HEADER PHOSPHOTRANSFERASE 07-MAR-94 1PKS
TITLE STRUCTURE OF THE PI3K SH3 DOMAIN AND ANALYSIS OF THE SH3 FAMILY
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHATIDYLINOSITOL 3-KINASE P85-ALPHA SUBUNIT SH3 DOMAIN;
COMPND 3 CHAIN: A;
COMPND 4 EC: 2.7.1.137;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS PHOSPHOTRANSFERASE
EXPDTA SOLUTION NMR
AUTHOR S.KOYAMA,H.YU,D.C.DALGARNO,T.B.SHIN,L.D.ZYDOWSKY,S.L.SCHREIBER
REVDAT 3 29-NOV-17 1PKS 1 REMARK HELIX
REVDAT 2 24-FEB-09 1PKS 1 VERSN
REVDAT 1 31-MAY-94 1PKS 0
JRNL AUTH S.KOYAMA,H.YU,D.C.DALGARNO,T.B.SHIN,L.D.ZYDOWSKY,
JRNL AUTH 2 S.L.SCHREIBER
JRNL TITL STRUCTURE OF THE PI3K SH3 DOMAIN AND ANALYSIS OF THE SH3
JRNL TITL 2 FAMILY.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 72 945 1993
JRNL REFN ISSN 0092-8674
JRNL PMID 7681364
JRNL DOI 10.1016/0092-8674(93)90582-B
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.KOYAMA,H.YU,D.C.DALGARNO,T.B.SHIN,L.D.ZYDOWSKY,
REMARK 1 AUTH 2 S.L.SCHREIBER
REMARK 1 TITL 1H AND 15N ASSIGNMENTS AND SECONDARY STRUCTURE OF THE PI3K
REMARK 1 TITL 2 SH3 DOMAIN
REMARK 1 REF FEBS LETT. V. 324 93 1993
REMARK 1 REFN ISSN 0014-5793
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 1PKS 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_1000175715.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : NULL
REMARK 210 PH : NULL
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 : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
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: 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 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 RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 SER A 2
REMARK 465 ALA A 3
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 HIS A 25 CG HIS A 25 ND1 -0.101
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 TRP A 55 CG - CD1 - NE1 ANGL. DEV. = -6.5 DEGREES
REMARK 500 TRP A 55 CD1 - NE1 - CE2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 TRP A 55 NE1 - CE2 - CZ2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 TRP A 55 NE1 - CE2 - CD2 ANGL. DEV. = -6.3 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 LYS A 16 88.53 -54.18
REMARK 500 GLU A 17 -76.35 -89.99
REMARK 500 ASN A 33 176.80 -51.76
REMARK 500 PHE A 42 -177.44 -49.78
REMARK 500 ASP A 44 85.78 -68.46
REMARK 500 ALA A 48 41.94 -95.48
REMARK 500 ARG A 49 66.25 -156.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1PKT RELATED DB: PDB
DBREF 1PKS A 1 79 UNP P27986 P85A_HUMAN 1 79
SEQRES 1 A 79 MET SER ALA GLU GLY TYR GLN TYR ARG ALA LEU TYR ASP
SEQRES 2 A 79 TYR LYS LYS GLU ARG GLU GLU ASP ILE ASP LEU HIS LEU
SEQRES 3 A 79 GLY ASP ILE LEU THR VAL ASN LYS GLY SER LEU VAL ALA
SEQRES 4 A 79 LEU GLY PHE SER ASP GLY GLN GLU ALA ARG PRO GLU GLU
SEQRES 5 A 79 ILE GLY TRP LEU ASN GLY TYR ASN GLU THR THR GLY GLU
SEQRES 6 A 79 ARG GLY ASP PHE PRO GLY THR TYR VAL GLU TYR ILE GLY
SEQRES 7 A 79 ARG
HELIX 1 H1 LYS A 34 ALA A 39 1RIGHT-HANDED ALPHA HELIX 6
HELIX 2 H2 GLN A 46 ARG A 49 1RIGHT-HANDED 3=10= HELIX 4
HELIX 3 H3 PRO A 50 ILE A 53 1RIGHT-HANDED 3=10= HELIX 4
HELIX 4 H4 GLY A 71 VAL A 74 1RIGHT-HANDED 3=10= HELIX 4
SHEET 1 S1 5 GLU A 65 PRO A 70 0
SHEET 2 S1 5 TRP A 55 ASN A 60 -1 N GLY A 58 O GLY A 67
SHEET 3 S1 5 ASP A 28 VAL A 32 -1 N THR A 31 O TYR A 59
SHEET 4 S1 5 TYR A 6 LEU A 11 -1 N TYR A 8 O LEU A 30
SHEET 5 S1 5 VAL A 74 GLY A 78 -1 N GLU A 75 O ARG A 9
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
(ATOM LINES ARE NOT SHOWN.)
END
