Header list of 1fad.pdb file
Complete list - b 23 2 Bytes
HEADER APOPTOSIS 23-MAR-99 1FAD
TITLE DEATH DOMAIN OF FAS-ASSOCIATED DEATH DOMAIN PROTEIN, RESIDUES 89-183
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN (FADD PROTEIN);
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DEATH DOMAIN (RESIDUES 89-183);
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 OTHER_DETAILS: N-TERMINAL EXTENSION OF GLY-SER-HIS-MET FROM CLONING
COMPND 8 ARTIFACT. COORDINATES ARE NOT SHOWN FOR ARTIFACT.
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS APOPTOSIS, FADD, DEATH DOMAIN
EXPDTA SOLUTION NMR
NUMMDL 21
AUTHOR E.-J.JEONG,S.BANG,T.H.LEE,Y.-I.PARK,W.-S.SIM,K.-S.KIM
REVDAT 4 23-FEB-22 1FAD 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1FAD 1 VERSN
REVDAT 2 01-APR-03 1FAD 1 JRNL
REVDAT 1 06-JUL-99 1FAD 0
JRNL AUTH E.J.JEONG,S.BANG,T.H.LEE,Y.I.PARK,W.S.SIM,K.S.KIM
JRNL TITL THE SOLUTION STRUCTURE OF FADD DEATH DOMAIN. STRUCTURAL
JRNL TITL 2 BASIS OF DEATH DOMAIN INTERACTIONS OF FAS AND FADD.
JRNL REF J.BIOL.CHEM. V. 274 16337 1999
JRNL REFN ISSN 0021-9258
JRNL PMID 10347191
JRNL DOI 10.1074/JBC.274.23.16337
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH J.ZHANG,A.WINOTO
REMARK 1 TITL A MOUSE FAS-ASSOCIATED PROTEIN WITH HOMOLOGY TO THE HUMAN
REMARK 1 TITL 2 MORT1/FADD IS ESSENTIAL FOR FAS-INDUCED APOPTOSIS
REMARK 1 REF MOL.CELL.BIOL. V. 16 2756 1996
REMARK 1 REFN ISSN 0270-7306
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1FAD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAR-99.
REMARK 100 THE DEPOSITION ID IS D_1000000704.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 4.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 2 MM
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D-15N-HSQC-NOESY; 3D-13C; 15N
REMARK 210 -EDITED NOESY; 13C-HCCH-TOCSY;
REMARK 210 3D-15N-HSQC-TOCSY; 3D HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS600; INOVA500
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : DISTANCE GEOMETRY AND SIMMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 21
REMARK 210
REMARK 210 REMARK: DISTANCE CONSTRAINTS ARE DERIVED FROM THE 3D-13C, 15N
REMARK 210 -EDITED NOESY. J-COUPLING CONSTANTS FROM HNHA AND 13C CHEMICAL
REMARK 210 SHIFTS WERE USED AS CONTRAINTS. DURING THE REFINEMENT, DATABASE
REMARK 210 POTENTIAL WAS USED.
