Header list of 1ejp.pdb file
Complete list - b 16 2 Bytes
HEADER SIGNALING PROTEIN 03-MAR-00 1EJP
TITLE SOLUTION STRUCTURE OF THE SYNDECAN-4 WHOLE CYTOPLASMIC DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SYNDECAN-4;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: WHOLE CYTOPLASMIC DOMAIN;
COMPND 5 SYNONYM: AMPHIGLYCAN, RYUDOCAN CORE PROTEIN, SYND4;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 4 OF THIS PETIDE OCCURS NATURALLY IN HUMANS (HOMO SAPIENS).
KEYWDS SYMMETRIC-PARALLEL-INTERWINDED DIMER, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 16
MDLTYP MINIMIZED AVERAGE
AUTHOR D.LEE,E.S.OH,A.WOODS,J.R.COUCHMAN,W.LEE
REVDAT 3 16-FEB-22 1EJP 1 REMARK
REVDAT 2 24-FEB-09 1EJP 1 VERSN
REVDAT 1 19-SEP-01 1EJP 0
JRNL AUTH J.SHIN,W.LEE,D.LEE,B.K.KOO,I.HAN,Y.LIM,A.WOODS,J.R.COUCHMAN,
JRNL AUTH 2 E.S.OH
JRNL TITL SOLUTION STRUCTURE OF THE DIMERIC CYTOPLASMIC DOMAIN OF
JRNL TITL 2 SYNDECAN-4.
JRNL REF BIOCHEMISTRY V. 40 8471 2001
JRNL REFN ISSN 0006-2960
JRNL PMID 11456484
JRNL DOI 10.1021/BI002750R
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 TITL SOLUTION STRUCTURE OF A SYNDECAN-4 CYTOPLASMIC DOMAIN AND
REMARK 1 TITL 2 ITS INTERACTION WITH PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE
REMARK 1 REF J.BIOL.CHEM. V. 273 13022 1998
REMARK 1 REFN ISSN 0021-9258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.5, X-PLOR 3.851
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER, A.T (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 THE STRUCTURES ARE BASED ON A TOTAL OF 306 RESTRAINTS, 246 ARE
REMARK 3 INTRAMONOMER NOE-DERIVED
REMARK 3 DISTANCE CONSTRAINTS, 48 INTERMONOMER NOE-DERIVED DISTANCE
REMARK 3 RESTRAINTS AND 12 DIHEDRAL ANGLE RESTRAINTS.
REMARK 4
REMARK 4 1EJP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAR-00.
REMARK 100 THE DEPOSITION ID IS D_1000010647.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298; 298; 298
REMARK 210 PH : 7.4; 7.4; 7.4
REMARK 210 IONIC STRENGTH : 50MM SODIUM PHOSPHATE; 50MM
REMARK 210 SODIUM PHOSPHATE; 50MM SODIUM
REMARK 210 PHOSPHATE
REMARK 210 PRESSURE : 1 ATM; 1 ATM; 1 ATM
REMARK 210 SAMPLE CONTENTS : 2-4MM SYNDECAN-4 PEPTIDE ; 50MM
REMARK 210 PHOSPHATE BUFFER; 90% H2O, 10%
REMARK 210 D2O; 2-4MM SYNDECAN-4 PEPTIDE ;
REMARK 210 50MM PHOSPHATE BUFFER; 90% H2O,
REMARK 210 10% D2O; 2-4MM SYNDECAN-4
REMARK 210 PEPTIDE ; 50MM PHOSPHATE BUFFER;
REMARK 210 100% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; DQF-COSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.5, SPARKY 3.6
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 90
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 16
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES.
