Header list of 1f2h.pdb file
Complete list - 16 20 Bytes
HEADER APOPTOSIS 24-MAY-00 1F2H
TITLE SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF THE TNFR1 ASSOCIATED
TITLE 2 PROTEIN, TRADD.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TUMOR NECROSIS FACTOR RECEPTOR TYPE 1 ASSOCIATED DEATH
COMPND 3 DOMAIN PROTEIN;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: N-TERMINAL DOMAIN;
COMPND 6 SYNONYM: TRADD, TNFR1-ASSOCIATED DEATH DOMAIN PROTEIN;
COMPND 7 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_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PRSETB
KEYWDS TNFR-1 ASSOCIATED PROTEIN, APOPTOSIS
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR D.TSAO,T.MCDONAUGH,K.MALAKIAN,G.-Y.XU,J.-B.TELLIEZ,H.HSU,L.-L.LIN
REVDAT 5 16-FEB-22 1F2H 1 REMARK
REVDAT 4 24-FEB-09 1F2H 1 VERSN
REVDAT 3 01-APR-03 1F2H 1 JRNL
REVDAT 2 01-AUG-01 1F2H 1 REMARK
REVDAT 1 30-MAY-01 1F2H 0
JRNL AUTH D.H.TSAO,T.MCDONAGH,J.B.TELLIEZ,S.HSU,K.MALAKIAN,G.Y.XU,
JRNL AUTH 2 L.L.LIN
JRNL TITL SOLUTION STRUCTURE OF N-TRADD AND CHARACTERIZATION OF THE
JRNL TITL 2 INTERACTION OF N-TRADD AND C-TRAF2, A KEY STEP IN THE TNFR1
JRNL TITL 3 SIGNALING PATHWAY.
JRNL REF MOL.CELL V. 5 1051 2000
JRNL REFN ISSN 1097-2765
JRNL PMID 10911999
JRNL DOI 10.1016/S1097-2765(00)80270-1
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER ET AL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES DETERMINED FROM 2402
REMARK 3 RESTRAINTS (1883 NOE RESTRAINTS, 159 DIHEDRAL, 100 DISTANCE
REMARK 3 RESTRAINTS FROM HYDROGEN BONDS AND 240 ALPHA AND BETA 13C
REMARK 3 CHEMICAL SHIFTS).
REMARK 4
REMARK 4 1F2H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUN-00.
REMARK 100 THE DEPOSITION ID IS D_1000011162.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298; 298
REMARK 210 PH : 6.6; 6.6; 6.6
REMARK 210 IONIC STRENGTH : 200MM NACL; 200MM NACL; 200MM
REMARK 210 NACL
REMARK 210 PRESSURE : 1 ATM; 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 1.0 MM 15N N-TRADD; 1.1 MM
REMARK 210 15N/13C N-TRADD; 0.8 MM 15N/13C
REMARK 210 N-TRADD
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNHA; HNCACB;
REMARK 210 HN(CO)CACB; C(CO)NH-TOCSY;
REMARK 210 HCCHTOCSY; HAHB(CO)NH; 15N-
REMARK 210 EDITED TOCSY-HSQC; METHYL-METHYL
REMARK 210 NOE
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY/SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 1
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOW ENERGIES AND VIOLATIONS NOT
REMARK 210 LARGER THAN 0.3A FOR NOES AND 5
REMARK 210 DEGREES FOR TORSIONAL RESTRAINTS
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: OTHER EXPERIMENTS USED WERE HC(CO)NH_TOCSY, 3D 13C-13C
REMARK 210 LONG RANGE CORRELATION, METHYL-METHYL NOE
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 9 65.00 39.46
REMARK 500 ASP A 68 -169.00 46.31
REMARK 500 CYS A 78 -44.02 -155.22
REMARK 500 LEU A 107 -79.34 -89.97
REMARK 500 ALA A 108 34.50 -167.32
REMARK 500 SER A 111 124.57 -178.05
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1F2H A 1 169 UNP Q15628 TRADD_HUMAN 1 169
SEQRES 1 A 169 MET ALA ALA GLY GLN ASN GLY HIS GLU GLU TRP VAL GLY
SEQRES 2 A 169 SER ALA TYR LEU PHE VAL GLU SER SER LEU ASP LYS VAL
SEQRES 3 A 169 VAL LEU SER ASP ALA TYR ALA HIS PRO GLN GLN LYS VAL
SEQRES 4 A 169 ALA VAL TYR ARG ALA LEU GLN ALA ALA LEU ALA GLU SER
SEQRES 5 A 169 GLY GLY SER PRO ASP VAL LEU GLN MET LEU LYS ILE HIS
SEQRES 6 A 169 ARG SER ASP PRO GLN LEU ILE VAL GLN LEU ARG PHE CYS
SEQRES 7 A 169 GLY ARG GLN PRO CYS GLY ARG PHE LEU ARG ALA TYR ARG
SEQRES 8 A 169 GLU GLY ALA LEU ARG ALA ALA LEU GLN ARG SER LEU ALA
SEQRES 9 A 169 ALA ALA LEU ALA GLN HIS SER VAL PRO LEU GLN LEU GLU
SEQRES 10 A 169 LEU ARG ALA GLY ALA GLU ARG LEU ASP ALA LEU LEU ALA
SEQRES 11 A 169 ASP GLU GLU ARG CYS LEU SER CYS ILE LEU ALA GLN GLN
SEQRES 12 A 169 PRO ASP ARG LEU ARG ASP GLU GLU LEU ALA GLU LEU GLU
SEQRES 13 A 169 ASP ALA LEU ARG ASN LEU LYS CYS GLY SER GLY ALA ARG
HELIX 1 1 VAL A 27 TYR A 32 1 6
HELIX 2 2 HIS A 34 GLY A 53 1 20
HELIX 3 3 GLY A 79 ALA A 108 1 30
HELIX 4 4 ARG A 124 ASP A 131 1 8
HELIX 5 5 ASP A 131 GLN A 142 1 12
HELIX 6 6 ASP A 149 LYS A 163 1 15
SHEET 1 A 4 MET A 61 SER A 67 0
SHEET 2 A 4 GLN A 70 ARG A 76 -1 N GLN A 70 O SER A 67
SHEET 3 A 4 SER A 14 GLU A 20 -1 O ALA A 15 N LEU A 75
SHEET 4 A 4 GLN A 115 ARG A 119 -1 N GLN A 115 O GLU A 20
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