Header list of 1t8d.pdb file
Complete list - t 27 2 Bytes
HEADER IMMUNE SYSTEM 12-MAY-04 1T8D
TITLE STRUCTURE OF THE C-TYPE LECTIN DOMAIN OF CD23
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LOW AFFINITY IMMUNOGLOBULIN EPSILON FC RECEPTOR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DERCD23;
COMPND 5 SYNONYM: LYMPHOCYTE IGE RECEPTOR, FC-EPSILON-RII, CD23,
COMPND 6 IMMUNOGLOBULIN E-BINDING FACTOR;
COMPND 7 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: FCER2, IGEBF;
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: PET5A
KEYWDS C-TYPE LECTIN, FCERII, FC RECEPTOR, IGE, IMMUNE SYSTEM
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR R.G.HIBBERT,P.TERIETE,G.J.GRUNDY,B.J.SUTTON,H.J.GOULD,J.M.MCDONNELL
REVDAT 4 27-OCT-21 1T8D 1 REMARK
REVDAT 3 24-FEB-09 1T8D 1 VERSN
REVDAT 2 04-OCT-05 1T8D 1 AUTHOR JRNL
REVDAT 1 26-JUL-05 1T8D 0
JRNL AUTH R.G.HIBBERT,P.TERIETE,G.J.GRUNDY,R.L.BEAVIL,R.RELJIC,
JRNL AUTH 2 V.M.HOLERS,J.P.HANNAN,B.J.SUTTON,H.J.GOULD,J.M.MCDONNELL
JRNL TITL THE STRUCTURE OF HUMAN CD23 AND ITS INTERACTIONS WITH IGE
JRNL TITL 2 AND CD21
JRNL REF J.EXP.MED. V. 202 751 2005
JRNL REFN ISSN 0022-1007
JRNL PMID 16172256
JRNL DOI 10.1084/JEM.20050811
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : A.T.BRUNGER, P.D.ADAMS, G.M.CLORE, W.L.DELANO,
REMARK 3 P.GROS, R.W.GROSSE-KUNSTLEVE, J.-S.JIANG,
REMARK 3 J.KUSZEWSKI, M.NILGES, N.S.PANNU, R.J.READ,
REMARK 3 L.M.RICE, T.SIMONSON, G.L.WARREN
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1T8D COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-MAY-04.
REMARK 100 THE DEPOSITION ID IS D_1000022439.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 162 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 25 MM TRIS, 125 MM NACL, 4 MM
REMARK 210 CACL2, 0.02% NAN3, 2 MM [U-100%
REMARK 210 13C; U-100% 15N] SOLUBLE CD23
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 15N EDITED NOESY-HSQC; 13C
REMARK 210 EDITED NOESY-HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : OMEGA
REMARK 210 SPECTROMETER MANUFACTURER : HOME-BUILT
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS 1.1
REMARK 210 METHOD USED : STANDARD RECOMMENDED PROTOCOL
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 : 1
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: 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 SER A 45 H GLY A 67 1.33
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 ASN A 6 87.35 -169.06
REMARK 500 1 PRO A 9 -75.81 -92.75
REMARK 500 1 GLU A 10 -86.61 -102.23
REMARK 500 1 PHE A 15 -130.26 -128.65
REMARK 500 1 ARG A 17 0.73 -164.76
REMARK 500 1 THR A 26 -169.59 55.26
REMARK 500 1 LYS A 27 16.12 -161.20
REMARK 500 1 GLU A 40 39.38 71.33
REMARK 500 1 VAL A 44 -76.37 -4.44
REMARK 500 1 LEU A 71 -79.58 -54.76
REMARK 500 1 ASP A 72 -71.69 -98.19
REMARK 500 1 LEU A 73 -64.55 -157.57
REMARK 500 1 SER A 88 146.94 62.02
REMARK 500 1 TRP A 90 92.20 -45.68
