Header list of 2ers.pdb file
Complete list - 9 20 Bytes
HEADER SIGNALING PROTEIN 25-OCT-05 2ERS
TITLE SOLUTION STRUCTURE OF THE INTERLEUKIN-15 RECEPTOR SUSHI DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERLEUKIN-15 RECEPTOR ALPHA CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SUSHI DOMAIN OF THE INTERLEUKIN-15 RECEPTOR;
COMPND 5 SYNONYM: IL-15RALPHA, IL-15RA;
COMPND 6 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_STRAIN: SG13009;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PQE30
KEYWDS SUSHI DOMAIN, SIGNALING PROTEIN
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR I.LORENZEN,A.J.DINGLEY,J.GROTZINGER
REVDAT 5 09-MAR-22 2ERS 1 REMARK
REVDAT 4 09-JUN-09 2ERS 1 REVDAT
REVDAT 3 24-FEB-09 2ERS 1 VERSN
REVDAT 2 06-JAN-09 2ERS 1 JRNL
REVDAT 1 07-FEB-06 2ERS 0
JRNL AUTH I.LORENZEN,A.J.DINGLEY,Y.JACQUES,J.GROTZINGER
JRNL TITL THE STRUCTURE OF THE INTERLEUKIN-15 ALPHA RECEPTOR AND ITS
JRNL TITL 2 IMPLICATIONS FOR LIGAND BINDING.
JRNL REF J.BIOL.CHEM. V. 281 6642 2006
JRNL REFN ISSN 0021-9258
JRNL PMID 16377614
JRNL DOI 10.1074/JBC.M513118200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5
REMARK 3 AUTHORS : GUENTERT
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ERS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-NOV-05.
REMARK 100 THE DEPOSITION ID IS D_1000035014.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.4
REMARK 210 IONIC STRENGTH : 150MM NACL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM IL-15 RECEPTOR SUSHI DOMIAN
REMARK 210 15N,13C; 20MM PHOSPHATE BUFFER;
REMARK 210 150MM SODIUM CHLORIDE; 7% D2O;
REMARK 210 PH = 7.4
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNCA; HC(CO)NH;
REMARK 210 3D_15N_EDITED TOCSY A.O.
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : DYANA 1.5
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 20
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
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: 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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (RES=RESIDUE NAME;
REMARK 470 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 470 RES CSSEQI ATOMS
REMARK 470 ASP A 96 OD2
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 HG CYS A 33 HG CYS A 75 0.40
REMARK 500 SG CYS A 33 HG CYS A 75 0.97
REMARK 500 HG1 THR A 69 H LYS A 92 1.03
REMARK 500 HA CYS A 59 HG CYS A 93 1.25
REMARK 500 HG CYS A 33 SG CYS A 75 1.34
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 TYR A 52 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 ARG A 95 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
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 SER A 38 -141.07 -153.84
REMARK 500 VAL A 39 -79.90 59.17
REMARK 500 GLU A 40 -75.85 103.44
REMARK 500 HIS A 41 48.60 -89.87
REMARK 500 TYR A 49 -166.65 45.92
REMARK 500 SER A 50 148.40 175.69
REMARK 500 CYS A 59 174.35 53.44
REMARK 500 SER A 61 89.91 -66.39
REMARK 500 PHE A 63 151.09 -49.32
REMARK 500 LYS A 66 154.48 -46.58
REMARK 500 SER A 71 66.39 -110.93
REMARK 500 ASN A 78 18.08 -67.90
REMARK 500 LYS A 79 21.67 46.85
REMARK 500 ALA A 80 -61.79 -150.27
REMARK 500 ASN A 82 6.94 49.16
REMARK 500 TRP A 86 67.84 -110.72
REMARK 500 THR A 87 -160.13 29.38
REMARK 500 LEU A 91 118.78 47.80
REMARK 500 ARG A 95 146.18 -38.77
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 HIS A 41 0.09 SIDE CHAIN
REMARK 500 TYR A 57 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY
REMARK 500
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 500 I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI ANGLE
REMARK 500 CYS A 59 11.59
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2ERS A 31 96 UNP Q13261 I15RA_HUMAN 31 96
SEQRES 1 A 66 ILE THR CYS PRO PRO PRO MET SER VAL GLU HIS ALA ASP
SEQRES 2 A 66 ILE TRP VAL LYS SER TYR SER LEU TYR SER ARG GLU ARG
SEQRES 3 A 66 TYR ILE CYS ASN SER GLY PHE LYS ARG LYS ALA GLY THR
SEQRES 4 A 66 SER SER LEU THR GLU CYS VAL LEU ASN LYS ALA THR ASN
SEQRES 5 A 66 VAL ALA HIS TRP THR THR PRO SER LEU LYS CYS ILE ARG
SEQRES 6 A 66 ASP
SHEET 1 A 3 ARG A 54 ARG A 56 0
SHEET 2 A 3 LEU A 72 LEU A 77 -1 O THR A 73 N GLU A 55
SHEET 3 A 3 ALA A 84 TRP A 86 -1 O HIS A 85 N VAL A 76
SHEET 1 B 2 LYS A 64 ARG A 65 0
SHEET 2 B 2 CYS A 93 ILE A 94 -1 O ILE A 94 N LYS A 64
SSBOND 1 CYS A 33 CYS A 75 1555 1555 2.04
SSBOND 2 CYS A 59 CYS A 93 1555 1555 2.04
CISPEP 1 ARG A 95 ASP A 96 0 10.85
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 - 9 20 Bytes