Header list of 1oo4.pdb file
Complete list - 10 20 Bytes
HEADER PROTEIN BINDING 03-MAR-03 1OO4
TITLE P395S MUTANT OF THE P85 REGULATORY SUBUNIT OF THE N-TERMINAL SRC
TITLE 2 HOMOLOGY 2 DOMAIN OF PI3-KINASE COMPLEXED TO A PEPTIDE DERIVED FROM
TITLE 3 PDGFR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY ALPHA SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: P85 N-SH2;
COMPND 5 SYNONYM: PI3-KINASE P85-ALPHA SUBUNIT;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: 8-MER PEPTIDE FROM PDGFR;
COMPND 10 CHAIN: B;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 OTHER_DETAILS: CHEMICALLY SYNTHESIZED
KEYWDS SRC HOMOLOGY 2 DOMAIN P85 REGULATORY SUBUNIT MUTANT, PDGFR COMPLEX,
KEYWDS 2 PROTEIN BINDING
EXPDTA SOLUTION NMR
MDLTYP MINIMIZED AVERAGE
AUTHOR U.L.GUENTHER,B.WEYRAUCH,B.SCHAFFHAUSEN
REVDAT 5 10-NOV-21 1OO4 1 REMARK SEQADV LINK
REVDAT 4 24-FEB-09 1OO4 1 VERSN
REVDAT 3 19-JUL-05 1OO4 1 REMARK
REVDAT 2 03-MAY-05 1OO4 1 JRNL ATOM
REVDAT 1 25-MAR-03 1OO4 0
JRNL AUTH U.L.GUENTHER,B.WEYRAUCH,X.ZHANG,B.SCHAFFHAUSEN
JRNL TITL NUCLEAR MAGNETIC RESONANCE STRUCTURE OF THE P395S MUTANT OF
JRNL TITL 2 THE N-SH2 DOMAIN OF THE P85 SUBUNIT OF PI3 KINASE: AN SH2
JRNL TITL 3 DOMAIN WITH ALTERED SPECIFICITY
JRNL REF BIOCHEMISTRY V. 42 11120 2003
JRNL REFN ISSN 0006-2960
JRNL PMID 14503862
JRNL DOI 10.1021/BI034353X
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5, DISCOVER 97.0
REMARK 3 AUTHORS : GUENTERT (DYANA), MSI INC. (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1022 NOE-DERIVED DISTANCE CONSTRAINTS,
REMARK 3 91 DIHEDRAL ANGLE RESTRAINTS, 37 NOE-DERIVED DISTANCE
REMARK 3 CONSTRAINTS FOR THE PEPTIDE LIGAND FROM 13C{F1}-FILTERED 2D-NOESY
REMARK 4
REMARK 4 1OO4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAR-03.
REMARK 100 THE DEPOSITION ID IS D_1000018491.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 6.8
REMARK 210 IONIC STRENGTH : 0.1M KCL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1.5MM P395S-15N, 13C, 0.1M KCL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_13C-SEPARATED_NOESY; 3D_15N
REMARK 210 -SEPARATED_NOESY; HNCA; HN(CO)CA;
REMARK 210 HCC(CO)NH
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : AMX; DMX; DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 2.5, PRONTO3D 19990506,
REMARK 210 TALOS 1999.019.15.47, NMR2ST 1.1
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING
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: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY.
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 HG1 THR A 34 O TYR A 106 1.44
REMARK 500 O VAL B 183 HD2 ASP B 184 1.50
REMARK 500 O MET A 6 HG SER A 7 1.52
REMARK 500 OG1 THR A 51 HG SER A 60 1.60
REMARK 500
REMARK 500 REMARK: NULL
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 GLU A 12 CD GLU A 12 OE2 0.114
REMARK 500 GLU A 21 CD GLU A 21 OE2 0.113
REMARK 500 GLU A 22 CD GLU A 22 OE2 0.111
REMARK 500 GLU A 25 CD GLU A 25 OE2 0.111
REMARK 500 GLU A 83 CD GLU A 83 OE2 0.113
REMARK 500 GLU A 91 CD GLU A 91 OE2 0.110
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 15 CD1 - NE1 - CE2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ASP A 17 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 17 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ARG A 20 NE - CZ - NH1 ANGL. DEV. = 3.8 DEGREES
REMARK 500 ARG A 20 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG A 28 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG A 28 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ASP A 29 CB - CG - OD2 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP A 32 CB - CG - OD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 ARG A 38 NE - CZ - NH1 ANGL. DEV. = 3.9 DEGREES
