Header list of 1g84.pdb file
Complete list - t 27 2 Bytes
HEADER IMMUNE SYSTEM 16-NOV-00 1G84 TITLE THE SOLUTION STRUCTURE OF THE C EPSILON2 DOMAIN FROM IGE COMPND MOL_ID: 1; COMPND 2 MOLECULE: IMMUNOGLOBULIN E; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C EPSILON2; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3) KEYWDS ALLERGY, IGE, IMMUNOGLOBULIN DOMAIN, CE2, ANTIBODY, FC., IMMUNE KEYWDS 2 SYSTEM EXPDTA SOLUTION NMR NUMMDL 15 AUTHOR J.M.MCDONNELL,D.COWBURN,H.J.GOULD,B.J.SUTTON,R.CALVERT,R.E.BEAVIL, AUTHOR 2 A.J.BEAVIL,A.J.HENRY REVDAT 4 27-OCT-21 1G84 1 REMARK SEQADV REVDAT 3 24-FEB-09 1G84 1 VERSN REVDAT 2 01-APR-03 1G84 1 JRNL REVDAT 1 16-MAY-01 1G84 0 JRNL AUTH J.M.MCDONNELL,R.CALVERT,R.L.BEAVIL,A.J.BEAVIL,A.J.HENRY, JRNL AUTH 2 B.J.SUTTON,H.J.GOULD,D.COWBURN JRNL TITL THE STRUCTURE OF THE IGE CEPSILON2 DOMAIN AND ITS ROLE IN JRNL TITL 2 STABILIZING THE COMPLEX WITH ITS HIGH-AFFINITY RECEPTOR JRNL TITL 3 FCEPSILONRIALPHA. JRNL REF NAT.STRUCT.BIOL. V. 8 437 2001 JRNL REFN ISSN 1072-8368 JRNL PMID 11323720 JRNL DOI 10.1038/87603 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : DYANA 1.5, DYANA 1.5 REMARK 3 AUTHORS : GUNTERT, MUMENTHALER, HERRMANN (DYANA), GUNTERT, REMARK 3 MUMENTHALER, HERRMANN (DYANA) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1G84 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-NOV-00. REMARK 100 THE DEPOSITION ID IS D_1000012352. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298 REMARK 210 PH : 6 REMARK 210 IONIC STRENGTH : 100MM REMARK 210 PRESSURE : 1 ATM REMARK 210 SAMPLE CONTENTS : 2MM CE2 U-15N,13C; 1.4MM CE2 U REMARK 210 -15N REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N REMARK 210 -SEPARATED_NOESY; HNHA; HCCH- REMARK 210 TOCSY; HNCOCA; HNCA REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XEASY 1.3.13 REMARK 210 METHOD USED : STRUCTURES CALCULATED USING REMARK 210 DYANA REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 1000 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL 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 HA THR A 87 HB3 SER A 100 1.22 REMARK 500 O THR A 57 H GLU A 72 1.51 REMARK 500 H SER A 59 O GLN A 70 1.52 REMARK 500 OG1 THR A 61 O SER A 68 1.96 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 ARG A 2 79.13 -167.15 REMARK 500 1 PHE A 4 -176.84 58.36 REMARK 500 1 ASP A 17 13.02 -140.51 REMARK 500 1 HIS A 21 178.99 64.53 REMARK 500 1 PHE A 22 148.58 57.68 REMARK 500 1 THR A 36 144.93 50.18 REMARK 500 1 THR A 39 171.27 159.20 REMARK 500 1 ILE A 40 -139.38 -111.75 REMARK 500 1 GLN A 49 86.52 167.61 REMARK 500 1 VAL A 50 43.68 -85.23 REMARK 500 1 ASP A 52 -151.13 -64.11 REMARK 500 1 ASP A 83 151.46 