Header list of 1bfi.pdb file
Complete list - b 16 2 Bytes
HEADER SH2 DOMAIN 18-NOV-97 1BFI
TITLE SOLUTION STRUCTURE OF THE C-TERMINAL SH2 DOMAIN OF THE P85ALPHA
TITLE 2 REGULATORY SUBUNIT OF PHOSPHOINOSITIDE 3-KINASE, NMR, 30 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: P85 ALPHA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C TERMINAL SH2 DOMAIN;
COMPND 5 SYNONYM: PHOSPHATIDYLINOSITOL 3-KINASE REGULATORY ALPHA SUBUNIT, PI3-
COMPND 6 KINASE P85-ALPHA SUBUNIT;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 CELL_LINE: BL21;
SOURCE 6 ORGAN: BRAIN;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 10 EXPRESSION_SYSTEM_VECTOR: PET-23D;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: BL21
KEYWDS SH2 DOMAIN, P85ALPHA, PI 3-KINASE, C TERMINAL SH2 DOMAIN
EXPDTA SOLUTION NMR
NUMMDL 30
AUTHOR G.SIEGAL,B.DAVIS,S.M.KRISTENSEN,A.SANKAR,J.LINACRE,R.C.STEIN,
AUTHOR 2 G.PANAYOTOU,M.D.WATERFIELD,P.C.DRISCOLL
REVDAT 3 16-FEB-22 1BFI 1 REMARK
REVDAT 2 24-FEB-09 1BFI 1 VERSN
REVDAT 1 25-FEB-98 1BFI 0
JRNL AUTH G.SIEGAL,B.DAVIS,S.M.KRISTENSEN,A.SANKAR,J.LINACRE,
JRNL AUTH 2 R.C.STEIN,G.PANAYOTOU,M.D.WATERFIELD,P.C.DRISCOLL
JRNL TITL SOLUTION STRUCTURE OF THE C-TERMINAL SH2 DOMAIN OF THE P85
JRNL TITL 2 ALPHA REGULATORY SUBUNIT OF PHOSPHOINOSITIDE 3-KINASE.
JRNL REF J.MOL.BIOL. V. 276 461 1998
JRNL REFN ISSN 0022-2836
JRNL PMID 9512716
JRNL DOI 10.1006/JMBI.1997.1562
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.84
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 30 CONFORMERS WERE DETERMINED BY
REMARK 3 RESTRAINED MOLECULAR DYNAMICS/SIMULATED ANNEALING METHOD USING
REMARK 3 THE PROGRAM X-PLOR 3.84. THE STRUCTURES ARE BASED ON 1908
REMARK 3 INTERPROTON DISTANCE RESTRAINTS DERIVED FROM NOE MEASUREMENTS;
REMARK 3 88 HYDROGEN-BONDING DISTANCE RESTRAINTS FOR 44 HYDROGEN-BONDS
REMARK 3 IDENTIFIED ON THE BASIS OF THE NOE AND AMIDE PROTON EXCHANGE
REMARK 3 DATA; 25 TORSION ANGLE RESTRAINTS DERIVED FROM COUPLING
REMARK 3 CONSTANTS AND NOE DATA. THE RMS DISTRIBUTION ABOUT THE MEAN
REMARK 3 COORDINATE POSITIONS IS 0.57 ANGSTROMS FOR ALL BACKBONE ATOMS
REMARK 3 AND 1.12 ANGSTROMS FOR ALL ATOMS. THE AVERAGE STRUCTURE WAS THEN
REMARK 3 CALCULATED BY BEST FIT SUPERPOSITION, COORDINATE AVERAGING AND
REMARK 3 RESTRAINED ENERGY MINIMIZATION.
