Header list of 1ich.pdb file
Complete list - 27 20 Bytes
HEADER APOPTOSIS 01-APR-01 1ICH
TITLE SOLUTION STRUCTURE OF THE TUMOR NECROSIS FACTOR RECEPTOR-1 DEATH
TITLE 2 DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TUMOR NECROSIS FACTOR RECEPTOR-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DEATH DOMAIN;
COMPND 5 SYNONYM: TNF-1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: 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: BL-21 (DE) PLYS;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRSET(T7)
KEYWDS DEATH DOMAIN, APOPTOSIS
EXPDTA SOLUTION NMR
AUTHOR S.F.SUKITS,L.-L.LIN,K.MALAKIAN,R.POWERS,G.-Y.XU
REVDAT 4 27-OCT-21 1ICH 1 REMARK SEQADV
REVDAT 3 24-FEB-09 1ICH 1 VERSN
REVDAT 2 01-APR-03 1ICH 1 JRNL
REVDAT 1 01-APR-02 1ICH 0
JRNL AUTH S.F.SUKITS,L.L.LIN,S.HSU,K.MALAKIAN,R.POWERS,G.Y.XU
JRNL TITL SOLUTION STRUCTURE OF THE TUMOR NECROSIS FACTOR RECEPTOR-1
JRNL TITL 2 DEATH DOMAIN.
JRNL REF J.MOL.BIOL. V. 310 895 2001
JRNL REFN ISSN 0022-2836
JRNL PMID 11453696
JRNL DOI 10.1006/JMBI.2001.4790
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 9.8, X-PLOR 9.8
REMARK 3 AUTHORS : BADGER, J., KUMAR, R.A., YIP, P. (X-PLOR), BADGER,
REMARK 3 J., KUMAR, R.A., YIP, P. (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES WERE BASED ON A TOTAL OF
REMARK 3 1167 DISTANCE CONSTRAINTS FROM NOE AND H-BOND, 117 DIHEDRAL
REMARK 3 ANGLE CONSTRAINTS FROM 3D HNHA AND TALOS PROGRAM AND 81 PAIRS OF
REMARK 3 CA/CB CHEMICAL SHIFT CONTRAINTS.
REMARK 4
REMARK 4 1ICH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-APR-01.
REMARK 100 THE DEPOSITION ID IS D_1000013155.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 308
REMARK 210 PH : 4.0
REMARK 210 IONIC STRENGTH : 10 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM SAMPLE
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 4D_13C-
REMARK 210 SEPARATED_NOESY
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 : NMRPIPE 1.8, 2000, PIPP 4.2.2,
REMARK 210 1998
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING MOLECULAR DYNAMICS
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: THE STRUCTURE WAS DETERMININED USING 3D TRIPLE-RESONANCE
REMARK 210 EXPERIMENTS WITH THE ENHANCED-SENSITIVITY PULSE FIELD GRADIENT
REMARK 210 APPROACH.
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 RES C SSSEQI
REMARK 465 MET A 315
REMARK 465 ALA A 316
REMARK 465 HIS A 317
REMARK 465 LYS A 318
REMARK 465 PRO A 319
REMARK 465 GLN A 320
REMARK 465 SER A 321
REMARK 465 LEU A 322
REMARK 465 ASP A 323
REMARK 465 THR A 324
REMARK 465 ASP A 325
REMARK 465 ASP A 326
REMARK 465 GLY A 414
REMARK 465 PRO A 415
REMARK 465 ALA A 416
REMARK 465 ALA A 417
REMARK 465 LEU A 418
REMARK 465 PRO A 419
REMARK 465 PRO A 420
REMARK 465 ALA A 421
REMARK 465 PRO A 422
REMARK 465 SER A 423
REMARK 465 LEU A 424
REMARK 465 LEU A 425
REMARK 465 ARG A 426
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 O LEU A 396 H LEU A 401 1.54
REMARK 500 O LEU A 405 H GLU A 409 1.56
REMARK 500 O LEU A 389 H GLY A 393 1.58
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 ASN A 363 90.89 179.96
REMARK 500 ALA A 387 34.22 71.77
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 341 0.26 SIDE CHAIN
REMARK 500 ARG A 348 0.32 SIDE CHAIN
REMARK 500 ARG A 358 0.22 SIDE CHAIN
REMARK 500 ARG A 365 0.27 SIDE CHAIN
REMARK 500 ARG A 368 0.25 SIDE CHAIN
REMARK 500 ARG A 379 0.18 SIDE CHAIN
REMARK 500 ARG A 380 0.25 SIDE CHAIN
REMARK 500 ARG A 381 0.21 SIDE CHAIN
REMARK 500 ARG A 384 0.21 SIDE CHAIN
REMARK 500 ARG A 385 0.27 SIDE CHAIN
REMARK 500 ARG A 394 0.28 SIDE CHAIN
REMARK 500 ARG A 397 0.30 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1ICH A 316 426 UNP P19438 TNR1A_HUMAN 345 455
SEQADV 1ICH MET A 315 UNP P19438 INITIATING METHIONINE
SEQADV 1ICH LYS A 347 UNP P19438 ARG 376 ENGINEERED MUTATION
SEQRES 1 A 112 MET ALA HIS LYS PRO GLN SER LEU ASP THR ASP ASP PRO
SEQRES 2 A 112 ALA THR LEU TYR ALA VAL VAL GLU ASN VAL PRO PRO LEU
SEQRES 3 A 112 ARG TRP LYS GLU PHE VAL LYS ARG LEU GLY LEU SER ASP
SEQRES 4 A 112 HIS GLU ILE ASP ARG LEU GLU LEU GLN ASN GLY ARG CYS
SEQRES 5 A 112 LEU ARG GLU ALA GLN TYR SER MET LEU ALA THR TRP ARG
SEQRES 6 A 112 ARG ARG THR PRO ARG ARG GLU ALA THR LEU GLU LEU LEU
SEQRES 7 A 112 GLY ARG VAL LEU ARG ASP MET ASP LEU LEU GLY CYS LEU
SEQRES 8 A 112 GLU ASP ILE GLU GLU ALA LEU CYS GLY PRO ALA ALA LEU
SEQRES 9 A 112 PRO PRO ALA PRO SER LEU LEU ARG
HELIX 1 1 PRO A 327 VAL A 337 1 11
HELIX 2 2 ARG A 341 GLY A 350 1 10
HELIX 3 3 SER A 352 ASN A 363 1 12
HELIX 4 4 CYS A 366 THR A 382 1 17
HELIX 5 5 ALA A 387 MET A 399 1 13
HELIX 6 6 LEU A 401 CYS A 413 1 13
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
Complete list - 27 20 Bytes