Header list of 2bbx.pdb file
Complete list - r 9 2 Bytes
HEADER CELL ADHESION 18-OCT-05 2BBX
TITLE NMR SOLUTION STRUCTURE OF THE TSR DOMAIN OF MALARIA TRAP PROTEIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THROMBOSPONDIN-RELATED ANONYMOUS PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: TSP DOMAIN TYPE 1;
COMPND 5 SYNONYM: TRAP;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM;
SOURCE 3 ORGANISM_COMMON: MALARIA PARASITE P. FALCIPARUM;
SOURCE 4 ORGANISM_TAXID: 5833;
SOURCE 5 GENE: TRAP;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL-21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-2T
KEYWDS ELONGATED THREE-STRANDED STRUCTURE, CELL ADHESION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR H.TOSSAVAINEN,P.PERMI,I.KILPELAINEN
REVDAT 3 09-MAR-22 2BBX 1 REMARK SEQADV
REVDAT 2 24-FEB-09 2BBX 1 VERSN
REVDAT 1 08-AUG-06 2BBX 0
JRNL AUTH H.TOSSAVAINEN,T.PIHLAJAMAA,T.K.HUTTUNEN,E.RAULO,H.RAUVALA,
JRNL AUTH 2 P.PERMI,I.KILPELAINEN
JRNL TITL THE LAYERED FOLD OF THE TSR DOMAIN OF P. FALCIPARUM TRAP
JRNL TITL 2 CONTAINS A HEPARIN BINDING SITE.
JRNL REF PROTEIN SCI. V. 15 1760 2006
JRNL REFN ISSN 0961-8368
JRNL PMID 16815922
JRNL DOI 10.1110/PS.052068506
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : VNMR 6.1C, AMBER 8.0
REMARK 3 AUTHORS : VARIAN INC. (VNMR), CASE DA ET AL. (AMBER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 754 NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS
REMARK 4
REMARK 4 2BBX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-OCT-05.
REMARK 100 THE DEPOSITION ID IS D_1000034918.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 283
REMARK 210 PH : 6.6
REMARK 210 IONIC STRENGTH : NA
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.5 MM TRAP-TSR U-15N,13C; 20 MM
REMARK 210 BIS-TRIS BUFFER
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : SPARKY 3.106, CYANA 1.0
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 300
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 3D
REMARK 210 HETERONUCLEAR TECHNIQUES.
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: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 7 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 8 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 9 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 10 ARG A 27 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 14 CYS A 18 CA - CB - SG ANGL. DEV. = 7.4 DEGREES
REMARK 500 19 ARG A 23 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
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 9 -166.37 -100.60
REMARK 500 1 CYS A 18 -20.89 -140.44
REMARK 500 1 LYS A 20 30.81 -92.98
REMARK 500 2 CYS A 5 20.62 -145.18
REMARK 500 2 ASP A 9 -167.86 -100.87
REMARK 500 3 THR A 17 25.83 48.78
REMARK 500 3 CYS A 18 -8.81 -147.69
REMARK 500 3 GLU A 45 -32.54 -132.31
REMARK 500 4 CYS A 18 -2.07 -140.39
REMARK 500 4 GLU A 43 79.83 -152.44
REMARK 500 5 CYS A 5 19.66 -141.80
REMARK 500 6 CYS A 18 -6.55 -141.14
REMARK 500 7 ARG A 46 82.94 54.22
REMARK 500 8 CYS A 5 18.30 -142.37
REMARK 500 9 SER A 2 11.95 -142.03
REMARK 500 9 CYS A 5 18.88 -140.52
REMARK 500 9 ASP A 9 -166.88 -104.61
REMARK 500 9 THR A 17 35.56 -143.64
REMARK 500 9 CYS A 18 -20.17 -149.83
REMARK 500 10 ALA A 3 30.40 -143.78
REMARK 500 10 ASP A 9 -166.58 -104.58
REMARK 500 10 THR A 17 39.56 38.08
REMARK 500 10 CYS A 18 -8.68 -148.24
REMARK 500 10 GLU A 43 27.79 -143.20
REMARK 500 11 CYS A 5 -36.46 57.69
REMARK 500 11 THR A 17 23.43 -77.72
REMARK 500 11 THR A 35 123.97 63.15
REMARK 500 12 ASP A 9 -167.67 -105.17
REMARK 500 12 CYS A 18 -0.31 -140.34
REMARK 500 12 GLU A 43 75.45 -152.71
REMARK 500 13 ALA A 3 20.05 -148.89
REMARK 500 13 CYS A 5 19.70 58.57
REMARK 500 13 ASP A 9 -168.61 -102.84
REMARK 500 13 CYS A 18 -8.42 -141.30
REMARK 500 14 SER A 4 168.79 60.81
REMARK 500 14 CYS A 5 19.35 -147.46
REMARK 500 14 ASP A 9 -168.51 -101.98
REMARK 500 14 CYS A 18 -5.52 -142.53
REMARK 500 14 GLU A 28 79.69 -100.86
REMARK 500 15 GLU A 28 79.37 -100.95
REMARK 500 15 GLU A 45 -72.73 -62.56
REMARK 500 16 SER A 4 -30.98 66.36
REMARK 500 16 ASP A 9 -166.73 -105.34
REMARK 500 16 CYS A 18 -11.07 -147.55
REMARK 500 16 CYS A 47 150.39 -48.74
REMARK 500 17 THR A 17 36.67 -93.52
REMARK 500 20 SER A 2 13.11 -149.84
REMARK 500 20 CYS A 18 -48.88 -150.48
REMARK 500 20 LYS A 20 78.30 44.34
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2BBX A 3 49 UNP P16893 TRAP_PLAFA 242 288
SEQADV 2BBX GLY A 1 UNP P16893 CLONING ARTIFACT
SEQADV 2BBX SER A 2 UNP P16893 CLONING ARTIFACT
SEQRES 1 A 49 GLY SER ALA SER CYS GLY VAL TRP ASP GLU TRP SER PRO
SEQRES 2 A 49 CYS SER VAL THR CYS GLY LYS GLY THR ARG SER ARG LYS
SEQRES 3 A 49 ARG GLU ILE LEU HIS GLU GLY CYS THR SER GLU ILE GLN
SEQRES 4 A 49 GLU GLN CYS GLU GLU GLU ARG CYS PRO PRO
SHEET 1 A 2 THR A 22 LYS A 26 0
SHEET 2 A 2 GLU A 37 GLN A 41 -1 O GLU A 40 N ARG A 23
SSBOND 1 CYS A 5 CYS A 34 1555 1555 2.03
SSBOND 2 CYS A 14 CYS A 42 1555 1555 2.03
SSBOND 3 CYS A 18 CYS A 47 1555 1555 2.04
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 9 2 Bytes