Header list of 2pnb.pdb file
Complete list - 29 20 Bytes
HEADER SIGNALLING PROTEIN 30-JUN-92 2PNB
TITLE STRUCTURE OF AN SH2 DOMAIN OF THE P85 ALPHA SUBUNIT OF
TITLE 2 PHOSPHATIDYLINOSITOL-3-OH KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHATIDYLINOSITOL 3-KINASE P85-ALPHA SUBUNIT N-TERMINAL
COMPND 3 SH2 DOMAIN;
COMPND 4 CHAIN: A;
COMPND 5 EC: 2.7.1.137;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS SIGNALLING PROTEIN
EXPDTA SOLUTION NMR
AUTHOR G.W.BOOKER,A.L.BREEZE,A.K.DOWNING,G.PANAYOTOU,I.GOUT,M.D.WATERFIELD,
AUTHOR 2 I.D.CAMPBELL
REVDAT 3 29-NOV-17 2PNB 1 REMARK HELIX
REVDAT 2 24-FEB-09 2PNB 1 VERSN
REVDAT 1 31-JAN-94 2PNB 0
JRNL AUTH G.W.BOOKER,A.L.BREEZE,A.K.DOWNING,G.PANAYOTOU,I.GOUT,
JRNL AUTH 2 M.D.WATERFIELD,I.D.CAMPBELL
JRNL TITL STRUCTURE OF AN SH2 DOMAIN OF THE P85 ALPHA SUBUNIT OF
JRNL TITL 2 PHOSPHATIDYLINOSITOL-3-OH KINASE.
JRNL REF NATURE V. 358 684 1992
JRNL REFN ISSN 0028-0836
JRNL PMID 1323062
JRNL DOI 10.1038/358684A0
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 2PNB 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_1000178488.
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 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 TRP A 22 CG TRP A 22 CD2 -0.117
REMARK 500 TRP A 24 CG TRP A 24 CD2 -0.129
REMARK 500 HIS A 54 CG HIS A 54 ND1 -0.120
REMARK 500 HIS A 74 CG HIS A 74 ND1 -0.122
REMARK 500 HIS A 96 CG HIS A 96 ND1 -0.120
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 22 CG - CD1 - NE1 ANGL. DEV. = -6.0 DEGREES
REMARK 500 TRP A 22 NE1 - CE2 - CZ2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 TRP A 22 NE1 - CE2 - CD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 TRP A 24 CG - CD1 - NE1 ANGL. DEV. = -6.7 DEGREES
REMARK 500 TRP A 24 NE1 - CE2 - CZ2 ANGL. DEV. = 9.4 DEGREES
REMARK 500 TRP A 24 NE1 - CE2 - CD2 ANGL. DEV. = -7.3 DEGREES
REMARK 500 TRP A 24 CG - CD2 - CE3 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ARG A 29 CG - CD - NE ANGL. DEV. = 17.2 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 ASP A 19 -24.00 -170.09
REMARK 500 ALA A 20 170.78 53.03
REMARK 500 GLU A 21 -63.17 -108.36
REMARK 500 ASP A 26 119.92 68.77
REMARK 500 ILE A 27 -130.52 -140.56
REMARK 500 GLU A 34 -27.73 -36.32
REMARK 500 ASP A 38 76.10 -151.18
REMARK 500 ALA A 40 -169.16 -54.27
REMARK 500 ASP A 41 58.96 -104.94
REMARK 500 ALA A 49 67.24 -103.98
REMARK 500 LYS A 52 -19.49 -172.58
REMARK 500 MET A 53 17.78 49.69
REMARK 500 ASP A 56 -90.02 -85.87
REMARK 500 TYR A 57 -151.94 -138.53
REMARK 500 LYS A 63 45.16 -92.00
REMARK 500 ARG A 75 -67.88 -133.00
REMARK 500 PHE A 81 -29.06 -148.06
REMARK 500 SER A 82 -49.28 -146.23
REMARK 500 PRO A 84 50.44 -69.40
REMARK 500 LEU A 85 82.92 51.97
REMARK 500 THR A 86 -33.12 -149.37
REMARK 500 ASN A 88 20.68 45.71
REMARK 500 LEU A 93 -71.50 -67.36
REMARK 500 ILE A 94 -34.89 -39.73
REMARK 500 GLU A 100 -105.43 -100.53
REMARK 500 SER A 101 136.98 172.60
REMARK 500 TYR A 105 -83.66 -56.35
REMARK 500 PRO A 107 -171.99 -65.26
REMARK 500 LYS A 108 -13.04 56.64
REMARK 500 LEU A 109 -159.72 -151.38
REMARK 500 LEU A 114 39.64 -95.05
REMARK 500 SER A 118 -160.54 -172.39
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 29 0.32 SIDE CHAIN
REMARK 500 ARG A 47 0.29 SIDE CHAIN
REMARK 500 ARG A 62 0.12 SIDE CHAIN
REMARK 500 ARG A 75 0.29 SIDE CHAIN
REMARK 500 ARG A 98 0.14 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: PYB
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PNA RELATED DB: PDB
DBREF 2PNB A 17 120 UNP P23727 P85A_BOVIN 328 431
SEQRES 1 A 104 LEU GLN ASP ALA GLU TRP TYR TRP GLY ASP ILE SER ARG
SEQRES 2 A 104 GLU GLU VAL ASN GLU LYS LEU ARG ASP THR ALA ASP GLY
SEQRES 3 A 104 THR PHE LEU VAL ARG ASP ALA SER THR LYS MET HIS GLY
SEQRES 4 A 104 ASP TYR THR LEU THR LEU ARG LYS GLY GLY ASN ASN LYS
SEQRES 5 A 104 LEU ILE LYS ILE PHE HIS ARG ASP GLY LYS TYR GLY PHE
SEQRES 6 A 104 SER ASP PRO LEU THR PHE ASN SER VAL VAL GLU LEU ILE
SEQRES 7 A 104 ASN HIS TYR ARG ASN GLU SER LEU ALA GLN TYR ASN PRO
SEQRES 8 A 104 LYS LEU ASP VAL LYS LEU LEU TYR PRO VAL SER LYS TYR
HELIX 1 H1 SER A 28 ARG A 37 1 10
HELIX 2 H2 SER A 89 GLU A 100 1 12
SHEET 1 B1 3 THR A 43 ARG A 47 0
SHEET 2 B1 3 THR A 58 ARG A 62 -1 N THR A 58 O ARG A 47
SHEET 3 B1 3 ASN A 67 LYS A 71 -1 N LYS A 68 O LEU A 61
SHEET 1 B2 2 ILE A 72 HIS A 74 0
SHEET 2 B2 2 TYR A 79 PHE A 81 -1 N GLY A 80 O PHE A 73
SHEET 1 B3 2 SER A 101 ALA A 103 0
SHEET 2 B3 2 ASP A 110 LYS A 112 -1 N VAL A 111 O LEU A 102
SITE 1 PYB 3 ARG A 29 ARG A 47 LEU A 69
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 - 29 20 Bytes