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 MODELS 1-21
REMARK 465 RES C SSSEQI
REMARK 465 GLY A 85
REMARK 465 SER A 86
REMARK 465 HIS A 87
REMARK 465 MET A 88
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 ALA A 90 -178.08 -66.52
REMARK 500 1 ASN A 107 -72.64 -93.42
REMARK 500 1 ARG A 135 18.03 -150.20
REMARK 500 1 LYS A 153 -104.15 54.89
REMARK 500 1 ARG A 169 -11.45 -177.46
REMARK 500 1 GLU A 182 -59.80 64.91
REMARK 500 2 ALA A 90 -176.86 -65.11
REMARK 500 2 VAL A 108 46.24 -162.88
REMARK 500 2 ARG A 135 17.90 -151.48
REMARK 500 2 LYS A 153 -72.96 -88.98
REMARK 500 2 ARG A 169 -21.18 -179.69
REMARK 500 3 ALA A 90 -178.70 -66.97
REMARK 500 3 ASN A 107 -77.63 -92.20
REMARK 500 3 ARG A 135 11.32 -148.70
REMARK 500 3 LYS A 153 -80.89 -91.06
REMARK 500 3 LEU A 165 -70.77 -51.40
REMARK 500 3 ARG A 169 -20.31 -175.70
REMARK 500 4 ALA A 90 -177.99 -68.34
REMARK 500 4 VAL A 108 70.19 -166.99
REMARK 500 4 LYS A 153 -74.47 -88.08
REMARK 500 4 ARG A 169 -13.55 -178.86
REMARK 500 5 ALA A 90 -179.27 -66.24
REMARK 500 5 VAL A 108 39.60 -163.00
REMARK 500 5 ARG A 135 13.28 -145.99
REMARK 500 5 LYS A 153 -79.09 -89.93
REMARK 500 5 ARG A 169 -10.44 179.99
REMARK 500 6 ALA A 90 -176.73 -69.30
REMARK 500 6 VAL A 108 33.83 -160.42
REMARK 500 6 ARG A 135 14.29 -151.10
REMARK 500 6 LYS A 153 -80.11 -89.98
REMARK 500 6 ARG A 169 -9.61 -179.68
REMARK 500 7 ALA A 90 -178.78 -65.87
REMARK 500 7 VAL A 108 36.95 -160.77
REMARK 500 7 LYS A 153 -78.78 -90.10
REMARK 500 7 ARG A 169 12.84 174.52
REMARK 500 7 LEU A 170 46.19 -92.65
REMARK 500 8 ALA A 90 -179.71 -65.21
REMARK 500 8 VAL A 108 54.35 -162.34
REMARK 500 8 TYR A 133 78.62 -117.50
REMARK 500 8 LYS A 153 -79.58 -90.02
REMARK 500 8 ARG A 169 -15.00 -177.61
REMARK 500 8 LEU A 170 47.97 -79.89
REMARK 500 8 GLU A 182 -58.55 66.36
REMARK 500 9 ALA A 90 -179.25 -64.76
REMARK 500 9 VAL A 108 45.70 -159.45
REMARK 500 9 ARG A 135 76.21 -151.02
REMARK 500 9 SER A 138 -71.07 -59.28
REMARK 500 9 LYS A 153 -73.69 -87.43
REMARK 500 9 ARG A 169 -21.53 -178.70
REMARK 500 10 ALA A 90 -178.73 -65.67
REMARK 500
REMARK 500 THIS ENTRY HAS 115 RAMACHANDRAN OUTLIERS.
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 1 ARG A 110 0.31 SIDE CHAIN
REMARK 500 1 ARG A 114 0.27 SIDE CHAIN
REMARK 500 1 ARG A 117 0.30 SIDE CHAIN
REMARK 500 1 ARG A 135 0.20 SIDE CHAIN
REMARK 500 1 ARG A 140 0.23 SIDE CHAIN
REMARK 500 1 ARG A 142 0.32 SIDE CHAIN
REMARK 500 1 ARG A 166 0.25 SIDE CHAIN
REMARK 500 1 ARG A 169 0.32 SIDE CHAIN
REMARK 500 2 ARG A 110 0.29 SIDE CHAIN
REMARK 500 2 ARG A 114 0.28 SIDE CHAIN
REMARK 500 2 ARG A 117 0.28 SIDE CHAIN
REMARK 500 2 ARG A 135 0.20 SIDE CHAIN
