Header list of 1osx.pdb file
Complete list - 23 20 Bytes
HEADER IMMUNE SYSTEM 20-MAR-03 1OSX
TITLE SOLUTION STRUCTURE OF THE EXTRACELLULAR DOMAIN OF BLYS RECEPTOR 3
TITLE 2 (BR3)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 13C;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: EXTRACELLULAR DOMAIN;
COMPND 5 SYNONYM: B CELL- ACTIVATING FACTOR RECEPTOR, BAFF RECEPTOR, BAFF-R,
COMPND 6 BLYS RECEPTOR 3;
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 GENE: TNFRSF13C OR BAFFR OR BR3;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CYSTEINE-RICH DOMAIN, EXTRACELLULAR DOMAIN, TUMOR NECROSIS FACTOR
KEYWDS 2 RECEPTOR, IMMUNE SYSTEM
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.C.GORDON,B.PAN,S.G.HYMOWITZ,J.P.YIN,R.F.KELLEY,A.G.COCHRAN,M.YAN,
AUTHOR 2 V.M.DIXIT,W.J.FAIRBROTHER,M.A.STAROVASNIK
REVDAT 3 23-FEB-22 1OSX 1 REMARK
REVDAT 2 24-FEB-09 1OSX 1 VERSN
REVDAT 1 27-MAY-03 1OSX 0
JRNL AUTH N.C.GORDON,B.PAN,S.G.HYMOWITZ,J.P.YIN,R.F.KELLEY,
JRNL AUTH 2 A.G.COCHRAN,M.YAN,V.M.DIXIT,W.J.FAIRBROTHER,M.A.STAROVASNIK
JRNL TITL BAFF/BLYS RECEPTOR 3 COMPRISES A MINIMAL TNF RECEPTOR-LIKE
JRNL TITL 2 MODULE THAT ENCODES A HIGHLY FOCUSED LIGAND-BINDING SITE
JRNL REF BIOCHEMISTRY V. 42 5977 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 12755599
JRNL DOI 10.1021/BI034017G
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.6, X-PLOR 98
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: ONLY 19 RESIDUES, INCLUDING CYS19
REMARK 3 THROUGH LEU37 ARE ORDERED IN SOLUTION, WHILE THE REST OF THE
REMARK 3 EXTRACELLULAR DOMAIN IS HIGHLY FLEXIBLE (BASED ON 1H-15N
REMARK 3 HETERONUCLEAR NOE ANALYSIS). FURTHERMORE, THE BAFF-BINDING
REMARK 3 DOMAIN OF BR3 WAS FOUND TO RESIDE WITHIN A FRAGMENT CONSISTING
REMARK 3 OF THR17-ARG42 DENOTED MINIBR3. THUS, THE STRUCTURE OF BR3 WAS
REMARK 3 CALCULATED ONLY FOR THESE 26 RESIDUES, BASED ON A TOTAL OF 315
REMARK 3 DISTANCE AND 46 DIHEDRAL ANGLE RESTRAINTS DERIVED FROM ANALYSIS
REMARK 3 OF NMR DATA COLLEECTED ON THE ENTIRE BR3 ECD.
REMARK 4
REMARK 4 1OSX COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-APR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018636.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 5.0
REMARK 210 IONIC STRENGTH : 50 MM NACL, 25 MM NA2PO4
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5 MM BR3 U-15N,25 MM NA2PO4,
REMARK 210 50 MM NACL, 0.1 MM NAN3, 0.1 MM
REMARK 210 DSS-D10; 1.5 MM BR3 U-15N,13C,25
REMARK 210 MM NA2PO4, 50 MM NACL, 0.1 MM
REMARK 210 NAN3, 0.1 MM DSS-D10; 1.5 MM BR3
REMARK 210 U-15N,13C,25 MM NA2PO4, 50 MM
REMARK 210 NACL, 0.1 MM NAN3, 0.1 MM DSS-D10
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; HNHA; HNHB; 3D
REMARK 210 HCCH-COSY; 3D HCCH-TOCSY; 3D
REMARK 210 HNCO; 3D HNCA; 3D CBCA(CO)NH
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : FELIX 98, X-PLOR 98
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 128
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 RESTRAINT VIOLATION ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 1-20
REMARK 465 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 ARG A 2
REMARK 465 ARG A 3
REMARK 465 GLY A 4
REMARK 465 PRO A 5
REMARK 465 ARG A 6
REMARK 465 SER A 7
REMARK 465 LEU A 8
REMARK 465 ARG A 9
REMARK 465 GLY A 10
REMARK 465 ARG A 11
