Header list of 1ddf.pdb file
Complete list - 16 20 Bytes
HEADER DEATH DOMAIN 08-NOV-96 1DDF
TITLE FAS DEATH DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FAS;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 ORGAN: FETAL LIVER;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: HMS174 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET30B;
SOURCE 10 OTHER_DETAILS: METHIONINE RESIDUE ADDED TO N-TERMINUS, AN LEHHHHHH
SOURCE 11 HISTIDINE TAG WAS ADDED AT THE C-TERMINUS FOR EASE OF PURIFICATION
KEYWDS DEATH DOMAIN, APOPTOSIS, RECEPTOR, GLYCOPROTEIN, TRANSMEMBRANE
EXPDTA SOLUTION NMR
AUTHOR B.HUANG,M.EBERSTADT,E.OLEJNICZAK,R.P.MEADOWS,S.FESIK
REVDAT 3 16-FEB-22 1DDF 1 REMARK
REVDAT 2 24-FEB-09 1DDF 1 VERSN
REVDAT 1 12-NOV-97 1DDF 0
JRNL AUTH B.HUANG,M.EBERSTADT,E.T.OLEJNICZAK,R.P.MEADOWS,S.W.FESIK
JRNL TITL NMR STRUCTURE AND MUTAGENESIS OF THE FAS (APO-1/CD95) DEATH
JRNL TITL 2 DOMAIN.
JRNL REF NATURE V. 384 638 1996
JRNL REFN ISSN 0028-0836
JRNL PMID 8967952
JRNL DOI 10.1038/384638A0
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1DDF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000172742.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : 4.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
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 : 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: 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 GLU A 202 -17.59 88.65
REMARK 500 THR A 203 169.12 57.57
REMARK 500 ILE A 206 161.24 66.09
REMARK 500 ASN A 207 11.24 -142.82
REMARK 500 LEU A 208 51.84 -90.50
REMARK 500 ASP A 210 41.62 -103.86
REMARK 500 LEU A 213 108.39 -57.30
REMARK 500 SER A 214 -35.34 173.80
REMARK 500 PHE A 232 -71.70 -68.69
REMARK 500 LYS A 235 39.21 -95.95
REMARK 500 ASN A 236 26.05 -143.59
REMARK 500 ASN A 239 125.77 65.90
REMARK 500 LYS A 247 -60.37 -90.25
REMARK 500 ASN A 250 69.95 -156.35
REMARK 500 ALA A 255 -78.98 -80.89
REMARK 500 HIS A 269 -88.57 -88.46
REMARK 500 LYS A 271 -80.17 -170.55
REMARK 500 ALA A 285 30.85 -97.81
REMARK 500 LEU A 287 -65.71 -136.92
REMARK 500 THR A 289 -44.24 -139.02
REMARK 500 ASP A 305 30.51 -98.54
REMARK 500 SER A 306 -40.58 -173.20
REMARK 500 ASN A 308 -160.04 -127.97
REMARK 500 SER A 309 55.35 -173.87
REMARK 500 ASN A 310 59.38 -149.95
REMARK 500 ILE A 315 -46.39 -149.00
REMARK 500 GLN A 316 -91.55 -179.20
REMARK 500 SER A 317 -57.77 176.99
REMARK 500 LEU A 318 -143.35 -65.27
REMARK 500 LEU A 320 -62.03 174.38
REMARK 500 GLU A 321 -80.73 -61.95
REMARK 500 HIS A 323 -161.23 -172.64
REMARK 500 HIS A 325 -43.69 -162.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 234 0.17 SIDE CHAIN
REMARK 500 ARG A 263 0.27 SIDE CHAIN
REMARK 500 ARG A 312 0.27 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1DDF A 202 319 UNP P25445 TNR6_HUMAN 218 335
SEQRES 1 A 127 MET GLU THR VAL ALA ILE ASN LEU SER ASP VAL ASP LEU
SEQRES 2 A 127 SER LYS TYR ILE THR THR ILE ALA GLY VAL MET THR LEU
SEQRES 3 A 127 SER GLN VAL LYS GLY PHE VAL ARG LYS ASN GLY VAL ASN
SEQRES 4 A 127 GLU ALA LYS ILE ASP GLU ILE LYS ASN ASP ASN VAL GLN
SEQRES 5 A 127 ASP THR ALA GLU GLN LYS VAL GLN LEU LEU ARG ASN TRP
SEQRES 6 A 127 HIS GLN LEU HIS GLY LYS LYS GLU ALA TYR ASP THR LEU
SEQRES 7 A 127 ILE LYS ASP LEU LYS LYS ALA ASN LEU CYS THR LEU ALA
SEQRES 8 A 127 GLU LYS ILE GLN THR ILE ILE LEU LYS ASP ILE THR SER
SEQRES 9 A 127 ASP SER GLU ASN SER ASN PHE ARG ASN GLU ILE GLN SER
SEQRES 10 A 127 LEU VAL LEU GLU HIS HIS HIS HIS HIS HIS
HELIX 1 1 TYR A 216 VAL A 223 1 8
HELIX 2 2 LEU A 226 ASN A 236 1 11
HELIX 3 3 GLU A 240 ASN A 250 1 11
HELIX 4 4 GLN A 257 LEU A 268 1 12
HELIX 5 5 ALA A 274 LYS A 284 1 11
HELIX 6 6 LEU A 290 ILE A 302 1 13
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 - 16 20 Bytes