Header list of 1a0n.pdb file
Complete list - b 16 2 Bytes
HEADER COMPLEX (PHOSPHOTRANSFERASE/PEPTIDE) 05-DEC-97 1A0N
TITLE NMR STUDY OF THE SH3 DOMAIN FROM FYN PROTO-ONCOGENE TYROSINE KINASE
TITLE 2 COMPLEXED WITH THE SYNTHETIC PEPTIDE P2L CORRESPONDING TO RESIDUES
TITLE 3 91-104 OF THE P85 SUBUNIT OF PI3-KINASE, FAMILY OF 25 STRUCTURES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PRO-PRO-ARG-PRO-LEU-PRO-VAL-ALA-PRO-GLY-SER-SER-LYS-THR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: P85 SUBUNIT OF PI3-KINASE, RESIDUES 91 - 104;
COMPND 5 SYNONYM: P2L;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: FYN;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: SH3 DOMAIN, RESIDUES 82 - 148;
COMPND 11 EC: 2.7.1.112;
COMPND 12 ENGINEERED: YES;
COMPND 13 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 MOL_ID: 2;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX
KEYWDS COMPLEX (PHOSPHOTRANSFERASE-PEPTIDE), SH3 DOMAIN, POLYPROLINE-
KEYWDS 2 BINDING, COMPLEX (PHOSPHOTRANSFERASE-PEPTIDE) COMPLEX
EXPDTA SOLUTION NMR
NUMMDL 25
AUTHOR D.A.RENZONI,D.J.R.PUGH,G.SILIGARDI,P.DAS,C.J.MORTON,C.ROSSI,
AUTHOR 2 M.D.WATERFIELD,I.D.CAMPBELL,J.E.LADBURY
REVDAT 3 16-FEB-22 1A0N 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1A0N 1 VERSN
REVDAT 1 25-FEB-98 1A0N 0
JRNL AUTH D.A.RENZONI,D.J.PUGH,G.SILIGARDI,P.DAS,C.J.MORTON,C.ROSSI,
JRNL AUTH 2 M.D.WATERFIELD,I.D.CAMPBELL,J.E.LADBURY
JRNL TITL STRUCTURAL AND THERMODYNAMIC CHARACTERIZATION OF THE
JRNL TITL 2 INTERACTION OF THE SH3 DOMAIN FROM FYN WITH THE PROLINE-RICH
JRNL TITL 3 BINDING SITE ON THE P85 SUBUNIT OF PI3-KINASE.
JRNL REF BIOCHEMISTRY V. 35 15646 1996
JRNL REFN ISSN 0006-2960
JRNL PMID 8961927
JRNL DOI 10.1021/BI9620969
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH C.J.MORTON,D.J.PUGH,E.L.BROWN,J.D.KAHMANN,D.A.RENZONI,
REMARK 1 AUTH 2 I.D.CAMPBELL
REMARK 1 TITL SOLUTION STRUCTURE AND PEPTIDE BINDING OF THE SH3 DOMAIN
REMARK 1 TITL 2 FROM HUMAN FYN
REMARK 1 REF STRUCTURE V. 4 705 1996
REMARK 1 REFN ISSN 0969-2126
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.1
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1A0N 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_1000170245.
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 : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 25
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 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 1-25
REMARK 465 RES C SSSEQI
REMARK 465 GLY B 80
REMARK 465 SER B 81
REMARK 465 THR B 82
REMARK 465 GLY B 83
REMARK 465 ASP B 152
REMARK 465 SER B 153
REMARK 465 ILE B 154
REMARK 465 GLN B 155
REMARK 465 ALA B 156
REMARK 465 GLU B 157
REMARK 465 GLU B 158
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 PRO A 94 0.87 -66.47
REMARK 500 1 LEU A 95 96.47 -33.95
REMARK 500 1 PRO A 99 -162.01 -61.04
REMARK 500 1 SER A 102 -162.93 42.88
REMARK 500 1 THR B 85 59.33 -156.27
REMARK 500 1 ASP B 110 173.98 -57.78
REMARK 500 1 PRO B 150 109.88 -58.77
REMARK 500 2 ARG A 93 83.43 -173.89
REMARK 500 2 LEU A 95 133.16 -22.80
REMARK 500 2 VAL A 97 34.05 -93.75