REMARK 4
REMARK 4 1BFI 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_1000171693.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 290
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : 50 MM
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : VARIOUS
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITYPLUS
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XPLOR
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 30
REMARK 210 CONFORMERS, SELECTION CRITERIA : NO NOE VIOLATION > 0.3A, NO
REMARK 210 DIHEDRAL VIOLATION > 3.0
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 MODELS 1-30
REMARK 465 RES C SSSEQI
REMARK 465 MET A 0
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 H GLU A 70 OD1 ASN A 73 1.33
REMARK 500 O TRP A 11 H VAL A 35 1.49
REMARK 500 O LEU A 90 H HIS A 93 1.56
REMARK 500 O ALA A 21 H LEU A 25 1.59
REMARK 500 O GLU A 70 O ASN A 73 2.15
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 12 ARG A 110 CZ ARG A 110 NH2 0.678
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 12 ARG A 110 NH1 - CZ - NH2 ANGL. DEV. = -25.2 DEGREES
REMARK 500 12 ARG A 110 NE - CZ - NH2 ANGL. DEV. = 25.7 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 1 SER A 39 -77.45 85.19
REMARK 500 1 ALA A 63 -35.78 -37.55
REMARK 500 1 TYR A 66 -8.17 -168.07
REMARK 500 1 ALA A 69 97.05 176.80
REMARK 500 1 ASN A 94 7.73 58.22
REMARK 500 1 SER A 96 15.48 -156.95
REMARK 500 1 LEU A 97 73.91 -101.62
REMARK 500 1 LEU A 101 95.57 -52.43
REMARK 500 2 SER A 39 131.03 97.86
REMARK 500 2 LYS A 40 -143.77 62.32
REMARK 500 2 ASP A 51 -17.17 -49.97
REMARK 500 2 GLU A 53 -165.53 -163.22
REMARK 500 2 TYR A 66 30.80 -64.44
REMARK 500 2 TYR A 75 175.02 60.58
REMARK 500 2 VAL A 91 -33.75 -36.66
REMARK 500 2 ASP A 95 -24.35 -35.98
REMARK 500 3 SER A 39 -37.58 112.76
REMARK 500 3 GLN A 41 -16.95 -47.94
REMARK 500 3 ASP A 51 24.28 40.88
REMARK 500 3 TYR A 66 -178.95 46.75
REMARK 500 3 PHE A 68 -58.80 -131.20
REMARK 500 3 ASN A 73 141.75 64.02
REMARK 500 3 LEU A 74 -118.15 -74.17
REMARK 500 3 VAL A 91 -75.24 12.31
REMARK 500 3 GLN A 92 -175.98 62.63
REMARK 500 3 ASP A 95 14.60 60.00
REMARK 500 3 LEU A 97 36.57 -96.58
REMARK 500 4 ARG A 36 -141.91 -146.11
REMARK 500 4 SER A 39 -43.47 101.97
REMARK 500 4 ASP A 51 -18.30 -49.30
REMARK 500 4 TYR A 66 177.62 56.66
REMARK 500 4 LEU A 74 84.20 43.60
REMARK 500 4 GLN A 92 -36.63 -38.58
REMARK 500 4 ASN A 94 9.71 44.28
REMARK 500 4 SER A 96 4.64 -151.61
REMARK 500 4 LEU A 97 70.68 -100.47
REMARK 500 4 VAL A 99 -177.81 -174.06
REMARK 500 5 SER A 39 -17.20 99.71
REMARK 500 5 ASP A 51 20.52 48.44
REMARK 500 5 ALA A 63 -81.40 54.29
REMARK 500 5 TYR A 66 -163.51 -169.55
REMARK 500 5 VAL A 91 -53.20 -9.23
REMARK 500 5 GLN A 92 146.49 -36.41
REMARK 500 5 HIS A 93 -120.13 103.94
REMARK 500 6 SER A 39 -51.42 61.09
REMARK 500 6 GLN A 41 -173.60 85.25
REMARK 500 6 ASP A 51 60.14 -65.48
REMARK 500 6 THR A 62 55.66 -140.43
REMARK 500 6 ALA A 63 -47.29 63.40
REMARK 500 6 TYR A 66 -11.07 -168.32
REMARK 500
REMARK 500 THIS ENTRY HAS 301 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1BFJ RELATED DB: PDB
DBREF 1BFI A 1 111 UNP P23727 P85A_BOVIN 614 724
SEQRES 1 A 112 MET GLU ASP LEU 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
HELIX 1 1 PRO A 4 HIS A 6 5 3
HELIX 2 2 GLU A 8 TRP A 11 1 4
HELIX 3 3 ARG A 18 LEU A 25 1 8
HELIX 4 4 LEU A 78 HIS A 87 1 10
HELIX 5 5 LEU A 90 ASP A 95 5 6
SHEET 1 A 3 PHE A 33 GLU A 37 0
SHEET 2 A 3 TYR A 44 VAL A 49 -1 N SER A 47 O LEU A 34
SHEET 3 A 3 VAL A 54 ILE A 59 -1 N ILE A 59 O TYR A 44
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 - b 16 2 Bytes