REMARK 500 1 ALA A 91 135.56 60.99
REMARK 500 1 THR A 96 -163.74 53.41
REMARK 500 1 SER A 97 -13.29 -145.01
REMARK 500 1 GLN A 100 -22.16 -140.20
REMARK 500 1 GLU A 102 93.60 -161.65
REMARK 500 1 ARG A 120 -92.17 -93.44
REMARK 500 1 LYS A 121 73.63 -178.07
REMARK 500 1 LEU A 122 -163.26 -106.00
REMARK 500 1 ALA A 131 171.40 -53.02
REMARK 500 1 THR A 134 87.85 -153.75
REMARK 500 1 SER A 138 -66.57 -100.59
REMARK 500 1 ALA A 142 81.01 55.84
REMARK 500 2 VAL A 4 -28.37 -142.37
REMARK 500 2 CYS A 5 -33.25 -157.65
REMARK 500 2 ASN A 6 55.43 70.79
REMARK 500 2 PRO A 9 -73.44 -94.69
REMARK 500 2 GLU A 10 -93.40 -99.59
REMARK 500 2 TRP A 12 132.05 -37.37
REMARK 500 2 PHE A 15 -130.38 -128.63
REMARK 500 2 ARG A 17 -0.26 -164.62
REMARK 500 2 THR A 26 -158.47 -160.32
REMARK 500 2 LYS A 27 -64.82 -141.06
REMARK 500 2 VAL A 44 -76.85 -5.49
REMARK 500 2 SER A 60 -60.01 -98.29
REMARK 500 2 ASP A 72 -96.64 57.23
REMARK 500 2 LEU A 73 -55.71 -158.02
REMARK 500 2 SER A 88 148.78 61.58
REMARK 500 2 TRP A 90 102.89 -41.76
REMARK 500 2 SER A 99 -168.21 -164.61
REMARK 500 2 GLN A 100 111.34 -160.61
REMARK 500 2 ASP A 103 105.20 -167.22
REMARK 500 2 ARG A 112 -156.08 -151.15
REMARK 500 2 PHE A 117 26.76 -72.65
REMARK 500 2 ARG A 120 -140.26 -93.66
REMARK 500 2 LYS A 121 79.84 -170.93
REMARK 500 2 ALA A 131 95.31 -56.08
REMARK 500
REMARK 500 THIS ENTRY HAS 531 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1T8C RELATED DB: PDB
DBREF 1T8D A 1 143 UNP P06734 FCER2_HUMAN 156 298
SEQRES 1 A 143 SER GLY PHE VAL CYS ASN THR CYS PRO GLU LYS TRP ILE
SEQRES 2 A 143 ASN PHE GLN ARG LYS CYS TYR TYR PHE GLY LYS GLY THR
SEQRES 3 A 143 LYS GLN TRP VAL HIS ALA ARG TYR ALA CYS ASP ASP MET
SEQRES 4 A 143 GLU GLY GLN LEU VAL SER ILE HIS SER PRO GLU GLU GLN
SEQRES 5 A 143 ASP PHE LEU THR LYS HIS ALA SER HIS THR GLY SER TRP
SEQRES 6 A 143 ILE GLY LEU ARG ASN LEU ASP LEU LYS GLY GLU PHE ILE
SEQRES 7 A 143 TRP VAL ASP GLY SER HIS VAL ASP TYR SER ASN TRP ALA
SEQRES 8 A 143 PRO GLY GLU PRO THR SER ARG SER GLN GLY GLU ASP CYS
SEQRES 9 A 143 VAL MET MET ARG GLY SER GLY ARG TRP ASN ASP ALA PHE
SEQRES 10 A 143 CYS ASP ARG LYS LEU GLY ALA TRP VAL CYS ASP ARG LEU
SEQRES 11 A 143 ALA THR CYS THR PRO PRO ALA SER GLU GLY SER ALA GLU
HELIX 1 1 GLN A 28 MET A 39 1 12
HELIX 2 2 SER A 48 ALA A 59 1 12
SHEET 1 A 3 ILE A 13 ASN A 14 0
SHEET 2 A 3 LYS A 18 LYS A 24 -1 O TYR A 20 N ILE A 13
SHEET 3 A 3 ALA A 124 LEU A 130 -1 O CYS A 127 N TYR A 21
SHEET 1 B 4 PHE A 77 TRP A 79 0
SHEET 2 B 4 SER A 64 ASN A 70 -1 N ARG A 69 O ILE A 78
SHEET 3 B 4 CYS A 104 ARG A 108 -1 O MET A 107 N SER A 64
SHEET 4 B 4 ARG A 112 ALA A 116 -1 O ASN A 114 N MET A 106
SSBOND 1 CYS A 5 CYS A 133 1555 1555 2.03
SSBOND 2 CYS A 8 CYS A 19 1555 1555 2.03
SSBOND 3 CYS A 36 CYS A 127 1555 1555 2.03
SSBOND 4 CYS A 104 CYS A 118 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
Complete list - t 27 2 Bytes