HEADER CYTOKINE RECEPTOR 26-OCT-04 1XUT
TITLE SOLUTION STRUCTURE OF TACI-CRD2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY
COMPND 3 MEMBER 13B;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: TACI_D2;
COMPND 6 SYNONYM: TRANSMEMBRANE ACTIVATOR AND CAML INTERACTOR,
COMPND 7 TNFRSF13B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TNFRSF13B, TACI;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET32A
KEYWDS TNF RECEPTOR,CYTOKINE, CYSTEINE-RICH DOMAIN,RECEPTOR,
KEYWDS 2 CYTOKINE RECEPTOR
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR S.G.HYMOWITZ,D.R.PATEL,H.J.WALLWEBER,S.RUNYON,M.YAN,J.YIN,
AUTHOR 2 S.K.SHRIVER,N.C.GORDON,B.PAN,N.J.SKELTON,R.F.KELLEY,
AUTHOR 3 M.A.STAROVASNIK
REVDAT 3 24-FEB-09 1XUT 1 VERSN
REVDAT 2 24-MAY-05 1XUT 1 JRNL
REVDAT 1 09-NOV-04 1XUT 0
JRNL AUTH S.G.HYMOWITZ,D.R.PATEL,H.J.WALLWEBER,S.RUNYON,
JRNL AUTH 2 M.YAN,J.YIN,S.K.SHRIVER,N.C.GORDON,B.PAN,
JRNL AUTH 3 N.J.SKELTON,R.F.KELLEY,M.A.STAROVASNIK
JRNL TITL STRUCTURES OF APRIL-RECEPTOR COMPLEXES: LIKE BCMA,
JRNL TITL 2 TACI EMPLOYS ONLY A SINGLE CYSTEINE-RICH DOMAIN
JRNL TITL 3 FOR HIGH AFFINITY LIGAND BINDING.
JRNL REF J.BIOL.CHEM. V. 280 7218 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 15542592
JRNL DOI 10.1074/JBC.M411714200
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TALOS 2002, CNX 2002
REMARK 3 AUTHORS : CORNILESCU ET AL, 1999 (TALOS), ACCELRYS, SAN
REMARK 3 DIEGO, CA (CNX)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 100 STRUCTURES WERE CALCULATED USING
REMARK 3 TORSION ANGLE DYNAMICS FOLLOWED BY CARTESION DYNAMICS AND
REMARK 3 MINIMIZATION. THE 20 STRUCTURES WITH THE LOWEST RESTRAINT
REMARK 3 VIOLATION ENERGY WERE CHOSEN TO REPRESENT THE SOLUTION
REMARK 3 STRUCTURE.
REMARK 4
REMARK 4 1XUT COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-NOV-04.
REMARK 100 THE RCSB ID CODE IS RCSB030787.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 290
REMARK 210 PH : 7.2
REMARK 210 IONIC STRENGTH : 200 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8-1.0 MM TACI_D2 UNIFORMLY
REMARK 210 ENRICHED WITH 15N & 13C, 50 MM
REMARK 210 SODIUM PHOSPHATE, 150 MM
REMARK 210 SODIUM CHLORIDE, 1 MM SODIUM
REMARK 210 AZIDE,DIOXANE, 10% DEUTERIUM
REMARK 210 OXIDE; 0.8-1.0 MM TACI_D2
REMARK 210 UNIFORMLY ENRICHED WITH 15N &
REMARK 210 13C, 50 MM SODIUM PHOSPHATE,
REMARK 210 150 MM SODIUM CHLORIDE, 1 MM
REMARK 210 SODIUM AZIDE,DIOXANE, 10%
REMARK 210 DEUTERIUM OXIDE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY, 3D_
REMARK 210 13C-SEPARATED_NOESY, 2D NOESY,
REMARK 210 3D-HNHB
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ, 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 2000.1, SPARKY 3.11,
REMARK 210 XWINNMR 3.5, CYANA 1.1
REMARK 210 METHOD USED : THE FINAL STRUCTURES WERE
REMARK 210 CALCULATED USING THE PROGRAM
REMARK 210 CNX (VERSION 2002; ACCELRYS,
REMARK 210 SAN DIEGO, CA).
