Header list of 1pic.pdb file
Complete list - 23 20 Bytes
HEADER COMPLEX (PHOSPHOTRANSFERASE/RECEPTOR) 23-JUN-97 1PIC
TITLE PHOSPHATIDYLINOSITOL 3-KINASE, P85-ALPHA SUBUNIT: C-TERMINAL SH2
TITLE 2 DOMAIN COMPLEXED WITH A TYR751 PHOSPHOPEPTIDE FROM THE PDGF RECEPTOR,
TITLE 3 NMR, MINIMIZED MEAN STRUCTURE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHATIDYLINOSITOL 3-KINASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL SH2 DOMAIN, RESIDUES 617 - 724 OF P85-ALPHA
COMPND 5 REGULATORY SUBUNIT;
COMPND 6 EC: 2.7.1.137;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: CONTAINS AN N-TERMINAL EXTENSION (GSPI) DERIVED FROM
COMPND 9 THE RECOMBINANT EXPRESSION VECTOR;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: BETA-PLATELET-DERIVED GROWTH FACTOR RECEPTOR;
COMPND 12 CHAIN: B;
COMPND 13 FRAGMENT: ACETYL-PTYR-VAL-PRO-MET-LEU, RESIDUES 751 - 755;
COMPND 14 ENGINEERED: YES;
COMPND 15 OTHER_DETAILS: TYROSINE-PHOSPHORYLATED PEPTIDE INCORPORATES AN N-
COMPND 16 TERMINAL ACETYL GROUP
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: W3110 (CGSC 6564);
SOURCE 8 MOL_ID: 2
KEYWDS PHOSPHOTRANSFERASE, SH2 DOMAIN, SIGNAL TRANSDUCTION, PHOSPHOINOSITIDE
KEYWDS 2 3-KINASE, COMPLEX (PHOSPHOTRANSFERASE-RECEPTOR), COMPLEX
KEYWDS 3 (PHOSPHOTRANSFERASE-RECEPTOR) COMPLEX
EXPDTA SOLUTION NMR
AUTHOR A.L.BREEZE,B.V.KARA,D.G.BARRATT,M.ANDERSON,J.C.SMITH,R.W.LUKE,
AUTHOR 2 J.R.BEST,S.A.CARTLIDGE
REVDAT 3 23-FEB-22 1PIC 1 REMARK LINK
REVDAT 2 24-FEB-09 1PIC 1 VERSN
REVDAT 1 17-SEP-97 1PIC 0
JRNL AUTH A.L.BREEZE,B.V.KARA,D.G.BARRATT,M.ANDERSON,J.C.SMITH,
JRNL AUTH 2 R.W.LUKE,J.R.BEST,S.A.CARTLIDGE
JRNL TITL STRUCTURE OF A SPECIFIC PEPTIDE COMPLEX OF THE
JRNL TITL 2 CARBOXY-TERMINAL SH2 DOMAIN FROM THE P85 ALPHA SUBUNIT OF
JRNL TITL 3 PHOSPHATIDYLINOSITOL 3-KINASE.
JRNL REF EMBO J. V. 15 3579 1996
JRNL REFN ISSN 0261-4189
JRNL PMID 8670861
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINEMENT DETAILS CAN BE FOUND IN THE
REMARK 3 JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1PIC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000175691.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 296
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 750 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
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 : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED BY TRIPLE-RESONANCE NMR ON
REMARK 210 13C,15N-LABELLED SH2 DOMAIN COMBINED WITH ISOTOPE-FILTERED 1H-
REMARK 210 NMR FOR THE UNLABELLED BOUND PEPTIDE.
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: 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 17 52.08 87.68
REMARK 500 ASN A 18 57.37 -155.83
REMARK 500 ARG A 19 -71.30 -78.33
REMARK 500 ARG A 27 89.09 -57.75
REMARK 500 LYS A 29 -176.14 -57.11
REMARK 500 GLU A 38 -161.17 -125.04
REMARK 500 SER A 39 -157.48 -177.57
REMARK 500 LYS A 41 -178.33 -52.88
REMARK 500 CYS A 44 -166.76 -75.45
REMARK 500 LYS A 62 -55.41 -132.90
REMARK 500 THR A 65 -29.64 -172.00
REMARK 500 ALA A 70 -26.46 166.54
REMARK 500 ASN A 74 -159.30 49.03
REMARK 500 LEU A 75 -109.86 -129.42
REMARK 500 TYR A 76 122.41 73.32
REMARK 500 SER A 77 41.54 -101.40
REMARK 500 LEU A 98 -77.68 -107.25
REMARK 500 ALA A 108 -166.92 43.20
REMARK 500 GLN A 109 45.25 174.02
REMARK 500 ARG A 111 -94.39 -111.62
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 ARG A 19 0.24 SIDE CHAIN
REMARK 500 ARG A 27 0.28 SIDE CHAIN
REMARK 500 ARG A 30 0.28 SIDE CHAIN
REMARK 500 ARG A 37 0.24 SIDE CHAIN
REMARK 500 ARG A 112 0.28 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACE B 200
DBREF 1PIC A 5 112 UNP P27986 P85A_HUMAN 617 724
DBREF 1PIC B 200 205 PDB 1PIC 1PIC 200 205
SEQRES 1 A 112 GLY SER PRO ILE PRO HIS HIS ASP GLU LYS THR TRP ASN
SEQRES 2 A 112 VAL GLY SER SER ASN ARG ASN LYS ALA GLU ASN LEU LEU
SEQRES 3 A 112 ARG GLY LYS ARG ASP GLY THR PHE LEU VAL ARG GLU SER
SEQRES 4 A 112 SER LYS GLN GLY CYS TYR ALA CYS SER VAL VAL VAL ASP
SEQRES 5 A 112 GLY GLU VAL LYS HIS CYS VAL ILE ASN LYS THR ALA THR
SEQRES 6 A 112 GLY TYR GLY PHE ALA GLU PRO TYR ASN LEU TYR SER SER
SEQRES 7 A 112 LEU LYS GLU LEU VAL LEU HIS TYR GLN HIS THR SER LEU
SEQRES 8 A 112 VAL GLN HIS ASN ASP SER LEU ASN VAL THR LEU ALA TYR
SEQRES 9 A 112 PRO VAL TYR ALA GLN GLN ARG ARG
SEQRES 1 B 6 ACE PTR VAL PRO MET LEU
MODRES 1PIC PTR B 201 TYR O-PHOSPHOTYROSINE
HET ACE B 200 6
HET PTR B 201 24
HETNAM ACE ACETYL GROUP
HETNAM PTR O-PHOSPHOTYROSINE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 2 ACE C2 H4 O
FORMUL 2 PTR C9 H12 N O6 P
HELIX 1 1 ARG A 19 LEU A 26 1 8
HELIX 2 2 LEU A 79 HIS A 88 1 10
SHEET 1 A 3 PHE A 34 ARG A 37 0
SHEET 2 A 3 ALA A 46 VAL A 51 -1 N SER A 48 O LEU A 35
SHEET 3 A 3 GLU A 54 VAL A 59 -1 N CYS A 58 O CYS A 47
LINK C ACE B 200 N PTR B 201 1555 1555 1.31
LINK C PTR B 201 N VAL B 202 1555 1555 1.30
SITE 1 AC1 2 HIS A 57 VAL B 202
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 - 23 20 Bytes