REMARK 500 2 ARG A 140 0.28 SIDE CHAIN
REMARK 500 2 ARG A 142 0.31 SIDE CHAIN
REMARK 500 2 ARG A 166 0.30 SIDE CHAIN
REMARK 500 2 ARG A 169 0.26 SIDE CHAIN
REMARK 500 3 ARG A 110 0.32 SIDE CHAIN
REMARK 500 3 ARG A 114 0.26 SIDE CHAIN
REMARK 500 3 ARG A 117 0.32 SIDE CHAIN
REMARK 500 3 ARG A 135 0.31 SIDE CHAIN
REMARK 500 3 ARG A 140 0.24 SIDE CHAIN
REMARK 500 3 ARG A 142 0.28 SIDE CHAIN
REMARK 500 3 ARG A 166 0.27 SIDE CHAIN
REMARK 500 3 ARG A 169 0.32 SIDE CHAIN
REMARK 500 4 ARG A 110 0.26 SIDE CHAIN
REMARK 500 4 ARG A 114 0.20 SIDE CHAIN
REMARK 500 4 ARG A 117 0.24 SIDE CHAIN
REMARK 500 4 ARG A 135 0.32 SIDE CHAIN
REMARK 500 4 ARG A 140 0.31 SIDE CHAIN
REMARK 500 4 ARG A 142 0.22 SIDE CHAIN
REMARK 500 4 ARG A 166 0.25 SIDE CHAIN
REMARK 500 4 ARG A 169 0.28 SIDE CHAIN
REMARK 500 5 ARG A 110 0.26 SIDE CHAIN
REMARK 500 5 ARG A 114 0.31 SIDE CHAIN
REMARK 500 5 ARG A 117 0.22 SIDE CHAIN
REMARK 500 5 ARG A 135 0.25 SIDE CHAIN
REMARK 500 5 ARG A 140 0.31 SIDE CHAIN
REMARK 500 5 ARG A 142 0.31 SIDE CHAIN
REMARK 500 5 ARG A 166 0.22 SIDE CHAIN
REMARK 500 5 ARG A 169 0.26 SIDE CHAIN
REMARK 500 6 ARG A 110 0.27 SIDE CHAIN
REMARK 500 6 ARG A 114 0.29 SIDE CHAIN
REMARK 500 6 ARG A 117 0.30 SIDE CHAIN
REMARK 500 6 ARG A 135 0.30 SIDE CHAIN
REMARK 500 6 ARG A 140 0.25 SIDE CHAIN
REMARK 500 6 ARG A 142 0.24 SIDE CHAIN
REMARK 500 6 ARG A 166 0.31 SIDE CHAIN
REMARK 500 6 ARG A 169 0.30 SIDE CHAIN
REMARK 500 7 ARG A 110 0.26 SIDE CHAIN
REMARK 500 7 ARG A 114 0.32 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 168 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1FAD A 89 183 UNP Q61160 FADD_MOUSE 89 183
SEQADV 1FAD TYR A 96 UNP Q61160 ASP 96 ENGINEERED MUTATION
SEQADV 1FAD GLY A 85 UNP Q61160 CLONING ARTIFACT
SEQADV 1FAD SER A 86 UNP Q61160 CLONING ARTIFACT
SEQADV 1FAD HIS A 87 UNP Q61160 CLONING ARTIFACT
SEQADV 1FAD MET A 88 UNP Q61160 CLONING ARTIFACT
SEQRES 1 A 99 GLY SER HIS MET ALA ALA PRO PRO GLY GLU ALA TYR LEU
SEQRES 2 A 99 GLN VAL ALA PHE ASP ILE VAL CYS ASP ASN VAL GLY ARG
SEQRES 3 A 99 ASP TRP LYS ARG LEU ALA ARG GLU LEU LYS VAL SER GLU
SEQRES 4 A 99 ALA LYS MET ASP GLY ILE GLU GLU LYS TYR PRO ARG SER
SEQRES 5 A 99 LEU SER GLU ARG VAL ARG GLU SER LEU LYS VAL TRP LYS
SEQRES 6 A 99 ASN ALA GLU LYS LYS ASN ALA SER VAL ALA GLY LEU VAL
SEQRES 7 A 99 LYS ALA LEU ARG THR CYS ARG LEU ASN LEU VAL ALA ASP
SEQRES 8 A 99 LEU VAL GLU GLU ALA GLN GLU SER
HELIX 1 1 GLU A 94 LEU A 119 1 26
HELIX 2 2 GLU A 123 LYS A 132 1 10
HELIX 3 3 LEU A 137 ALA A 156 1 20
HELIX 4 4 VAL A 158 CYS A 168 1 11
HELIX 5 5 ASN A 171 GLN A 181 1 11
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 - b 23 2 Bytes