66.88 REMARK 500 1 ARG A 84 -173.87 -173.11 REMARK 500 1 SER A 100 -142.01 -166.52 REMARK 500 2 PHE A 4 173.54 76.94 REMARK 500 2 SER A 16 77.90 -155.88 REMARK 500 2 ASP A 17 155.56 -38.38 REMARK 500 2 HIS A 21 112.58 71.09 REMARK 500 2 PHE A 22 158.82 56.15 REMARK 500 2 THR A 36 139.64 49.56 REMARK 500 2 THR A 39 -168.24 95.12 REMARK 500 2 ILE A 40 -142.23 -128.47 REMARK 500 2 GLN A 49 101.49 172.14 REMARK 500 2 MET A 51 -155.68 -65.77 REMARK 500 2 ASP A 83 149.14 69.10 REMARK 500 2 SER A 100 -143.27 -171.82 REMARK 500 2 LYS A 102 -157.02 -169.38 REMARK 500 2 LYS A 103 -174.71 59.10 REMARK 500 2 SER A 104 -124.36 -104.87 REMARK 500 3 ARG A 2 173.52 174.11 REMARK 500 3 ASP A 3 176.86 52.11 REMARK 500 3 PHE A 4 158.57 85.74 REMARK 500 3 ASP A 17 171.61 176.78 REMARK 500 3 GLN A 27 77.70 -118.19 REMARK 500 3 THR A 36 139.56 51.48 REMARK 500 3 THR A 39 -168.11 88.58 REMARK 500 3 ILE A 40 -139.92 -125.94 REMARK 500 3 GLN A 49 96.74 64.33 REMARK 500 3 VAL A 50 43.55 -86.06 REMARK 500 3 ASP A 52 -154.73 -65.89 REMARK 500 3 ASP A 83 146.72 70.10 REMARK 500 3 ARG A 84 175.02 177.58 REMARK 500 3 SER A 100 -141.84 -167.02 REMARK 500 3 LYS A 102 137.17 -171.43 REMARK 500 3 SER A 104 18.83 -149.39 REMARK 500 4 ARG A 2 -136.95 35.68 REMARK 500 4 ASP A 3 157.40 57.66 REMARK 500 4 PHE A 4 95.91 56.67 REMARK 500 4 PRO A 7 -94.83 -74.97 REMARK 500 4 THR A 8 149.94 -171.14 REMARK 500 REMARK 500 THIS ENTRY HAS 234 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL DBREF 1G84 A 1 105 UNP P01854 IGHE_HUMAN 106 210 SEQADV 1G84 SER A 16 UNP P01854 CYS 121 ENGINEERED MUTATION SEQADV 1G84 SER A 104 UNP P01854 CYS 209 ENGINEERED MUTATION SEQRES 1 A 105 SER ARG ASP PHE THR PRO PRO THR VAL LYS ILE LEU GLN SEQRES 2 A 105 SER SER SER ASP GLY GLY GLY HIS PHE PRO PRO THR ILE SEQRES 3 A 105 GLN LEU LEU CYS LEU VAL SER GLY TYR THR PRO GLY THR SEQRES 4 A 105 ILE ASN ILE THR TRP LEU GLU ASP GLY GLN VAL MET ASP SEQRES 5 A 105 VAL ASP LEU SER THR ALA SER THR THR GLN GLU GLY GLU SEQRES 6 A 105 LEU ALA SER THR GLN SER GLU LEU THR LEU SER GLN LYS SEQRES 7 A 105 HIS TRP LEU SER ASP ARG THR TYR THR CYS GLN VAL THR SEQRES 8 A 105 TYR GLN GLY HIS THR PHE GLU ASP SER THR LYS LYS SER SEQRES 9 A 105 ALA HELIX 1 1 GLN A 77 SER A 82 1 6 SHEET 1 A 4 THR A 8 SER A 14 0 SHEET 2 A 4 THR A 25 SER A 33 -1 N GLN A 27 O SER A 14 SHEET 3 A 4 LEU A 66 SER A 76 -1 N THR A 69 O VAL A 32 SHEET 4 A 4 LEU A 55 GLU A 63 -1 O LEU A 55 N THR A 74 SHEET 1 B 3 ASN A 41 ASP A 47 0 SHEET 2 B 3 ARG A 84 TYR A 92 -1 O THR A 85 N ASP A 47 SHEET 3 B 3 HIS A 95 LYS A 103 -1 O HIS A 95 N TYR A 92 SSBOND 1 CYS A 30 CYS A 88 1555 1555 1.88 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