Header list of 1n6v.pdb file
Complete list - 23 20 Bytes
HEADER IMMUNE SYSTEM 12-NOV-02 1N6V TITLE AVERAGE STRUCTURE OF THE INTERFERON-BINDING ECTODOMAIN OF THE HUMAN TITLE 2 TYPE I INTERFERON RECEPTOR COMPND MOL_ID: 1; COMPND 2 MOLECULE: INTERFERON-ALPHA/BETA RECEPTOR BETA CHAIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: IFNAR2-EC, IFN-ALPHA-REC, TYPE I INTERFERON RECEPTOR, IFN-R, COMPND 5 INTERFERON ALPHA/BETA RECEPTOR- 2; COMPND 6 ENGINEERED: 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; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: TG1; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID KEYWDS IMMUNOGLOBULIN FOLD, FIBRONECTIN FOLD, TWO-DOMAIN STRUCTURE, IMMUNE KEYWDS 2 SYSTEM EXPDTA SOLUTION NMR MDLTYP MINIMIZED AVERAGE AUTHOR J.H.CHILL,S.R.QUADT,R.LEVY,G.SCHREIBER,J.ANGLISTER REVDAT 3 23-FEB-22 1N6V 1 REMARK SEQADV REVDAT 2 24-FEB-09 1N6V 1 VERSN REVDAT 1 15-JUL-03 1N6V 0 JRNL AUTH J.H.CHILL,S.R.QUADT,R.LEVY,G.SCHREIBER,J.ANGLISTER JRNL TITL THE HUMAN TYPE I INTERFERON RECEPTOR. NMR STRUCTURE REVEALS JRNL TITL 2 THE MOLECULAR BASIS OF LIGAND BINDING. JRNL REF STRUCTURE V. 11 791 2003 JRNL REFN ISSN 0969-2126 JRNL PMID 12842042 JRNL DOI 10.1016/S0969-2126(03)00120-5 REMARK 1 REMARK 1 REFERENCE 1 REMARK 1 AUTH J.H.CHILL,R.NIVASCH,R.LEVY,S.ALBECK,G.SCHREIBER,J.ANGLISTER REMARK 1 TITL THE HUMAN INTERFERON RECEPTOR: NMR-BASED MODELING, MAPPING REMARK 1 TITL 2 OF THE IFN-ALPHA2 BINDING SITE, AND OBSERVED LIGAND-INDUCED REMARK 1 TITL 3 TIGHTENING REMARK 1 REF BIOCHEMISTRY V. 41 3575 2002 REMARK 1 REFN ISSN 0006-2960 REMARK 1 DOI 10.1021/BI011778F REMARK 2 REMARK 2 RESOLUTION. NOT APPLICABLE. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : XWINNMR 3.0, CNS 1.1 REMARK 3 AUTHORS : NEIDIG (XWINNMR), BRUNGER (CNS) REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURE BASED UPON 1947 NOE-DERIVED REMARK 3 DISTANCE RESTRAINTS (1066 OF WHICH LONG RANGE), 172 DIHEDRAL REMARK 3 ANGLE RESTRAINTS (OF WHICH 88 EXPERIMENTAL AND 84 TALOS-DERIVED), REMARK 3 138 HYDROGEN-BOND RESTRAINTS AND 109 RESIDUAL DIPOLAR COUPLING REMARK 3 RESTRAINTS REMARK 4 REMARK 4 1N6V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-NOV-02. REMARK 100 THE DEPOSITION ID IS D_1000017592. REMARK 210 REMARK 210 EXPERIMENTAL DETAILS REMARK 210 EXPERIMENT TYPE : NMR REMARK 210 TEMPERATURE (KELVIN) : 308; 308; 305 REMARK 210 PH : 8; 8; 8 REMARK 210 IONIC STRENGTH : 20MM TRIS BUFFER; 20MM TRIS REMARK 210 BUFFER; 20MM TRIS BUFFER REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT REMARK 210 SAMPLE CONTENTS : 0.4MM U-15N IFNAR2-EC; 20MM D REMARK 210 -TRIS PH 8, 0.02% NAN3; 0.35MM U- REMARK 210 13C,15N IFNAR2-EC; 20MM D-TRIS REMARK 210 PH 8, 0.02% NAN3; 0.3MM U-13C, REMARK 210 15N IFNAR2-EC; 20MM D-TRIS PH 8, REMARK 210 0.02% NAN3 REMARK 210 REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; HNHA; REMARK 210 HNCA; HNCACB; CBCACONH; 3D_13C- REMARK 210 SEPARATED_NOESY REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ; 500 MHZ REMARK 210 SPECTROMETER MODEL : DRX; DMX REMARK 210 SPECTROMETER MANUFACTURER : BRUKER REMARK 210 REMARK 210 STRUCTURE DETERMINATION. REMARK 210 SOFTWARE USED : CNS 1.1, NMRPIPE 2.1 REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED REMARK 210 ANNEALING REMARK 210 REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1 REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL REMARK 210 REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1 REMARK 210 REMARK 210 REMARK: ALL EXPERIMENTS CONDUCTED IN SHIGEMI TUBES EQUIPPED WITH REMARK 210 INSERT 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: 