Header list of 1sgg.pdb file
Complete list - 2 20 Bytes
HEADER TYROSINE-PROTEIN KINASE 08-JAN-99 1SGG
TITLE THE SOLUTION STRUCTURE OF SAM DOMAIN FROM THE RECEPTOR TYROSINE KINASE
TITLE 2 EPHB2, NMR, 10 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EPHRIN TYPE-B RECEPTOR 2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SAM DOMAIN;
COMPND 5 EC: 2.7.1.112;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: POTENTIAL TYROSINE PHOSPHORYLATION AT Y 25
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_CELL_LINE: BL21;
SOURCE 8 EXPRESSION_SYSTEM_TISSUE: EMBRYO;
SOURCE 9 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET 28D
KEYWDS RECEPTOR OLIGOMERIZATION, EPH RECEPTORS, TYROSINE PHOSPHORYLATION,
KEYWDS 2 SIGNAL TRANSDUCTION, TYROSINE-PROTEIN KINASE
EXPDTA SOLUTION NMR
NUMMDL 10
AUTHOR M.SMALLA,P.SCHMIEDER,M.KELLY,A.TER LAAK,G.KRAUSE,L.BALL,M.WAHL,
AUTHOR 2 P.BORK,H.OSCHKINAT
REVDAT 3 02-MAR-22 1SGG 1 REMARK
REVDAT 2 24-FEB-09 1SGG 1 VERSN
REVDAT 1 06-OCT-99 1SGG 0
JRNL AUTH M.SMALLA,P.SCHMIEDER,M.KELLY,A.TER LAAK,G.KRAUSE,L.BALL,
JRNL AUTH 2 M.WAHL,P.BORK,H.OSCHKINAT
JRNL TITL SOLUTION STRUCTURE OF THE RECEPTOR TYROSINE KINASE EPHB2 SAM
JRNL TITL 2 DOMAIN AND IDENTIFICATION OF TWO DISTINCT HOMOTYPIC
JRNL TITL 3 INTERACTION SITES.
JRNL REF PROTEIN SCI. V. 8 1954 1999
JRNL REFN ISSN 0961-8368
JRNL PMID 10548040
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1SGG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000176362.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 300
REMARK 210 PH : 5.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : 100% H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D-NOESY; 2D-TOCSY; 1H-15 NOESY;
REMARK 210 1H-13C NOESY; HCCH-TOCSY; HCCH-
REMARK 210 COSY; CBCANNH; CBCA (CO)NNH;
REMARK 210 CC(CO)NNH-TOCSY; HBHA(CO)NNH;
REMARK 210 HC(CO)NNH-TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : DRX600; DRX750
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 10
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGIES
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 ON 13C, 15N-LABELED EPHB2 SAM DOMAIN
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 1-10
REMARK 465 RES C SSSEQI
REMARK 465 ASP A 1
REMARK 465 ARG A 2
REMARK 465 THR A 3
REMARK 465 ILE A 4
REMARK 465 PRO A 5
REMARK 465 ASP A 6
REMARK 465 ASN A 74
REMARK 465 GLN A 75
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 21 75.91 56.54
REMARK 500 1 GLN A 24 37.65 -91.66
REMARK 500 1 LYS A 26 -81.79 -73.23
REMARK 500 1 PHE A 34 44.94 -95.42
REMARK 500 1 ASP A 38 -76.22 -178.88
REMARK 500 1 SER A 41 42.25 -91.47
REMARK 500 1 GLN A 42 43.37 -160.51
REMARK 500 1 THR A 44 -150.02 -152.26
REMARK 500 1 VAL A 53 46.43 -89.22
REMARK 500 2 THR A 8 41.36 -90.08
REMARK 500 2 LYS A 21 76.60 53.22
REMARK 500 2 TYR A 25 21.72 -142.54
REMARK 500 2 LYS A 26 -80.80 -65.87
