Header list of 2ple.pdb file
Complete list - v 29 2 Bytes
HEADER PHOSPHORIC DIESTER HYDROLASE 19-AUG-94 2PLE
TITLE NUCLEAR MAGNETIC RESONANCE STRUCTURE OF AN SH2 DOMAIN OF PHOSPHOLIPASE
TITLE 2 C-GAMMA1 COMPLEXED WITH A HIGH AFFINITY BINDING PEPTIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PHOSPHOLIPASE C GAMMA-1, C-TERMINAL SH2 DOMAIN;
COMPND 3 CHAIN: A;
COMPND 4 EC: 3.1.4.11;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: PHOSPHOPEPTIDE FROM PDGF;
COMPND 8 CHAIN: B;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913;
SOURCE 5 MOL_ID: 2;
SOURCE 6 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 7 ORGANISM_COMMON: CATTLE;
SOURCE 8 ORGANISM_TAXID: 9913
KEYWDS PHOSPHORIC DIESTER HYDROLASE
EXPDTA SOLUTION NMR
NUMMDL 18
AUTHOR S.M.PASCAL,A.U.SINGER,G.GISH,T.YAMAZAKI,S.E.SHOELSON,T.PAWSON,
AUTHOR 2 L.E.KAY,J.D.FORMAN-KAY
REVDAT 3 29-NOV-17 2PLE 1 REMARK HELIX
REVDAT 2 24-FEB-09 2PLE 1 VERSN
REVDAT 1 26-JAN-95 2PLE 0
JRNL AUTH S.M.PASCAL,A.U.SINGER,G.GISH,T.YAMAZAKI,S.E.SHOELSON,
JRNL AUTH 2 T.PAWSON,L.E.KAY,J.D.FORMAN-KAY
JRNL TITL NUCLEAR MAGNETIC RESONANCE STRUCTURE OF AN SH2 DOMAIN OF
JRNL TITL 2 PHOSPHOLIPASE C-GAMMA 1 COMPLEXED WITH A HIGH AFFINITY
JRNL TITL 3 BINDING PEPTIDE.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 77 461 1994
JRNL REFN ISSN 0092-8674
JRNL PMID 8181064
JRNL DOI 10.1016/0092-8674(94)90160-0
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 2PLE 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_1000178481.
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 : 18
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: 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 1 HIS A 6 -92.38 56.56
REMARK 500 1 LYS A 9 99.05 -172.77
REMARK 500 1 GLU A 10 -27.94 171.31
REMARK 500 1 ALA A 14 44.23 -167.72
REMARK 500 1 SER A 15 -65.97 -163.38
REMARK 500 1 ARG A 30 87.25 53.18
REMARK 500 1 ASP A 31 145.25 68.14
REMARK 500 1 ARG A 39 -154.29 -101.39
REMARK 500 1 ASN A 40 36.81 -88.53
REMARK 500 1 GLU A 41 154.53 175.13
REMARK 500 1 SER A 44 136.00 165.83
REMARK 500 1 GLU A 52 -95.49 50.54
REMARK 500 1 ILE A 55 128.56 -13.81
REMARK 500 1 HIS A 57 -155.59 -97.39
REMARK 500 1 GLU A 63 -169.07 -113.71
REMARK 500 1 PHE A 74 84.25 -150.34
REMARK 500 1 LEU A 89 -75.19 -84.19
REMARK 500 1 TYR A 90 -148.18 -87.93
REMARK 500 1 LYS A 92 -41.98 -169.05