REMARK 500 ARG A 38 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ASP A 39 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 39 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 HIS A 45 ND1 - CE1 - NE2 ANGL. DEV. = 8.4 DEGREES
REMARK 500 ASP A 47 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 47 CB - CG - OD2 ANGL. DEV. = -6.3 DEGREES
REMARK 500 ARG A 53 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 HIS A 65 ND1 - CE1 - NE2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 ARG A 66 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ASP A 67 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 67 CB - CG - OD2 ANGL. DEV. = -5.9 DEGREES
REMARK 500 ASP A 74 CB - CG - OD2 ANGL. DEV. = -5.6 DEGREES
REMARK 500 HIS A 87 ND1 - CE1 - NE2 ANGL. DEV. = 8.5 DEGREES
REMARK 500 ARG A 89 NE - CZ - NH1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG A 89 NE - CZ - NH2 ANGL. DEV. = -3.7 DEGREES
REMARK 500 TYR A 96 CB - CG - CD2 ANGL. DEV. = -3.6 DEGREES
REMARK 500 ASP A 101 CB - CG - OD2 ANGL. DEV. = -5.7 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 MET A 2 -70.77 -159.50
REMARK 500 ASN A 5 -46.43 -147.81
REMARK 500 MET A 6 74.51 68.98
REMARK 500 SER A 7 88.65 -166.03
REMARK 500 LEU A 8 -73.54 -168.09
REMARK 500 ASP A 10 75.40 -119.33
REMARK 500 ALA A 11 -108.02 -92.87
REMARK 500 GLU A 12 -76.51 -94.94
REMARK 500 LEU A 27 -107.71 -160.39
REMARK 500 THR A 42 -68.28 -154.21
REMARK 500 MET A 44 -102.16 62.84
REMARK 500 TYR A 48 63.55 -110.25
REMARK 500 ILE A 63 -99.04 -104.14
REMARK 500 PHE A 64 127.85 97.11
REMARK 500 HIS A 65 95.55 -67.98
REMARK 500 LYS A 69 79.35 74.34
REMARK 500 PHE A 72 89.65 -69.70
REMARK 500 SER A 73 75.96 -102.28
REMARK 500 ASP A 74 -76.37 -118.61
REMARK 500 GLU A 91 -89.77 -150.63
REMARK 500 ASN A 97 -61.87 167.67
REMARK 500 LEU A 105 -78.48 -94.41
REMARK 500 ASP B 184 -90.81 -145.02
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 53 0.12 SIDE CHAIN
REMARK 500 TYR A 96 0.09 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1OO3 RELATED DB: PDB
REMARK 900 P395S MUTANT OF THE P85 REGULATORY SUBUNIT OF THE N-TERMINAL SRC
REMARK 900 HOMOLOGY 2 DOMAIN OF PI3-KINASE
DBREF 1OO4 A 1 111 UNP P23727 P85A_BOVIN 321 431
DBREF 1OO4 B 182 189 PDB 1OO4 1OO4 182 189
SEQADV 1OO4 SER A 60 UNP P23727 LEU 380 CONFLICT
SEQADV 1OO4 SER A 75 UNP P23727 PRO 395 ENGINEERED MUTATION
SEQRES 1 A 111 GLY MET ASN ASN ASN MET SER LEU GLN ASP ALA GLU TRP
SEQRES 2 A 111 TYR TRP GLY ASP ILE SER ARG GLU GLU VAL ASN GLU LYS
SEQRES 3 A 111 LEU ARG ASP THR ALA ASP GLY THR PHE LEU VAL ARG ASP
SEQRES 4 A 111 ALA SER THR LYS MET HIS GLY ASP TYR THR LEU THR LEU
SEQRES 5 A 111 ARG LYS GLY GLY ASN ASN LYS SER ILE LYS ILE PHE HIS
SEQRES 6 A 111 ARG ASP GLY LYS TYR GLY PHE SER ASP SER LEU THR PHE
SEQRES 7 A 111 ASN SER VAL VAL GLU LEU ILE ASN HIS TYR ARG ASN GLU
SEQRES 8 A 111 SER LEU ALA GLN TYR ASN PRO LYS LEU ASP VAL LYS LEU
SEQRES 9 A 111 LEU TYR PRO VAL SER LYS TYR
SEQRES 1 B 8 SER VAL ASP PTR VAL PRO MET LEU
MODRES 1OO4 PTR B 185 TYR O-PHOSPHOTYROSINE
HET PTR B 185 25
HETNAM PTR O-PHOSPHOTYROSINE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 2 PTR C9 H12 N O6 P
HELIX 1 1 SER A 19 GLU A 25 1 7
HELIX 2 2 SER A 80 ASN A 90 1 11
HELIX 3 3 SER A 92 TYR A 96 5 5
SHEET 1 A 3 ASP A 32 ALA A 40 0
SHEET 2 A 3 GLY A 46 LYS A 54 -1 O THR A 51 N LEU A 36
SHEET 3 A 3 ASN A 58 LYS A 62 -1 O ILE A 61 N LEU A 50
LINK C ASP B 184 N PTR B 185 1555 1555 1.35
LINK C PTR B 185 N VAL B 186 1555 1555 1.35
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 - 10 20 Bytes