Header list of 1g2t.pdb file
Complete list - b 23 2 Bytes
HEADER CYTOKINE 20-OCT-00 1G2T
TITLE SOLUTION STRUCTURE OF EOTAXIN-3
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EOTAXIN-3;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: SMALL INDUCIBLE CYTOKINE A26, MACROPHAGE INFLAMMATORY
COMPND 5 PROTEIN 4-ALPHA;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: LUNG;
SOURCE 6 GENE: EOTAXIN-3;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET28A+
KEYWDS BETA-BETA-BETA-ALPHA HELIX, CYTOKINE
EXPDTA SOLUTION NMR
NUMMDL 20
MDLTYP MINIMIZED AVERAGE
AUTHOR J.YE,K.L.MAYER,M.R.MAYER,M.J.STONE
REVDAT 3 23-FEB-22 1G2T 1 REMARK
REVDAT 2 24-FEB-09 1G2T 1 VERSN
REVDAT 1 13-MAR-02 1G2T 0
JRNL AUTH J.YE,K.L.MAYER,M.R.MAYER,M.J.STONE
JRNL TITL NMR SOLUTION STRUCTURE AND BACKBONE DYNAMICS OF THE CC
JRNL TITL 2 CHEMOKINE EOTAXIN-3.
JRNL REF BIOCHEMISTRY V. 40 7820 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11425309
JRNL DOI 10.1021/BI010252S
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR XPLOR98.1, PROCHECK-NMR PROCHECK V.3
REMARK 3 AUTHORS : BRUNGER (X-PLOR), LASKOWSKI (PROCHECK-NMR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 1250 RESTRAINTS, 1157 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 69
REMARK 3 DIHEDRAL ANGLE RESTRAINTS, 17 DISTANCE RESTRAINTS FROM HYDROGN
REMARK 3 BONDS.
REMARK 4
REMARK 4 1G2T COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-OCT-00.
REMARK 100 THE DEPOSITION ID IS D_1000012163.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 5
REMARK 210 IONIC STRENGTH : 20 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM EOTAXIN-3,U-15N, 20MM
REMARK 210 SODIUM ACETATE (DETEURATED), 90%
REMARK 210 H2O, 10% D2O; 2 MM EOTAXIN-3,U-
REMARK 210 15N, 13C, 20MM SODIUM ACETATE
REMARK 210 (DETEURATED), 90% H2O, 10% D2O;
REMARK 210 2 MM EOTAXIN-3,U-15N, 13C, 20MM
REMARK 210 SODIUM ACETATE (DETEURATED), 90%
REMARK 210 H2O, 10% D2O; 0.5 MM EOTAXIN-3,
REMARK 210 10% 13C-LABELED, 20MM SODIUM
REMARK 210 ACETATE (DETEURATED), 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNHA;
REMARK 210 13C, 15N SIMULTANEOUSLY EDITED
REMARK 210 NOESY; 3D_13C-SEPARATED_NOESY;
REMARK 210 13C-EDITED HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX FELIX98, VNMR VNMR6.1,
REMARK 210 PROCHECK-NMR PROCHECK V.3
REMARK 210 METHOD USED : DISTANCE GEOMETRY-SIMULATED
REMARK 210 ANNEALING PROTOCOL IMPLEMENTED
REMARK 210 IN XPLOR
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : PDB ID 1G2S