REMARK 500 1 MET A 93 157.33 -48.30
REMARK 500 1 LYS A 94 17.90 -154.50
REMARK 500 1 LEU A 95 29.10 48.45
REMARK 500 1 TYR A 97 78.95 -118.17
REMARK 500 1 GLU A 102 -38.22 -165.14
REMARK 500 1 ASN A 103 35.12 -158.73
REMARK 500 1 PTR B 4 145.31 -178.57
REMARK 500 1 ASP B 10 158.10 165.03
REMARK 500 2 GLU A 10 -51.34 -152.20
REMARK 500 2 TRP A 11 24.99 43.39
REMARK 500 2 ALA A 14 -81.55 -154.47
REMARK 500 2 LEU A 16 -172.50 -176.27
REMARK 500 2 THR A 17 94.67 -42.48
REMARK 500 2 ARG A 18 -98.27 -62.01
REMARK 500 2 ARG A 30 -163.16 67.74
REMARK 500 2 ASP A 31 100.63 -163.17
REMARK 500 2 ARG A 39 -144.84 -74.12
REMARK 500 2 ASN A 40 46.00 -86.99
REMARK 500 2 PRO A 42 -78.63 -84.21
REMARK 500 2 ASN A 43 59.31 178.61
REMARK 500 2 SER A 44 -166.46 166.61
REMARK 500 2 GLU A 63 72.88 -154.20
REMARK 500 2 PHE A 74 -165.92 -119.86
REMARK 500 2 ASP A 75 14.92 -153.58
REMARK 500 2 LEU A 89 -71.86 -84.80
REMARK 500 2 LYS A 92 -94.64 168.56
REMARK 500 2 LYS A 94 -159.08 -155.16
REMARK 500 2 LEU A 95 39.53 -89.78
REMARK 500 2 ILE A 99 -169.03 -166.02
REMARK 500 2 ASN A 100 -103.05 -109.40
REMARK 500 2 GLU A 101 76.89 -165.42
REMARK 500
REMARK 500 THIS ENTRY HAS 452 RAMACHANDRAN OUTLIERS.
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 1 ARG A 18 0.10 SIDE CHAIN
REMARK 500 1 ARG A 27 0.23 SIDE CHAIN
REMARK 500 1 ARG A 30 0.32 SIDE CHAIN
REMARK 500 1 ARG A 37 0.19 SIDE CHAIN
REMARK 500 1 ARG A 39 0.28 SIDE CHAIN
REMARK 500 1 ARG A 50 0.21 SIDE CHAIN
REMARK 500 1 ARG A 59 0.32 SIDE CHAIN
REMARK 500 1 ARG A 91 0.14 SIDE CHAIN
REMARK 500 1 ARG A 96 0.28 SIDE CHAIN
REMARK 500 2 ARG A 27 0.27 SIDE CHAIN
REMARK 500 2 ARG A 30 0.16 SIDE CHAIN
REMARK 500 2 ARG A 37 0.29 SIDE CHAIN
REMARK 500 2 ARG A 50 0.09 SIDE CHAIN
REMARK 500 2 ARG A 59 0.30 SIDE CHAIN
REMARK 500 2 ARG A 91 0.29 SIDE CHAIN
REMARK 500 2 ARG A 96 0.30 SIDE CHAIN
REMARK 500 3 ARG A 18 0.29 SIDE CHAIN
REMARK 500 3 ARG A 27 0.20 SIDE CHAIN
REMARK 500 3 ARG A 30 0.11 SIDE CHAIN
REMARK 500 3 ARG A 37 0.17 SIDE CHAIN
REMARK 500 3 ARG A 39 0.14 SIDE CHAIN
REMARK 500 3 ARG A 50 0.24 SIDE CHAIN
REMARK 500 3 ARG A 59 0.30 SIDE CHAIN
REMARK 500 3 ARG A 91 0.13 SIDE CHAIN
REMARK 500 3 ARG A 96 0.27 SIDE CHAIN
REMARK 500 4 ARG A 18 0.31 SIDE CHAIN
REMARK 500 4 ARG A 27 0.21 SIDE CHAIN
REMARK 500 4 ARG A 30 0.31 SIDE CHAIN
REMARK 500 4 ARG A 37 0.21 SIDE CHAIN
REMARK 500 4 ARG A 39 0.10 SIDE CHAIN
