Header list of 1vmp.pdb file
Complete list - 2 20 Bytes
HEADER ANTIVIRAL PROTEIN 25-MAR-99 1VMP
TITLE STRUCTURE OF THE ANTI-HIV CHEMOKINE VMIP-II
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (ANTI-HIV CHEMOKINE MIP VII);
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: VMIP-II;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HUMAN HERPESVIRUS 8;
SOURCE 3 ORGANISM_TAXID: 37296;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_CELL_LINE: BL21;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET32A+;
SOURCE 8 OTHER_DETAILS: SYNTHETIC GENE
KEYWDS VMIP-II, CHEMOKINE, MONOMER, SARCOMA, HERPESVIRUS, HHV-8, KAPOSI'S,
KEYWDS 2 ANTIVIRAL PROTEIN
EXPDTA SOLUTION NMR
AUTHOR A.C.LIWANG,Z.-X.WANG,Y.SUN,S.C.PEIPER,P.J.LIWANG
REVDAT 4 02-MAR-22 1VMP 1 REMARK
REVDAT 3 24-FEB-09 1VMP 1 VERSN
REVDAT 2 01-APR-03 1VMP 1 JRNL
REVDAT 1 24-NOV-99 1VMP 0
JRNL AUTH A.C.LIWANG,Z.X.WANG,Y.SUN,S.C.PEIPER,P.J.LIWANG
JRNL TITL THE SOLUTION STRUCTURE OF THE ANTI-HIV CHEMOKINE VMIP-II.
JRNL REF PROTEIN SCI. V. 8 2270 1999
JRNL REFN ISSN 0961-8368
JRNL PMID 10595530
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES WERE CALCULATED USING THE SIMULATED ANNEALING
REMARK 3 PROTOCOL OF
REMARK 3 NILGES ET AL. (1988) FEBS LETT. 229, 129-136 USING THE PROGRAM
REMARK 3 XPLOR 3.1 (
REMARK 3 BRUNGER) MODIFIED TO INCORPORATE COUPLING CONSTANTS (GARRETT EL
REMARK 3 AL. (1984) J.
REMARK 3 MAGN. RESON. SER. B 104, 99-103) AND A CONFORMATIONAL DATA BASE
REMARK 3 POTENTIAL (
REMARK 3 KUSZEWSKI ET AL. (1996) PROTEIN SCI 5, 1067- 1080 AND (1997) J.
REMARK 3 MAGN. RESON.
REMARK 3 125, 171-177).
REMARK 4
REMARK 4 1VMP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000754.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 5.4
REMARK 210 IONIC STRENGTH : 0.01
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D NOESY; 4D NOESY; 3D TOCSY;
REMARK 210 HNHA; HNHB; HACAHB; HBHACONH;
REMARK 210 CBCACONH; CBCANH; HCCHCOSY;
REMARK 210 HCCHTOCSY; CC(CO)NH
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 MODIFIED
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 30
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : MINIMIZED MEAN STRUCTURE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK:
REMARK 210 MEAN STRUCTURE. THE STRUCTURE WAS DETERMINED USING TRIPLE-
REMARK 210 RESONANCE NMR
REMARK 210 SPECTROSCOPY ON 13C, 15N-LABELED VMIP-II
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 H THR A 34 O GLY A 42 1.54
REMARK 500 O PRO A 24 H LEU A 27 1.57
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 GLN A 25 -57.41 -9.45
REMARK 500 CYS A 38 -151.94 -72.37
REMARK 500 LYS A 48 -9.17 -58.68
REMARK 500 ASP A 60 -70.70 -47.81
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1VMP A 4 74 UNP Q98157 VMI2_HHV8 24 94
SEQRES 1 A 71 LEU GLY ALA SER TRP HIS ARG PRO ASP LYS CYS CYS LEU
SEQRES 2 A 71 GLY TYR GLN LYS ARG PRO LEU PRO GLN VAL LEU LEU SER
SEQRES 3 A 71 SER TRP TYR PRO THR SER GLN LEU CYS SER LYS PRO GLY
SEQRES 4 A 71 VAL ILE PHE LEU THR LYS ARG GLY ARG GLN VAL CYS ALA
SEQRES 5 A 71 ASP LYS SER LYS ASP TRP VAL LYS LYS LEU MET GLN GLN
SEQRES 6 A 71 LEU PRO VAL THR ALA ARG
HELIX 1 1 GLN A 25 LEU A 27 5 3
HELIX 2 2 ASP A 60 GLN A 68 1 9
SHEET 1 A 2 LEU A 28 THR A 34 0
SHEET 2 A 2 GLY A 42 THR A 47 -1 N LEU A 46 O SER A 29
SSBOND 1 CYS A 14 CYS A 38 1555 1555 2.02
SSBOND 2 CYS A 15 CYS A 54 1555 1555 2.02
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
Complete list - 2 20 Bytes