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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
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 LYS A 5 -173.17 46.49
REMARK 500 1 ASP A 6 120.80 66.65
REMARK 500 1 GLU A 7 -168.60 -121.61
REMARK 500 1 SER A 9 -166.29 -172.16
REMARK 500 1 TYR A 10 -164.65 41.22
REMARK 500 1 ASP A 11 -71.93 -170.19
REMARK 500 1 LEU A 12 -168.95 43.88
REMARK 500 1 LYS A 14 -92.62 -170.05
REMARK 500 1 TYR A 18 72.64 -170.02
REMARK 500 1 LYS A 20 127.66 170.63
REMARK 500 1 PRO A 22 -167.57 -72.84
REMARK 500 1 THR A 23 76.48 -168.08
REMARK 500 1 PHE A 26 45.58 -82.77
REMARK 500 1 LYS B 5 -173.17 46.66
REMARK 500 1 ASP B 6 120.77 66.59
REMARK 500 1 GLU B 7 -168.57 -121.52
REMARK 500 1 SER B 9 -166.40 -172.11
REMARK 500 1 TYR B 10 -164.69 41.27
REMARK 500 1 ASP B 11 -72.00 -170.11
REMARK 500 1 LEU B 12 -169.05 44.03
REMARK 500 1 LYS B 14 -92.66 -170.08
REMARK 500 1 TYR B 18 72.55 -170.06
REMARK 500 1 LYS B 20 127.71 170.57
REMARK 500 1 PRO B 22 -167.60 -72.78
REMARK 500 1 THR B 23 76.45 -168.01
REMARK 500 1 PHE B 26 45.49 -82.71
REMARK 500 2 LYS A 3 -154.67 -132.26
REMARK 500 2 ASP A 6 127.04 173.34
REMARK 500 2 SER A 9 -150.30 -69.89
REMARK 500 2 LYS A 14 -92.94 -170.13
REMARK 500 2 TYR A 18 64.84 -158.64
REMARK 500 2 LYS A 20 94.82 174.27
REMARK 500 2 THR A 23 -151.51 32.20
REMARK 500 2 GLU A 25 83.48 -169.96
REMARK 500 2 PHE A 26 130.67 179.95
REMARK 500 2 TYR A 27 -68.41 -128.97
REMARK 500 2 LYS B 3 -154.68 -132.13
REMARK 500 2 ASP B 6 127.03 173.39
REMARK 500 2 SER B 9 -150.26 -69.88
REMARK 500 2 LYS B 14 -92.85 -170.23
REMARK 500 2 TYR B 18 64.82 -158.57
REMARK 500 2 LYS B 20 94.93 174.33
REMARK 500 2 THR B 23 -151.49 32.19
REMARK 500 2 GLU B 25 83.56 -169.95
REMARK 500 2 PHE B 26 130.56 179.83
REMARK 500 2 TYR B 27 -68.26 -128.92
REMARK 500 3 ASP A 6 56.77 -110.97
REMARK 500 3 ASP A 11 -91.22 -69.75
REMARK 500 3 LEU A 12 -169.29 44.21
REMARK 500 3 LYS A 14 -94.80 -170.17
REMARK 500
REMARK 500 THIS ENTRY HAS 357 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 1 0.31 SIDE CHAIN
REMARK 500 1 ARG B 1 0.31 SIDE CHAIN
REMARK 500 2 ARG A 1 0.29 SIDE CHAIN
REMARK 500 2 ARG B 1 0.29 SIDE CHAIN
REMARK 500 3 ARG A 1 0.20 SIDE CHAIN
REMARK 500 3 ARG B 1 0.20 SIDE CHAIN
REMARK 500 4 ARG A 1 0.25 SIDE CHAIN
REMARK 500 4 ARG B 1 0.25 SIDE CHAIN
REMARK 500 5 ARG A 1 0.31 SIDE CHAIN
REMARK 500 5 ARG B 1 0.31 SIDE CHAIN
REMARK 500 6 ARG A 1 0.30 SIDE CHAIN
REMARK 500 6 ARG B 1 0.30 SIDE CHAIN
REMARK 500 7 ARG A 1 0.10 SIDE CHAIN
REMARK 500 7 ARG B 1 0.10 SIDE CHAIN
REMARK 500 8 ARG A 1 0.17 SIDE CHAIN
REMARK 500 8 ARG B 1 0.17 SIDE CHAIN
REMARK 500 9 ARG A 1 0.32 SIDE CHAIN
REMARK 500 9 ARG B 1 0.32 SIDE CHAIN
REMARK 500 10 ARG A 1 0.26 SIDE CHAIN
REMARK 500 10 ARG B 1 0.26 SIDE CHAIN
REMARK 500 11 ARG A 1 0.24 SIDE CHAIN
REMARK 500 11 ARG B 1 0.24 SIDE CHAIN
REMARK 500 12 ARG A 1 0.32 SIDE CHAIN
REMARK 500 12 ARG B 1 0.32 SIDE CHAIN
REMARK 500 13 ARG A 1 0.32 SIDE CHAIN
REMARK 500 13 ARG B 1 0.32 SIDE CHAIN
REMARK 500 16 ARG A 1 0.30 SIDE CHAIN
REMARK 500 16 ARG B 1 0.30 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EJQ RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE SYNDECAN-4 WHOLE CYTOPLASMIC DOMAIN IN
REMARK 900 THE PRESENCE OF PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE
DBREF 1EJP A 1 28 UNP P31431 SDC4_HUMAN 171 198
DBREF 1EJP B 1 28 UNP P31431 SDC4_HUMAN 171 198
SEQRES 1 A 28 ARG MET LYS LYS LYS ASP GLU GLY SER TYR ASP LEU GLY
SEQRES 2 A 28 LYS LYS PRO ILE TYR LYS LYS ALA PRO THR ASN GLU PHE
SEQRES 3 A 28 TYR ALA
SEQRES 1 B 28 ARG MET LYS LYS LYS ASP GLU GLY SER TYR ASP LEU GLY
SEQRES 2 B 28 LYS LYS PRO ILE TYR LYS LYS ALA PRO THR ASN GLU PHE
SEQRES 3 B 28 TYR ALA
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 16 2 Bytes