Header list of 1jbj.pdb file
Complete list - b 23 2 Bytes
HEADER IMMUNE SYSTEM 05-JUN-01 1JBJ TITLE CD3 EPSILON AND GAMMA ECTODOMAIN FRAGMENT COMPLEX IN SINGLE-CHAIN TITLE 2 CONSTRUCT COMPND MOL_ID: 1; COMPND 2 MOLECULE: CD3 EPSILON AND GAMMA ECTODOMAIN FRAGMENT COMPLEX; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: RESIDUES 1-79 ARE A FRAGMENT OF T-CELL SURFACE COMPND 6 GLYCOPROTEIN CD3 EPSILON CHAIN, RESIDUES 80-105 ARE AN ENGINEERED COMPND 7 LINKER MODELED FROM A SINGLE CHAIN T CELL RECEPTOR CONSTRUCT, COMPND 8 RESIDUES 106-186 ARE A FRAGMENT OF T-CELL SURFACE GLYCOPROTEIN CD3 COMPND 9 GAMMA CHAIN SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 GENE: CD3E FOR EPSILON CHAIN/CD3G FOR GAMMA CHAIN; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-11A KEYWDS BETA-SHEET, C2-SET IMMUNOGLOBULIN SUPERFAMILY, H-BONDED G STRAND KEYWDS 2 PAIR, SINGLE-CHAIN, IMMUNE SYSTEM EXPDTA SOLUTION NMR NUMMDL 18 AUTHOR Z.-Y.J.SUN,K.S.KIM,G.WAGNER,E.L.REINHERZ REVDAT 4 23-FEB-22 1JBJ 1 REMARK REVDAT 3 24-FEB-09 1JBJ 1 VERSN REVDAT 2 01-APR-03 1JBJ 1 JRNL REVDAT 1 05-DEC-01 1JBJ 0 JRNL AUTH Z.J.SUN,K.S.KIM,G.WAGNER,E.L.REINHERZ JRNL TITL MECHANISMS CONTRIBUTING TO T CELL RECEPTOR SIGNALING AND JRNL TITL 2 ASSEMBLY REVEALED BY THE SOLUTION STRUCTURE OF AN ECTODOMAIN JRNL TITL 3 FRAGMENT OF THE CD3 EPSILON GAMMA HETERODIMER. JRNL REF CELL(CAMBRIDGE,MASS.) V. 105 913 2001 JRNL REFN ISSN 0092-8674 JRNL PMID 11439187 JRNL DOI 10.1016/S0092-8674(01)00395-6 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH K.S.KIM,Z.Y.SUN,G.WAGNER,E.L.REINHERZ REMARK 1 TITL HETERODIMERIC CD3EPSILONGAMMA EXTRACELLULAR DOMAIN REMARK 1 TITL 2 FRAGMENTS: PRODUCTION, PURIFICATION AND STRUCTURAL ANALYSIS REMARK 1 REF J.MOL.BIOL. V. 302 899 2000 REMARK 1 REFN ISSN 0022-2836 REMARK 1 DOI 10.1006/JMBI.2000.4098 REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PROSA 3.7, X-PLOR 3.1 REMARK 3 AUTHORS : GUNTERT (PROSA), BRUNGER (X-PLOR) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: CALCULATED USING 1623 NOE RESTRAINTS, REMARK 3 105 H-BOND RESTRAINTS, AND 194 DIHEDRAL ANGLE RESTRINTS REMARK 4 REMARK 4 1JBJ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUN-01. REMARK 100 THE DEPOSITION ID IS D_1000013588. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 298; 298; 298; 298; 298; 298 REMARK 210 PH : 4.5; 4.5; 4.5; 4.5; 4.5; 4.5 REMARK 210 IONIC STRENGTH : 5 MM SODIUM ACETATE; 5 MM SODIUM REMARK 210 ACETATE; 5 MM SODIUM ACETATE; 5 REMARK 210 MM SODIUM ACETATE; 5 MM SODIUM REMARK 210 ACETATE; 5 MM SODIUM ACETATE REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT; REMARK 210 AMBIENT; AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : U-15N,13C,2D; 5 MM SODIUM REMARK 210 ACETATE, PH 4.5; UNLABELED; 5 MM REMARK 210 SODIUM ACETATE, PH 4.5; U-15N, REMARK 210 13C, U-70% 2D; 5 MM SODIUM REMARK 210 ACETATE, PH 4.5; U-15N; 5 MM REMARK 210 SODIUM ACETATE, PH 4.5; U-13C; 5 REMARK 210 MM SODIUM ACETATE, PH 4.5; U-10% REMARK 210 13C; 5 MM SODIUM ACETATE, PH 