REMARK 500 2 PHE A 34 55.43 -95.66
REMARK 500 2 THR A 35 -61.45 -93.14
REMARK 500 2 PHE A 37 41.64 -92.01
REMARK 500 2 ASP A 38 -79.43 -130.57
REMARK 500 2 SER A 41 44.02 -90.58
REMARK 500 2 GLN A 42 74.34 -163.62
REMARK 500 2 MET A 43 -158.05 -137.29
REMARK 500 2 THR A 44 -152.46 -175.07
REMARK 500 2 VAL A 53 42.71 -91.36
REMARK 500 3 LYS A 21 77.91 53.41
REMARK 500 3 TYR A 25 17.50 -144.39
REMARK 500 3 LYS A 26 -80.37 -66.07
REMARK 500 3 PHE A 34 56.25 -94.53
REMARK 500 3 PHE A 37 42.09 -92.41
REMARK 500 3 ASP A 38 -79.06 -133.28
REMARK 500 3 SER A 41 41.01 -95.46
REMARK 500 3 GLN A 42 45.51 -155.22
REMARK 500 3 THR A 44 -164.68 -117.11
REMARK 500 3 VAL A 53 44.87 -94.60
REMARK 500 4 LYS A 21 78.45 53.83
REMARK 500 4 GLN A 24 47.60 -86.09
REMARK 500 4 LYS A 26 -82.52 -77.56
REMARK 500 4 PHE A 34 55.79 -93.65
REMARK 500 4 PHE A 37 41.60 -92.44
REMARK 500 4 ASP A 38 -79.50 -130.72
REMARK 500 4 SER A 41 37.00 -93.66
REMARK 500 4 GLN A 42 47.89 -156.44
REMARK 500 4 THR A 44 -164.07 -109.84
REMARK 500 4 VAL A 53 42.93 -90.87
REMARK 500 5 THR A 8 38.50 -91.39
REMARK 500 5 LYS A 21 89.84 55.28
REMARK 500 5 PHE A 34 42.58 -92.35
REMARK 500 5 PHE A 37 42.71 -92.46
REMARK 500 5 ASP A 38 -81.15 -130.79
REMARK 500 5 SER A 41 37.82 -94.11
REMARK 500 5 GLN A 42 52.78 -166.99
REMARK 500 5 VAL A 53 49.24 -94.99
REMARK 500
REMARK 500 THIS ENTRY HAS 100 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 50 0.22 SIDE CHAIN
REMARK 500 1 ARG A 70 0.31 SIDE CHAIN
REMARK 500 2 ARG A 50 0.16 SIDE CHAIN
REMARK 500 2 ARG A 70 0.19 SIDE CHAIN
REMARK 500 3 ARG A 50 0.24 SIDE CHAIN
REMARK 500 3 ARG A 70 0.31 SIDE CHAIN
REMARK 500 4 ARG A 50 0.17 SIDE CHAIN
REMARK 500 4 ARG A 70 0.20 SIDE CHAIN
REMARK 500 5 ARG A 50 0.30 SIDE CHAIN
REMARK 500 5 ARG A 70 0.25 SIDE CHAIN
REMARK 500 6 ARG A 50 0.32 SIDE CHAIN
REMARK 500 6 ARG A 70 0.28 SIDE CHAIN
REMARK 500 7 ARG A 50 0.22 SIDE CHAIN
REMARK 500 7 ARG A 70 0.22 SIDE CHAIN
REMARK 500 8 ARG A 50 0.32 SIDE CHAIN
REMARK 500 8 ARG A 70 0.29 SIDE CHAIN
REMARK 500 9 ARG A 50 0.31 SIDE CHAIN
REMARK 500 9 ARG A 70 0.21 SIDE CHAIN
REMARK 500 10 ARG A 50 0.18 SIDE CHAIN
REMARK 500 10 ARG A 70 0.23 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1SGG A 1 75 UNP P28693 EPHB2_CHICK 924 998
SEQRES 1 A 75 ASP ARG THR ILE PRO ASP TYR THR SER PHE ASN THR VAL
SEQRES 2 A 75 ASP GLU TRP LEU ASP ALA ILE LYS MET SER GLN TYR LYS
SEQRES 3 A 75 GLU SER PHE ALA SER ALA GLY PHE THR THR PHE ASP ILE
SEQRES 4 A 75 VAL SER GLN MET THR VAL GLU ASP ILE LEU ARG VAL GLY
SEQRES 5 A 75 VAL THR LEU ALA GLY HIS GLN LYS LYS ILE LEU ASN SER
SEQRES 6 A 75 ILE GLN VAL MET ARG ALA GLN MET ASN GLN
HELIX 1 1 THR A 12 ILE A 20 1 9
HELIX 2 2 SER A 23 SER A 31 1 9
HELIX 3 3 ASP A 38 GLN A 42 5 5
HELIX 4 4 VAL A 45 VAL A 51 1 7
HELIX 5 5 HIS A 58 MET A 73 1 16
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 - 2 20 Bytes