HEADER SIGNALING PROTEIN 11-AUG-09 2KN1
TITLE SOLUTION NMR STRUCTURE OF BCMA
CAVEAT 2KN1 IN MODEL 11, RESIDUE A LYS 49 AND RESIDUE A CY1 50 ARE NOT
CAVEAT 2 2KN1 PROPERLY LINKED, WITH A C-N BOND DISTANCE OF 6.76 ANGSTROM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 17;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 2-50;
COMPND 5 SYNONYM: B-CELL MATURATION PROTEIN;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606;
SOURCE 6 OTHER_DETAILS: SOLID PHASE PEPTIDE SYNTHESIS
KEYWDS BCMA, BAFF, TNF RECEPTOR, CRD, APRIL, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR M.PELLEGRINI,L.WILLEN,M.PERROUD,D.KRUSHINSKIE,K.STRAUCH,H.CUERVO,
AUTHOR 2 Y.SUN,E.S.DAY,P.SCHNEIDER,T.S.ZHENG
REVDAT 3 01-MAY-13 2KN1 1 JRNL
REVDAT 2 10-APR-13 2KN1 1 JRNL VERSN
REVDAT 1 23-FEB-11 2KN1 0
JRNL AUTH M.PELLEGRINI,L.WILLEN,M.PERROUD,D.KRUSHINSKIE,K.STRAUCH,
JRNL AUTH 2 H.CUERVO,E.S.DAY,P.SCHNEIDER,T.S.ZHENG
JRNL TITL STRUCTURE OF THE EXTRACELLULAR DOMAINS OF HUMAN AND XENOPUS
JRNL TITL 2 FN14: IMPLICATIONS IN THE EVOLUTION OF TWEAK AND FN14
JRNL TITL 3 INTERACTIONS.
JRNL REF FEBS J. V. 280 1818 2013
JRNL REFN ISSN 1742-464X
JRNL PMID 23438059
JRNL DOI 10.1111/FEBS.12206
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER A. T. ET.AL.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2KN1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-AUG-09.
REMARK 100 THE RCSB ID CODE IS RCSB101323.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298-318
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : 10
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 900 UM BCMA, 10 MM SODIUM
REMARK 210 PHOSPHATE, 0.02 % SODIUM AZIDE,
REMARK 210 95% H2O, 5% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : CNS 1.1, SPARKY 3.11
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : 20 LOWEST ENERGY STRUCTURES
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: 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 H TYR A 12 O ILE A 21 1.54
REMARK 500 O ASP A 14 H HIS A 18 1.56
REMARK 500 O CYS A 36 H CYS A 40 1.59
REMARK 500 O TYR A 12 H ILE A 21 1.60
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 MET A 3 -2.14 75.76
REMARK 500 1 ALA A 4 73.09 -64.89
REMARK 500 1 GLN A 6 72.67 168.46
REMARK 500 1 ASN A 30 -14.91 76.26
REMARK 500 1 THR A 31 53.35 30.30
REMARK 500 1 THR A 45 146.32 -29.43
REMARK 500 1 SER A 47 146.71 67.78
REMARK 500 1 VAL A 48 93.77 50.67
REMARK 500 1 LYS A 49 158.30 65.08
REMARK 500 2 GLN A 2 139.31 63.71
REMARK 500 2 MET A 3 -7.99 78.50
REMARK 500 2 GLN A 6 73.72 165.28
REMARK 500 2 THR A 31 67.16 11.79