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
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: ALL NMR DATA WERE PROCESSED USING FELIX (VERSION
REMARK 210 2000.1; ACCELRYS, SAN DIEGO, CA) AND ANALYZED USING SPARKY
REMARK 210 (VERSION 3.11; GODDARD & KNELLER, UNIVERSITY OF CALIFORNIA,
REMARK 210 SAN FRANCISCO, CA). NOE ASSIGNMENTS WERE OBTAINED USING CANDID
REMARK 210 (HERRMANN ET AL., 2002). LOOSE BACKBONE DIGHEDRAL ANGLE
REMARK 210 RESTRAINTS WERE OBTAINED FROM ANALYSIS OF BACKBONE CHEMICAL
REMARK 210 SHIFTS WITH THE PROGRAM TALOS (CORNILESCU ET AL., 1999).
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
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 SER A 68 -33.78 -145.56
REMARK 500 1 GLU A 74 -165.39 -119.99
REMARK 500 1 PRO A 97 -176.62 -58.45
REMARK 500 1 PHE A 103 -69.23 -94.58
REMARK 500 1 LEU A 108 -69.12 -132.41
REMARK 500 2 TRP A 67 36.20 -97.41
REMARK 500 2 SER A 68 46.02 -164.01
REMARK 500 2 SER A 70 49.75 -173.61
REMARK 500 2 PHE A 103 -69.16 -100.65
REMARK 500 3 SER A 68 -63.37 -174.93
REMARK 500 3 ARG A 72 176.17 -59.24
REMARK 500 3 PRO A 97 -177.03 -61.40
REMARK 500 3 PHE A 103 -69.88 -94.48
REMARK 500 3 LEU A 108 -45.59 -157.74
REMARK 500 4 SER A 68 49.85 -176.68
REMARK 500 4 GLN A 95 49.04 -140.01
REMARK 500 4 ASN A 106 86.19 -58.46
REMARK 500 4 LYS A 107 -36.46 -179.14
REMARK 500 4 LEU A 108 64.93 -112.34
REMARK 500 5 TRP A 67 -82.15 -118.93
REMARK 500 5 SER A 70 103.51 -57.08
REMARK 500 5 GLN A 95 56.90 -145.51
REMARK 500 5 PRO A 97 -177.00 -64.79
REMARK 500 5 PHE A 103 -70.25 -80.10
REMARK 500 6 SER A 68 -36.32 -178.44
REMARK 500 6 SER A 70 38.22 -95.67
REMARK 500 6 GLN A 95 58.40 -143.08
REMARK 500 6 PHE A 103 -69.26 -103.35
REMARK 500 6 ASN A 106 76.12 -68.16
REMARK 500 6 LYS A 107 -41.88 -165.66
REMARK 500 7 SER A 68 37.52 -99.50
REMARK 500 7 SER A 70 -74.75 -74.24
REMARK 500 8 TRP A 67 -65.16 -102.17
REMARK 500 8 ARG A 72 171.21 -57.66
REMARK 500 8 PHE A 103 -68.53 -90.04
REMARK 500 8 LYS A 107 36.63 -94.31
REMARK 500 8 LEU A 108 43.07 -179.08
REMARK 500 9 PRO A 66 -74.53 -59.56
REMARK 500 9 SER A 70 97.60 -178.18
REMARK 500 9 LEU A 108 -35.89 -175.98
REMARK 500 10 SER A 65 58.88 -158.02
REMARK 500 10 PRO A 66 -72.66 -57.63
REMARK 500 10 PRO A 97 -178.01 -56.72
REMARK 500 11 SER A 65 108.40 -56.59
REMARK 500 11 SER A 68 -90.31 -159.70
REMARK 500 11 GLN A 95 55.71 -148.12
REMARK 500 11 PHE A 103 -68.99 -98.00