REMARK 210
REMARK 210 REMARK: NULL
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: 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 5 30.05 -167.96
REMARK 500 1 SER A 7 42.53 -91.82
REMARK 500 1 THR A 9 115.45 -162.19
REMARK 500 1 CYS A 10 -158.05 -73.64
REMARK 500 1 PHE A 12 31.63 -160.11
REMARK 500 1 GLN A 13 91.59 -169.64
REMARK 500 1 LYS A 17 134.85 -179.29
REMARK 500 1 ARG A 25 -53.71 -129.68
REMARK 500 1 SER A 26 -158.01 -165.86
REMARK 500 1 GLU A 28 145.75 -174.99
REMARK 500 1 SER A 33 39.46 -89.66
REMARK 500 1 LYS A 66 141.10 62.50
REMARK 500 2 SER A 4 52.29 -106.03
REMARK 500 2 SER A 7 40.65 -100.89
REMARK 500 2 LYS A 8 -158.70 -60.13
REMARK 500 2 PHE A 12 -62.71 -136.69
REMARK 500 2 HIS A 16 39.19 -91.57
REMARK 500 2 SER A 26 -160.23 -167.66
REMARK 500 2 THR A 43 -167.91 -104.81
REMARK 500 2 THR A 67 50.50 -158.74
REMARK 500 3 THR A 9 106.83 -160.59
REMARK 500 3 CYS A 10 -168.80 -59.85
REMARK 500 3 SER A 26 -156.40 -162.04
REMARK 500 3 GLU A 28 139.04 -175.64
REMARK 500 3 THR A 30 170.53 -57.22
REMARK 500 4 ARG A 2 -81.38 60.16
REMARK 500 4 ILE A 6 33.89 -98.70
REMARK 500 4 LYS A 8 -167.26 -178.05
REMARK 500 4 THR A 9 -48.12 -131.89
REMARK 500 4 CYS A 10 -157.82 -75.66
REMARK 500 4 PHE A 12 -70.43 -141.26
REMARK 500 4 LYS A 17 146.55 -177.57
REMARK 500 4 SER A 26 -153.09 -173.27
REMARK 500 4 GLU A 28 126.91 -178.04
REMARK 500 4 GLN A 36 70.39 -100.78
REMARK 500 4 GLN A 70 -167.63 -122.14
REMARK 500 5 ARG A 2 -171.07 53.16
REMARK 500 5 ILE A 6 39.38 -98.81
REMARK 500 5 LYS A 8 -175.38 -68.92
REMARK 500 5 PHE A 12 -48.14 -146.31
REMARK 500 5 ARG A 25 -38.10 -131.05
REMARK 500 5 SER A 26 -162.25 -176.34
REMARK 500 5 GLU A 28 133.39 -179.87
REMARK 500 5 SER A 31 -176.54 -68.30
REMARK 500 5 SER A 33 39.23 -97.73
REMARK 500 5 THR A 43 -166.95 -105.78
REMARK 500 5 LYS A 66 103.55 54.29
REMARK 500 5 THR A 67 49.99 -144.81
REMARK 500 6 ARG A 2 102.21 55.59
REMARK 500 6 ASP A 5 175.99 -59.51
REMARK 500
REMARK 500 THIS ENTRY HAS 196 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 2 0.25 SIDE CHAIN
REMARK 500 1 ARG A 25 0.15 SIDE CHAIN
REMARK 500 1 ARG A 37 0.29 SIDE CHAIN
REMARK 500 1 ARG A 45 0.27 SIDE CHAIN
REMARK 500 1 ARG A 54 0.30 SIDE CHAIN
REMARK 500 2 ARG A 2 0.31 SIDE CHAIN
REMARK 500 2 ARG A 25 0.10 SIDE CHAIN
REMARK 500 2 ARG A 37 0.17 SIDE CHAIN
REMARK 500 2 ARG A 45 0.31 SIDE CHAIN
REMARK 500 2 ARG A 54 0.29 SIDE CHAIN
REMARK 500 3 ARG A 2 0.28 SIDE CHAIN
