU A 4 -30.79 -177.37
REMARK 500 3 ALA A 6 99.36 51.83
REMARK 500 3 SER A 7 31.35 -95.54
REMARK 500 3 LYS A 13 -154.30 -57.98
REMARK 500 3 CYS A 14 -76.19 -84.06
REMARK 500 3 TYR A 18 126.90 178.85
REMARK 500 3 SER A 29 -73.47 -96.83
REMARK 500 3 LYS A 40 89.88 -177.37
REMARK 500 3 PRO A 41 -167.80 -70.83
REMARK 500 3 THR A 47 -155.21 -60.01
REMARK 500 3 ARG A 49 -76.61 -121.34
REMARK 500 3 VAL A 71 76.79 -60.80
REMARK 500 3 THR A 72 164.54 -40.93
REMARK 500 4 ASP A 2 -128.84 -126.28
REMARK 500
REMARK 500 THIS ENTRY HAS 377 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 21 0.32 SIDE CHAIN
REMARK 500 1 ARG A 49 0.09 SIDE CHAIN
REMARK 500 1 ARG A 51 0.25 SIDE CHAIN
REMARK 500 1 ARG A 74 0.30 SIDE CHAIN
REMARK 500 2 ARG A 10 0.32 SIDE CHAIN
REMARK 500 2 ARG A 21 0.32 SIDE CHAIN
REMARK 500 2 ARG A 49 0.20 SIDE CHAIN
REMARK 500 2 ARG A 74 0.29 SIDE CHAIN
REMARK 500 3 ARG A 10 0.23 SIDE CHAIN
REMARK 500 3 ARG A 49 0.13 SIDE CHAIN
REMARK 500 3 ARG A 51 0.17 SIDE CHAIN
REMARK 500 3 ARG A 74 0.14 SIDE CHAIN
REMARK 500 4 ARG A 10 0.31 SIDE CHAIN
REMARK 500 4 ARG A 21 0.32 SIDE CHAIN
REMARK 500 4 ARG A 49 0.30 SIDE CHAIN
REMARK 500 4 ARG A 51 0.31 SIDE CHAIN
REMARK 500 4 ARG A 74 0.32 SIDE CHAIN
REMARK 500 5 ARG A 10 0.30 SIDE CHAIN
REMARK 500 5 ARG A 21 0.16 SIDE CHAIN
REMARK 500 5 ARG A 49 0.18 SIDE CHAIN
REMARK 500 5 ARG A 51 0.28 SIDE CHAIN
REMARK 500 5 ARG A 74 0.31 SIDE CHAIN
REMARK 500 6 ARG A 10 0.29 SIDE CHAIN
REMARK 500 6 ARG A 21 0.25 SIDE CHAIN
REMARK 500 6 ARG A 49 0.26 SIDE CHAIN
REMARK 500 6 ARG A 51 0.31 SIDE CHAIN
REMARK 500 6 ARG A 74 0.29 SIDE CHAIN
REMARK 500 7 ARG A 10 0.19 SIDE CHAIN
REMARK 500 7 ARG A 21 0.15 SIDE CHAIN
REMARK 500 7 ARG A 49 0.21 SIDE CHAIN
REMARK 500 7 ARG A 51 0.22 SIDE CHAIN
REMARK 500 7 ARG A 74 0.32 SIDE CHAIN
REMARK 500 8 ARG A 10 0.32 SIDE CHAIN
REMARK 500 8 ARG A 21 0.10 SIDE CHAIN
REMARK 500 8 ARG A 49 0.28 SIDE CHAIN
REMARK 500 8 ARG A 51 0.31 SIDE CHAIN
REMARK 500 8 ARG A 74 0.32 SIDE CHAIN
REMARK 500 9 ARG A 10 0.30 SIDE CHAIN
REMARK 500 9 ARG A 21 0.32 SIDE CHAIN
REMARK 500 9 ARG A 49 0.31 SIDE CHAIN
REMARK 500 9 ARG A 51 0.13 SIDE CHAIN
REMARK 500 9 ARG A 74 0.21 SIDE CHAIN
REMARK 500 10 ARG A 10 0.14 SIDE CHAIN
REMARK 500 10 ARG A 21 0.30 SIDE CHAIN
REMARK 500 10 ARG A 49 0.19 SIDE CHAIN
REMARK 500 10 ARG A 51 0.30 SIDE CHAIN
REMARK 500 10 ARG A 74 0.19 SIDE CHAIN
REMARK 500 11 ARG A 10 0.21 SIDE CHAIN
REMARK 500 11 ARG A 21 0.11 SIDE CHAIN
REMARK 500 11 ARG A 49 0.09 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 117 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1HHV A 1 74 UNP Q98157 VMI2_HHV8 21 94
SEQRES 1 A 74 GLY ASP THR LEU GLY ALA SER TRP HIS ARG PRO ASP LYS
SEQRES 2 A 74 CYS CYS LEU GLY TYR GLN LYS ARG PRO LEU PRO GLN VAL
SEQRES 3 A 74 LEU LEU SER SER TRP TYR PRO THR SER GLN LEU CYS SER
SEQRES 4 A 74 LYS PRO GLY VAL ILE PHE LEU THR LYS ARG GLY ARG GLN
SEQRES 5 A 74 VAL CYS ALA ASP LYS SER LYS ASP TRP VAL LYS LYS LEU
SEQRES 6 A 74 MSE GLN GLN LEU PRO VAL THR ALA ARG
MODRES 1HHV MSE A 66 MET SELENOMETHIONINE
HET MSE A 66 17
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE C5 H11 N O2 SE
HELIX 1 1 ASP A 60 GLN A 68 1 9
SHEET 1 A 3 SER A 30 PRO A 33 0
SHEET 2 A 3 VAL A 43 LEU A 46 0
SHEET 3 A 3 GLN A 52 ALA A 55 -1 N ALA A 55 O VAL A 43
SSBOND 1 CYS A 14 CYS A 38 1555 1555 2.02
SSBOND 2 CYS A 15 CYS A 54 1555 1555 2.02
LINK C LEU A 65 N MSE A 66 1555 1555 1.30
LINK C MSE A 66 N GLN A 67 1555 1555 1.31
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 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 - n 24 2 Bytes