Header list of 1t8c.pdb file
Complete list - r 2 2 Bytes
HEADER IMMUNE SYSTEM 12-MAY-04 1T8C 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 02-MAR-22 1T8C 1 REMARK REVDAT 3 24-FEB-09 1T8C 1 VERSN REVDAT 2 04-OCT-05 1T8C 1 AUTHOR JRNL REVDAT 1 26-JUL-05 1T8C 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 1T8C 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_1000022438. 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 : 25MM TRIS, 125MM NACL, 4MM REMARK 210 CACL2, 0.02% NAN3, 2MM SOLUBLE REMARK 210 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 : GE/HOMEBUILT 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 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 CYS A 5 -92.56 -102.44 REMARK 500 1 ASN A 6 74.03 -177.73 REMARK 500 1 GLU A 10 -81.39 -127.99 REMARK 500 1 PHE A 15 -128.97 -130.94 REMARK 500 1 ARG A 17 -1.60 -165.63 REMARK 500 1 THR A 26 87.51 -166.03 REMARK 500 1 LYS A 27 -142.40 -162.95 REMARK 500 1 MET A 39 -27.18 -178.58 REMARK 500 1 GLU A 40 -91.22 -47.59 REMARK 500 1 VAL A 44 -70.77 -21.62 REMARK 500 1 SER A 60 -71.76 -60.06 REMARK 500 1 LEU A 71 -79.10 -54.14 REMARK 500 1 ASP A 72 -75.15 -110.20 REMARK 500 1 LEU A 73 -76.99 -152.96 REMARK 500 1 SER A 88 157.59 59.96 REMARK 500 1 TRP A 90 112.19 -35.07 REMARK 500 1 ALA A 91 115.30 -28.89 REMARK 500 1 SER A 97 25.40 -160.07 REMARK 500 1 GLN A 100 -33.95 -166.18 REMARK 500 1 ASP A 103 -29.21 -169.02 REMARK 500 1 ARG A 108 -160.31 168.86 REMARK 500 1 SER A 110 37.17 -81.69 REMARK 500 1 ARG A 112 -146.14 -133.13 REMARK 500 1 PHE A 117 -77.42 -40.90 REMARK 500 1 CYS A 118 32.18 174.49 REMARK 500 1 LEU A 122 -159.18 -85.34 REMARK 500 1 SER A 141 -65.17 -124.17 REMARK 500 2 VAL A 4 -58.43 -126.44 REMARK 500 2 ASN A 6 66.92 -168.21 REMARK 500 2 GLU A 10 -76.80 -123.60 REMARK 500 2 PHE A 15 -128.90 -131.16 REMARK 500 2 ARG A 17 -2.46 -165.47 REMARK 500 2 LYS A 27 -143.91 -167.18 REMARK 500 2 MET A 39 -26.88 -179.10 REMARK 500 2 GLU A 40 -89.64 -46.72 REMARK 500 2 VAL A 44 -72.47 -22.90 REMARK 500 2 ASP A 72 -77.36 -156.33 REMARK 500 2 LEU A 73 -78.47 -149.93 REMARK 500 2 ASP A 86 -64.10 -124.18 REMARK 500 2 SER A 88 162.76 59.56 REMARK 500 2 ASN A 89 -20.13 -140.45 REMARK 500 2 TRP A 90 95.89 -35.96 REMARK 500 2 ALA A 91 149.87 62.62 REMARK 500 2 GLU A 94 112.11 -160.44 REMARK 500 2 ARG A 98 41.87 -143.51 REMARK 500 2 SER A 99 -73.83 -80.96 REMARK 500 2 GLU A 102 96.49 60.50 REMARK 500 2 ARG A 112 -164.68 -163.17 REMARK 500 2 PHE A 117 -78.00 -41.31 REMARK 500 2 CYS A 118 32.17 174.32 REMARK 500 REMARK 500 THIS ENTRY HAS 562 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1T8D RELATED DB: PDB DBREF 1T8C 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 ASP A 38 1 11 HELIX 2 2 SER A 48 ALA A 59 1 12 SHEET 1 A 4 ILE A 13 ASN A 14 0 SHEET 2 A 4 LYS A 18 LYS A 24 -1 O TYR A 20 N ILE A 13 SHEET 3 A 4 ALA A 124 LEU A 130 -1 O ARG A 129 N CYS A 19 SHEET 4 A 4 GLN A 42 LEU A 43 -1 N GLN A 42 O ASP A 128 SHEET 1 B 4 PHE A 77 TRP A 79 0 SHEET 2 B 4 TRP A 65 ASN A 70 -1 N ARG A 69 O ILE A 78 SHEET 3 B 4 CYS A 104 ARG A 108 -1 O VAL A 105 N ILE A 66 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 - r 2 2 Bytes