REMARK 465 ASP A 12
REMARK 465 ALA A 13
REMARK 465 PRO A 14
REMARK 465 ALA A 15
REMARK 465 PRO A 16
REMARK 465 PRO A 43
REMARK 465 LYS A 44
REMARK 465 PRO A 45
REMARK 465 ALA A 46
REMARK 465 GLY A 47
REMARK 465 ALA A 48
REMARK 465 SER A 49
REMARK 465 SER A 50
REMARK 465 PRO A 51
REMARK 465 ALA A 52
REMARK 465 PRO A 53
REMARK 465 ARG A 54
REMARK 465 THR A 55
REMARK 465 ALA A 56
REMARK 465 LEU A 57
REMARK 465 GLN A 58
REMARK 465 PRO A 59
REMARK 465 GLN A 60
REMARK 465 GLU A 61
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 PRO A 18 -163.60 -71.04
REMARK 500 1 CYS A 19 -146.78 -58.46
REMARK 500 1 PRO A 21 -24.62 -37.64
REMARK 500 1 HIS A 31 -177.68 -174.00
REMARK 500 1 ALA A 34 101.53 -40.05
REMARK 500 1 CYS A 35 115.77 -39.85
REMARK 500 1 LEU A 37 17.00 56.26
REMARK 500 1 THR A 40 131.11 62.52
REMARK 500 1 PRO A 41 -95.13 -75.19
REMARK 500 2 PRO A 18 155.31 -38.69
REMARK 500 2 CYS A 19 -145.70 -69.22
REMARK 500 2 PRO A 21 -22.83 -38.22
REMARK 500 2 ARG A 30 46.53 80.26
REMARK 500 2 HIS A 31 -158.44 -173.07
REMARK 500 2 ALA A 34 103.87 -47.68
REMARK 500 2 CYS A 35 99.95 -42.83
REMARK 500 2 LEU A 38 -157.18 -140.00
REMARK 500 2 THR A 40 68.18 -160.57
REMARK 500 3 CYS A 19 -157.36 -75.85
REMARK 500 3 PRO A 21 -22.78 -37.27
REMARK 500 3 HIS A 31 -175.40 -173.00
REMARK 500 3 ALA A 34 105.59 -55.13
REMARK 500 3 CYS A 35 100.04 -40.85
REMARK 500 3 LEU A 37 0.15 56.82
REMARK 500 3 THR A 40 64.65 29.55
REMARK 500 3 PRO A 41 100.41 -49.73
REMARK 500 4 CYS A 19 -156.68 -75.81
REMARK 500 4 PRO A 21 -23.69 -37.39
REMARK 500 4 ARG A 30 31.30 80.05
REMARK 500 4 HIS A 31 -176.79 -175.09
REMARK 500 4 ALA A 34 107.87 -52.20
REMARK 500 5 PRO A 18 -93.65 -72.82
REMARK 500 5 CYS A 19 -158.33 -78.87
REMARK 500 5 PRO A 21 -35.56 -34.78
REMARK 500 5 ARG A 30 24.99 80.12
REMARK 500 5 ALA A 34 107.22 -49.01
REMARK 500 5 CYS A 35 122.44 -39.98
REMARK 500 5 LEU A 37 19.50 54.56
REMARK 500 5 ARG A 39 116.66 -171.99
REMARK 500 6 PRO A 18 112.35 -38.59
REMARK 500 6 CYS A 19 -146.79 -76.10
REMARK 500 6 PRO A 21 -9.31 -48.58
REMARK 500 6 HIS A 31 -151.72 -173.96
REMARK 500 6 ALA A 34 106.57 -52.01
REMARK 500 6 CYS A 35 99.84 -46.58
REMARK 500 6 LEU A 38 -103.19 -99.90
REMARK 500 6 ARG A 39 -34.70 -172.50
REMARK 500 7 CYS A 19 -158.27 -106.67
REMARK 500 7 PRO A 21 -22.48 -37.57
REMARK 500 7 HIS A 31 -172.85 -173.63
REMARK 500
REMARK 500 THIS ENTRY HAS 151 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MPV RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF BHPBR3; BR3 RESIDUES 26-31 EMBEDDED IN A BETA-
REMARK 900 HAIRPIN PEPTIDE
REMARK 900 RELATED ID: 1OSG RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF BHPBR3 IN COMPLEX WITH BAFF
DBREF 1OSX A 1 61 UNP Q96RJ3 TR13C_HUMAN 1 61
SEQRES 1 A 61 MET ARG ARG GLY PRO ARG SER LEU ARG GLY ARG ASP ALA
SEQRES 2 A 61 PRO ALA PRO THR PRO CYS VAL PRO ALA GLU CYS PHE ASP
SEQRES 3 A 61 LEU LEU VAL ARG HIS CYS VAL ALA CYS GLY LEU LEU ARG
SEQRES 4 A 61 THR PRO ARG PRO LYS PRO ALA GLY ALA SER SER PRO ALA
SEQRES 5 A 61 PRO ARG THR ALA LEU GLN PRO GLN GLU
SHEET 1 A 2 GLU A 23 ASP A 26 0
SHEET 2 A 2 HIS A 31 ALA A 34 -1 O HIS A 31 N ASP A 26
SSBOND 1 CYS A 19 CYS A 32 1555 1555 2.03
SSBOND 2 CYS A 24 CYS A 35 1555 1555 2.03
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 - 23 20 Bytes