REMARK 500 11 ASN A 106 -37.95 -35.48
REMARK 500 11 LEU A 108 -177.99 -177.11
REMARK 500 12 SER A 70 43.15 -93.86
REMARK 500 12 GLU A 74 158.28 -49.40
REMARK 500 12 ILE A 92 -85.89 -108.21
REMARK 500 12 CYS A 93 116.75 57.39
REMARK 500 12 PHE A 103 -68.29 -103.95
REMARK 500 13 SER A 68 89.78 -151.70
REMARK 500 13 SER A 70 124.35 -172.20
REMARK 500 13 PRO A 97 176.89 -52.85
REMARK 500 13 LEU A 108 35.28 -149.98
REMARK 500 14 TRP A 67 -47.61 -131.92
REMARK 500 14 PRO A 97 176.58 -58.61
REMARK 500 14 PHE A 103 -69.92 -90.38
REMARK 500 15 PHE A 103 -72.49 -102.73
REMARK 500 15 ASN A 106 74.52 -60.89
REMARK 500 15 LYS A 107 -52.43 -178.56
REMARK 500 16 SER A 68 -44.22 -149.67
REMARK 500 16 PRO A 97 -176.85 -58.78
REMARK 500 16 ASN A 106 -41.62 -179.60
REMARK 500 16 LYS A 107 26.19 -149.57
REMARK 500 17 SER A 70 66.58 -168.93
REMARK 500 17 PHE A 103 -68.81 -104.94
REMARK 500 17 LEU A 108 -166.19 -113.56
REMARK 500 18 SER A 68 -64.19 -175.15
REMARK 500 18 GLN A 95 78.12 -113.23
REMARK 500 18 PHE A 103 -72.62 -101.47
REMARK 500 18 LEU A 108 -178.18 -173.15
REMARK 500 19 SER A 68 -66.05 -173.11
REMARK 500 19 GLN A 95 58.69 -140.60
REMARK 500 19 PHE A 103 -61.14 -94.75
REMARK 500 19 LYS A 107 53.84 -94.97
REMARK 500 19 LEU A 108 111.73 -173.13
REMARK 500 20 SER A 65 87.42 -158.65
REMARK 500 20 ARG A 72 173.71 -57.92
REMARK 500 20 PRO A 97 -176.88 -61.31
REMARK 500 20 PHE A 103 -68.57 -104.02
REMARK 500 20 LYS A 107 -79.21 -60.57
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1XU1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF APRIL BOUND TO TACI
REMARK 900 RELATED ID: 1XU2 RELATED DB: PDB
DBREF 1XUT A 68 109 UNP O14836 TR13B_HUMAN 68 109
SEQADV 1XUT GLY A 64 UNP O14836 CLONING ARTIFACT
SEQADV 1XUT SER A 65 UNP O14836 CLONING ARTIFACT
SEQADV 1XUT PRO A 66 UNP O14836 CLONING ARTIFACT
SEQADV 1XUT TRP A 67 UNP O14836 CLONING ARTIFACT
SEQRES 1 A 46 GLY SER PRO TRP SER LEU SER CYS ARG LYS GLU GLN GLY
SEQRES 2 A 46 LYS PHE TYR ASP HIS LEU LEU ARG ASP CYS ILE SER CYS
SEQRES 3 A 46 ALA SER ILE CYS GLY GLN HIS PRO LYS GLN CYS ALA TYR
SEQRES 4 A 46 PHE CYS GLU ASN LYS LEU ARG
HELIX 1 1 LYS A 98 PHE A 103 5 6
SHEET 1 A 2 LYS A 77 ASP A 80 0
SHEET 2 A 2 ASP A 85 SER A 88 -1 O ILE A 87 N PHE A 78
SSBOND 1 CYS A 71 CYS A 86 1555 1555 2.03
SSBOND 2 CYS A 89 CYS A 100 1555 1555 2.03
SSBOND 3 CYS A 93 CYS A 104 1555 1555 2.03
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
(ATOM LINES ARE NOT SHOWN.)
END