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 ASP A 3 -169.25 45.55 REMARK 500 ASP A 6 95.65 -69.85 REMARK 500 TYR A 7 73.55 -69.89 REMARK 500 GLU A 10 63.83 174.19 REMARK 500 CYS A 12 34.60 38.40 REMARK 500 HIS A 32 -70.34 -120.31 REMARK 500 SER A 33 -67.99 -100.75 REMARK 500 ASP A 51 55.51 -111.70 REMARK 500 ASN A 57 -9.29 79.95 REMARK 500 ASN A 60 75.49 13.08 REMARK 500 LEU A 68 88.74 -171.49 REMARK 500 TYR A 79 88.47 -59.51 REMARK 500 SER A 94 94.73 -160.52 REMARK 500 ALA A 102 -33.11 -39.78 REMARK 500 MET A 105 88.43 28.93 REMARK 500 GLU A 108 -59.03 -158.53 REMARK 500 PRO A 110 153.50 -33.66 REMARK 500 ASP A 138 34.48 -156.83 REMARK 500 GLN A 146 68.29 -110.00 REMARK 500 LYS A 159 67.20 -69.81 REMARK 500 MET A 162 41.48 -93.17 REMARK 500 ASP A 171 -165.70 -110.69 REMARK 500 PRO A 175 156.17 -38.70 REMARK 500 ASN A 176 67.96 64.67 REMARK 500 SER A 188 39.76 177.79 REMARK 500 ALA A 192 42.71 -95.21 REMARK 500 PRO A 197 107.63 -50.21 REMARK 500 LEU A 198 174.84 -49.87 REMARK 500 PRO A 204 103.23 -55.44 REMARK 500 GLN A 207 38.02 -92.27 REMARK 500 GLU A 208 -159.65 -74.65 REMARK 500 SER A 209 -166.72 -56.92 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1N6U RELATED DB: PDB DBREF 1N6V A 1 210 UNP P48551 INAR2_HUMAN 28 237 SEQADV 1N6V PHE A 211 UNP P48551 CLONING ARTIFACT SEQADV 1N6V SER A 212 UNP P48551 CLONING ARTIFACT SEQRES 1 A 212 SER TYR ASP SER PRO ASP TYR THR ASP GLU SER CYS THR SEQRES 2 A 212 PHE LYS ILE SER LEU ARG ASN PHE ARG SER ILE LEU SER SEQRES 3 A 212 TRP GLU LEU LYS ASN HIS SER ILE VAL PRO THR HIS TYR SEQRES 4 A 212 THR LEU LEU TYR THR ILE MET SER LYS PRO GLU ASP LEU SEQRES 5 A 212 LYS VAL VAL LYS ASN CYS ALA ASN THR THR ARG SER PHE SEQRES 6 A 212 CYS ASP LEU THR ASP GLU TRP ARG SER THR HIS GLU ALA SEQRES 7 A 212 TYR VAL THR VAL LEU GLU GLY PHE SER GLY ASN THR THR SEQRES 8 A 212 LEU PHE SER CYS SER HIS ASN PHE TRP LEU ALA ILE ASP SEQRES 9 A 212 MET SER PHE GLU PRO PRO GLU PHE GLU ILE VAL GLY PHE SEQRES 10 A 212 THR ASN HIS ILE ASN VAL MET VAL LYS PHE PRO SER ILE SEQRES 11 A 212 VAL GLU GLU GLU LEU GLN PHE ASP LEU SER LEU VAL ILE SEQRES 12 A 212 GLU GLU GLN SER GLU GLY ILE VAL LYS LYS HIS LYS PRO SEQRES 13 A 212 GLU ILE LYS GLY ASN MET SER GLY ASN PHE THR TYR ILE SEQRES 14 A 212 ILE ASP LYS LEU ILE PRO ASN THR ASN TYR CYS VAL SER SEQRES 15 A 212 VAL TYR LEU GLU HIS SER ASP GLU GLN ALA VAL ILE LYS SEQRES 16 A 212 SER PRO LEU LYS CYS THR LEU LEU PRO PRO GLY GLN GLU SEQRES 17 A 212 SER GLU PHE SER HELIX 1 1 LEU A 101 MET A 105 1 5 HELIX 2 2 VAL A 131 LEU A 135 5 5 SHEET 1 A 3 THR A 13 LEU A 18 0 SHEET 2 A 3 SER A 23 GLU A 28 -1 O SER A 26 N LYS A 15 SHEET 3 A 3 CYS A 66 LEU A 68 -1 O LEU A 68 N SER A 23 SHEET 1 B 4 LYS A 48 VAL A 54 0 SHEET 2 B 4 TYR A 39 ILE A 45 -1 N ILE A 45 O LYS A 48 SHEET 3 B 4 ALA A 78 SER A 87 -1 O VAL A 82 N LEU A 42 SHEET 4 B 4 THR A 90 THR A 91 -1 O THR A 90 N SER A 87 SHEET 1 C 4 LYS A 48 VAL A 54 0 SHEET 2 C 4 TYR A 39 ILE A 45 -1 N ILE A 45 O LYS A 48 SHEET 3 C 4 ALA A 78 SER A 87 -1 O VAL A 82 N LEU A 42 SHEET 4 C 4 CYS A 95 TRP A 100 -1 O HIS A 97 N THR A 81 SHEET 1 D 2 GLU A 111 PHE A 117 0 SHEET 2 D 2 HIS A 120 LYS A 126 -1 O MET A 124 N GLU A 113 SHEET 1 E 4 ILE A 150 HIS A 154 0 SHEET 2 E 4 SER A 140 SER A 147 -1 N SER A 147 O ILE A 150 SHEET 3 E 4 TYR A 179 GLU A 186 -1 O TYR A 184 N VAL A 142 SHEET 4 E 4 LYS A 199 THR A 201 -1 O LYS A 199 N VAL A 181 SSBOND 1 CYS A 12 CYS A 95 1555 1555 2.03 SSBOND 2 CYS A 58 CYS A 66 1555 1555 2.03 SSBOND 3 CYS A 180 CYS A 200 1555 1555 2.04 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
Complete list - 23 20 Bytes