REMARK 500 2 PRO A 32 92.19 -33.48
REMARK 500 2 VAL A 44 55.65 -142.71
REMARK 500 2 THR A 45 171.78 53.37
REMARK 500 2 SER A 47 147.69 62.79
REMARK 500 2 VAL A 48 100.38 168.17
REMARK 500 2 LYS A 49 92.87 56.69
REMARK 500 3 MET A 3 -5.50 77.42
REMARK 500 3 GLN A 6 70.79 176.50
REMARK 500 3 CYS A 23 -21.66 -145.03
REMARK 500 3 THR A 31 75.14 0.32
REMARK 500 3 PRO A 32 94.97 -38.30
REMARK 500 3 VAL A 44 58.01 -141.53
REMARK 500 3 THR A 45 -44.56 82.68
REMARK 500 3 ASN A 46 -164.74 49.29
REMARK 500 3 SER A 47 94.13 74.47
REMARK 500 3 VAL A 48 99.15 168.37
REMARK 500 3 LYS A 49 -167.96 165.31
REMARK 500 4 MET A 3 -6.43 78.93
REMARK 500 4 GLN A 6 71.08 176.36
REMARK 500 4 PRO A 22 167.16 -45.64
REMARK 500 4 CYS A 23 -20.31 -143.01
REMARK 500 4 CYS A 27 -101.23 -34.15
REMARK 500 4 ASN A 30 27.19 47.37
REMARK 500 4 THR A 31 84.13 -176.16
REMARK 500 4 PRO A 32 109.65 -49.84
REMARK 500 4 SER A 43 -37.21 -130.81
REMARK 500 4 THR A 45 -50.18 68.32
REMARK 500 4 ASN A 46 -176.04 50.88
REMARK 500 4 SER A 47 131.54 70.13
REMARK 500 4 VAL A 48 93.51 50.65
REMARK 500 4 LYS A 49 -172.30 55.36
REMARK 500 5 MET A 3 -50.75 159.00
REMARK 500 5 ALA A 4 82.39 -12.07
REMARK 500 5 GLN A 6 70.38 178.48
REMARK 500 5 CYS A 27 -84.57 38.49
REMARK 500 5 SER A 28 55.76 -143.81
REMARK 500 5 THR A 31 77.94 -170.60
REMARK 500
REMARK 500 THIS ENTRY HAS 255 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2KMZ RELATED DB: PDB
REMARK 900 HUMAN FN14 SOLUTION NMR STRUCTURE
REMARK 900 RELATED ID: 2KN0 RELATED DB: PDB
REMARK 900 XENOPUS FN14 SOLUTION NMR STRUCTURE
DBREF 2KN1 A 1 49 UNP Q02223 TNR17_HUMAN 2 50
SEQADV 2KN1 CY1 A 50 UNP Q02223 INSERTION
SEQADV 2KN1 NH2 A 51 UNP Q02223 INSERTION
SEQRES 1 A 51 LEU GLN MET ALA GLY GLN CYS SER GLN ASN GLU TYR PHE
SEQRES 2 A 51 ASP SER LEU LEU HIS ALA CYS ILE PRO CYS GLN LEU ARG
SEQRES 3 A 51 CYS SER SER ASN THR PRO PRO LEU THR CYS GLN ARG TYR
SEQRES 4 A 51 CYS ASN ALA SER VAL THR ASN SER VAL LYS CY1 NH2
MODRES 2KN1 CY1 A 50 CYS ACETAMIDOMETHYLCYSTEINE
HET CY1 A 50 21
HET NH2 A 51 3
HETNAM CY1 ACETAMIDOMETHYLCYSTEINE
HETNAM NH2 AMINO GROUP
FORMUL 1 CY1 C6 H12 N2 O3 S
FORMUL 1 NH2 H2 N
HELIX 1 1 CYS A 23 SER A 28 1 6
HELIX 2 2 CYS A 36 ASN A 41 1 6
SHEET 1 A 2 GLU A 11 PHE A 13 0
SHEET 2 A 2 CYS A 20 PRO A 22 -1 O ILE A 21 N TYR A 12
SSBOND 1 CYS A 7 CYS A 20 1555 1555 2.03
SSBOND 2 CYS A 23 CYS A 36 1555 1555 2.03
SSBOND 3 CYS A 27 CYS A 40 1555 1555 2.03
LINK C LYS A 49 N CY1 A 50 1555 1555 1.33
LINK C CY1 A 50 N NH2 A 51 1555 1555 1.33
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
(ATOM LINES ARE NOT SHOWN.)
END