REMARK 500 4 ARG A 50 0.25 SIDE CHAIN
REMARK 500 4 ARG A 59 0.24 SIDE CHAIN
REMARK 500 4 ARG A 91 0.20 SIDE CHAIN
REMARK 500 4 ARG A 96 0.25 SIDE CHAIN
REMARK 500 5 ARG A 18 0.30 SIDE CHAIN
REMARK 500 5 ARG A 27 0.29 SIDE CHAIN
REMARK 500 5 ARG A 30 0.27 SIDE CHAIN
REMARK 500 5 ARG A 37 0.29 SIDE CHAIN
REMARK 500 5 ARG A 39 0.24 SIDE CHAIN
REMARK 500 5 ARG A 50 0.22 SIDE CHAIN
REMARK 500 5 ARG A 59 0.32 SIDE CHAIN
REMARK 500 5 ARG A 91 0.29 SIDE CHAIN
REMARK 500 5 ARG A 96 0.30 SIDE CHAIN
REMARK 500 6 ARG A 18 0.23 SIDE CHAIN
REMARK 500 6 ARG A 27 0.17 SIDE CHAIN
REMARK 500 6 ARG A 30 0.31 SIDE CHAIN
REMARK 500 6 ARG A 37 0.32 SIDE CHAIN
REMARK 500 6 ARG A 39 0.32 SIDE CHAIN
REMARK 500 6 ARG A 50 0.26 SIDE CHAIN
REMARK 500 6 ARG A 59 0.28 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 150 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2PLD RELATED DB: PDB
DBREF 2PLE A 6 102 UNP P08487 PLCG1_BOVIN 663 759
DBREF 2PLE B 1 12 UNP P09619 PGDR_HUMAN 1018 1029
SEQRES 1 A 105 GLY SER PRO GLY ILE HIS GLU SER LYS GLU TRP TYR HIS
SEQRES 2 A 105 ALA SER LEU THR ARG ALA GLN ALA GLU HIS MET LEU MET
SEQRES 3 A 105 ARG VAL PRO ARG ASP GLY ALA PHE LEU VAL ARG LYS ARG
SEQRES 4 A 105 ASN GLU PRO ASN SER TYR ALA ILE SER PHE ARG ALA GLU
SEQRES 5 A 105 GLY LYS ILE LYS HIS CYS ARG VAL GLN GLN GLU GLY GLN
SEQRES 6 A 105 THR VAL MET LEU GLY ASN SER GLU PHE ASP SER LEU VAL
SEQRES 7 A 105 ASP LEU ILE SER TYR TYR GLU LYS HIS PRO LEU TYR ARG
SEQRES 8 A 105 LYS MET LYS LEU ARG TYR PRO ILE ASN GLU GLU ASN SER
SEQRES 9 A 105 SER
SEQRES 1 B 12 ASP ASN ASP PTR ILE ILE PRO LEU PRO ASP PRO LYS
MODRES 2PLE PTR B 4 TYR O-PHOSPHOTYROSINE
HET PTR B 4 24
HETNAM PTR O-PHOSPHOTYROSINE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 2 PTR C9 H12 N O6 P
HELIX 1 A THR A 17 VAL A 28 1 12
HELIX 2 B LEU A 77 HIS A 87 1SL.IRR., BIFURCATED H-BONDS 11
SHEET 1 S1 4 TRP A 11 HIS A 13 0
SHEET 2 S1 4 PHE A 34 LYS A 38 1 O VAL A 36 N HIS A 13
SHEET 3 S1 4 TYR A 45 ALA A 51 -1 O SER A 48 N LEU A 35
SHEET 4 S1 4 LYS A 54 VAL A 60 -1 O CYS A 58 N ILE A 47
SHEET 1 ASC 3 GLN A 61 GLU A 63 0
SHEET 2 ASC 3 THR A 66 LEU A 69 -1 O MET A 68 N GLN A 61
SHEET 3 ASC 3 SER A 72 PHE A 74 -1 N PHE A 74 O VAL A 67
LINK C ASP B 3 N PTR B 4 1555 1555 1.31
LINK C PTR B 4 N ILE B 5 1555 1555 1.31
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 - v 29 2 Bytes