REMARK 500 3 ARG A 25 0.16 SIDE CHAIN
REMARK 500 3 ARG A 37 0.26 SIDE CHAIN
REMARK 500 3 ARG A 45 0.32 SIDE CHAIN
REMARK 500 3 ARG A 54 0.29 SIDE CHAIN
REMARK 500 4 ARG A 2 0.28 SIDE CHAIN
REMARK 500 4 ARG A 25 0.31 SIDE CHAIN
REMARK 500 4 ARG A 37 0.29 SIDE CHAIN
REMARK 500 4 ARG A 45 0.32 SIDE CHAIN
REMARK 500 4 ARG A 54 0.30 SIDE CHAIN
REMARK 500 5 ARG A 2 0.30 SIDE CHAIN
REMARK 500 5 ARG A 25 0.18 SIDE CHAIN
REMARK 500 5 ARG A 37 0.17 SIDE CHAIN
REMARK 500 5 ARG A 45 0.16 SIDE CHAIN
REMARK 500 5 ARG A 54 0.26 SIDE CHAIN
REMARK 500 6 ARG A 2 0.27 SIDE CHAIN
REMARK 500 6 ARG A 25 0.21 SIDE CHAIN
REMARK 500 6 ARG A 37 0.30 SIDE CHAIN
REMARK 500 6 ARG A 45 0.24 SIDE CHAIN
REMARK 500 6 ARG A 54 0.30 SIDE CHAIN
REMARK 500 7 ARG A 2 0.30 SIDE CHAIN
REMARK 500 7 ARG A 25 0.32 SIDE CHAIN
REMARK 500 7 ARG A 37 0.20 SIDE CHAIN
REMARK 500 7 ARG A 45 0.32 SIDE CHAIN
REMARK 500 7 ARG A 54 0.31 SIDE CHAIN
REMARK 500 8 ARG A 2 0.32 SIDE CHAIN
REMARK 500 8 ARG A 25 0.31 SIDE CHAIN
REMARK 500 8 ARG A 37 0.19 SIDE CHAIN
REMARK 500 8 ARG A 45 0.30 SIDE CHAIN
REMARK 500 8 ARG A 54 0.32 SIDE CHAIN
REMARK 500 9 ARG A 2 0.30 SIDE CHAIN
REMARK 500 9 ARG A 25 0.23 SIDE CHAIN
REMARK 500 9 ARG A 37 0.31 SIDE CHAIN
REMARK 500 9 ARG A 45 0.24 SIDE CHAIN
REMARK 500 9 ARG A 54 0.27 SIDE CHAIN
REMARK 500 10 ARG A 2 0.32 SIDE CHAIN
REMARK 500 10 ARG A 25 0.27 SIDE CHAIN
REMARK 500 10 ARG A 37 0.14 SIDE CHAIN
REMARK 500 10 ARG A 45 0.20 SIDE CHAIN
REMARK 500 10 ARG A 54 0.27 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 100 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G2S RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF EOTAXIN-3, ENERGY MINIMIZED AVERAGE STRUCTURE
DBREF 1G2T A 1 71 UNP Q9Y258 CCL26_HUMAN 24 94
SEQRES 1 A 71 THR ARG GLY SER ASP ILE SER LYS THR CYS CYS PHE GLN
SEQRES 2 A 71 TYR SER HIS LYS PRO LEU PRO TRP THR TRP VAL ARG SER
SEQRES 3 A 71 TYR GLU PHE THR SER ASN SER CYS SER GLN ARG ALA VAL
SEQRES 4 A 71 ILE PHE THR THR LYS ARG GLY LYS LYS VAL CYS THR HIS
SEQRES 5 A 71 PRO ARG LYS LYS TRP VAL GLN LYS TYR ILE SER LEU LEU
SEQRES 6 A 71 LYS THR PRO LYS GLN LEU
HELIX 1 1 PRO A 20 THR A 22 5 3
HELIX 2 2 LYS A 55 LEU A 65 1 11
SHEET 1 A 3 VAL A 24 PHE A 29 0
SHEET 2 A 3 VAL A 39 THR A 43 -1 O ILE A 40 N GLU A 28
SHEET 3 A 3 LYS A 48 THR A 51 -1 N VAL A 49 O PHE A 41
SSBOND 1 CYS A 10 CYS A 34 1555 1555 2.02
SSBOND 2 CYS A 11 CYS A 50 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
MODEL 1
Complete list - b 23 2 Bytes