4.5 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : REMARK 210 HNCA,HN(CO)CA,HN(CA)CB,HN(COCA)CB,HNCO,HN(CA)CO; 2D-NOESY,2D- REMARK 210 TOCSY; H(CCO)NH; 15N-NOESYHSQC,TOCSY; 13C-NOESYHSQC,TOCSY; 13C- REMARK 210 HSQC; 15N-HSQC,HNHA,HNHB REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 750 MHZ REMARK 210 SPECTROMETER MODEL : AVANCE; INOVA REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : XEASY 1.3.13, DYANA 1.4, X-PLOR REMARK 210 3.1 REMARK 210 METHOD USED : SIMULATED ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : 20 REMARK 210 CONFORMERS, NUMBER SUBMITTED : 18 REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST REMARK 210 RESTRAINT VIOLATIONS REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 12 REMARK 210 REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR REMARK 210 SPECTROSCOPY. STRUCTURES ARE SUPERIMPOSED BASED ON BACKBONE REMARK 210 ATOMS FROM RESIDUES 7 TO 79 AND 113 TO 184. 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 DBREF 1JBJ A 1 79 UNP P22646 CD3E_MOUSE 22 100 DBREF 1JBJ A 80 105 GB 1531627 AAB09468 134 159 DBREF 1JBJ A 106 186 UNP P11942 CD3G_MOUSE 23 103 SEQRES 1 A 186 ASP ASP ALA GLU ASN ILE GLU TYR LYS VAL SER ILE SER SEQRES 2 A 186 GLY THR SER VAL GLU LEU THR CYS PRO LEU ASP SER ASP SEQRES 3 A 186 GLU ASN LEU LYS TRP GLU LYS ASN GLY GLN GLU LEU PRO SEQRES 4 A 186 GLN LYS HIS ASP LYS HIS LEU VAL LEU GLN ASP PHE SER SEQRES 5 A 186 GLU VAL GLU ASP SER GLY TYR TYR VAL CYS TYR THR PRO SEQRES 6 A 186 ALA SER ASN LYS ASN THR TYR LEU TYR LEU LYS ALA ARG SEQRES 7 A 186 VAL GLY SER ALA ASP ASP ALA LYS LYS ASP ALA ALA LYS SEQRES 8 A 186 LYS ASP ASP ALA LYS LYS ASP ASP ALA LYS LYS ASP GLY SEQRES 9 A 186 SER GLN THR ASN LYS ALA LYS ASN LEU VAL GLN VAL ASP SEQRES 10 A 186 GLY SER ARG GLY ASP GLY SER VAL LEU LEU THR CYS GLY SEQRES 11 A 186 LEU THR ASP LYS THR ILE LYS TRP LEU LYS ASP GLY SER SEQRES 12 A 186 ILE ILE SER PRO LEU ASN ALA THR LYS ASN THR TRP ASN SEQRES 13 A 186 LEU GLY ASN ASN ALA LYS ASP PRO ARG GLY THR TYR GLN SEQRES 14 A 186 CYS GLN GLY ALA LYS GLU THR SER ASN PRO LEU GLN VAL SEQRES 15 A 186 TYR TYR ARG MET SHEET 1 A 3 LYS A 9 SER A 13 0 SHEET 2 A 3 SER A 16 THR A 20 -1 O SER A 16 N SER A 13 SHEET 3 A 3 HIS A 45 GLN A 49 -1 O LEU A 46 N LEU A 19 SHEET 1 B 8 GLN A 36 LEU A 38 0 SHEET 2 B 8 LYS A 30 LYS A 33 -1 N TRP A 31 O LEU A 38 SHEET 3 B 8 GLY A 58 TYR A 63 -1 O VAL A 61 N GLU A 32 SHEET 4 B 8 LEU A 73 LEU A 75 -1 N LEU A 73 O TYR A 60 SHEET 5 B 8 THR A 176 TYR A 183 1 O GLN A 181 N TYR A 74 SHEET 6 B 8 ARG A 165 GLY A 172 -1 O GLY A 166 N VAL A 182 SHEET 7 B 8 ILE A 136 LYS A 140 -1 O LYS A 137 N GLN A 171 SHEET 8 B 8 SER A 143 ILE A 144 -1 O SER A 143 N LYS A 140 SHEET 1 C 3 GLN A 115 VAL A 116 0 SHEET 2 C 3 SER A 124 THR A 128 -1 N THR A 128 O GLN A 115 SHEET 3 C 3 ASN A 156 ASN A 159 -1 N LEU A 157 O VAL A 125 SSBOND 1 CYS A 21 CYS A 62 1555 1555 2.03 SSBOND 2 CYS A 129 CYS A 170 1555 1555 2.03 CRYST1 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