REMARK 500 2 ALA A 98 168.23 54.77
REMARK 500 2 SER A 101 44.13 -92.28
REMARK 500 2 SER A 102 93.11 -177.68
REMARK 500 2 THR B 85 64.04 -158.19
REMARK 500 2 ASP B 128 24.63 48.84
REMARK 500 2 THR B 136 -64.12 -109.02
REMARK 500 3 ARG A 93 75.20 -159.13
REMARK 500 3 LEU A 95 143.04 74.13
REMARK 500 3 SER A 101 -76.23 77.41
REMARK 500 3 SER A 102 136.37 64.29
REMARK 500 3 LYS A 103 -52.63 -121.58
REMARK 500 3 ALA B 105 91.18 -68.32
REMARK 500 3 SER B 125 -38.73 -161.09
REMARK 500 4 PRO A 92 83.27 -61.96
REMARK 500 4 ARG A 93 57.80 -146.81
REMARK 500 4 PRO A 94 105.60 -59.28
REMARK 500 4 LEU A 95 150.19 -45.02
REMARK 500 4 SER A 101 108.67 61.29
REMARK 500 4 ALA B 105 108.00 -42.34
REMARK 500 4 SER B 125 36.42 -172.13
REMARK 500 4 GLU B 126 44.67 -140.05
REMARK 500 4 THR B 136 -72.66 -91.24
REMARK 500 5 PRO A 92 82.36 -62.53
REMARK 500 5 ARG A 93 86.69 40.87
REMARK 500 5 LEU A 95 98.34 65.40
REMARK 500 5 PRO A 96 -164.73 -63.04
REMARK 500 5 SER A 101 -154.30 60.27
REMARK 500 5 SER B 125 -72.08 -143.01
REMARK 500 6 LEU A 95 101.07 62.49
REMARK 500 6 PRO A 96 -165.80 -60.78
REMARK 500 6 PRO A 99 -157.55 -60.99
REMARK 500 6 SER A 102 -50.67 -123.47
REMARK 500 6 THR B 85 73.64 -161.15
REMARK 500 6 PHE B 113 -166.93 -169.23
REMARK 500 6 SER B 125 -68.76 -101.63
REMARK 500 7 ARG A 93 97.49 -177.56
REMARK 500 7 LEU A 95 156.26 -47.21
REMARK 500 7 SER A 101 69.31 61.09
REMARK 500 7 THR B 85 75.52 -166.13
REMARK 500 7 THR B 107 -168.57 -160.31
REMARK 500
REMARK 500 THIS ENTRY HAS 179 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 93 0.30 SIDE CHAIN
REMARK 500 1 ARG B 106 0.31 SIDE CHAIN
REMARK 500 1 ARG B 133 0.31 SIDE CHAIN
REMARK 500 2 ARG A 93 0.30 SIDE CHAIN
REMARK 500 2 ARG B 106 0.25 SIDE CHAIN
REMARK 500 2 ARG B 133 0.29 SIDE CHAIN
REMARK 500 3 ARG A 93 0.24 SIDE CHAIN
REMARK 500 3 ARG B 106 0.24 SIDE CHAIN
REMARK 500 3 ARG B 133 0.25 SIDE CHAIN
REMARK 500 4 ARG A 93 0.27 SIDE CHAIN
REMARK 500 4 ARG B 106 0.28 SIDE CHAIN
REMARK 500 4 ARG B 133 0.30 SIDE CHAIN
REMARK 500 5 ARG A 93 0.22 SIDE CHAIN
REMARK 500 5 ARG B 106 0.29 SIDE CHAIN
REMARK 500 5 ARG B 133 0.24 SIDE CHAIN
REMARK 500 6 ARG B 106 0.32 SIDE CHAIN
REMARK 500 6 ARG B 133 0.32 SIDE CHAIN
REMARK 500 7 ARG A 93 0.30 SIDE CHAIN
REMARK 500 7 ARG B 106 0.20 SIDE CHAIN
REMARK 500 7 ARG B 133 0.10 SIDE CHAIN
REMARK 500 8 ARG A 93 0.22 SIDE CHAIN
REMARK 500 8 ARG B 106 0.26 SIDE CHAIN
REMARK 500 8 ARG B 133 0.32 SIDE CHAIN
REMARK 500 9 ARG A 93 0.19 SIDE CHAIN
REMARK 500 9 ARG B 106 0.29 SIDE CHAIN
REMARK 500 9 ARG B 133 0.22 SIDE CHAIN
REMARK 500 10 ARG A 93 0.22 SIDE CHAIN
REMARK 500 10 ARG B 106 0.23 SIDE CHAIN
REMARK 500 10 ARG B 133 0.30 SIDE CHAIN
REMARK 500 11 ARG A 93 0.29 SIDE CHAIN
REMARK 500 11 ARG B 106 0.31 SIDE CHAIN
REMARK 500 11 ARG B 133 0.30 SIDE CHAIN
REMARK 500 12 ARG A 93 0.24 SIDE CHAIN
REMARK 500 12 ARG B 133 0.28 SIDE CHAIN
REMARK 500 13 ARG A 93 0.29 SIDE CHAIN
REMARK 500 13 ARG B 106 0.24 SIDE CHAIN
REMARK 500 14 ARG A 93 0.20 SIDE CHAIN
REMARK 500 14 ARG B 106 0.28 SIDE CHAIN
REMARK 500 14 ARG B 133 0.31 SIDE CHAIN
REMARK 500 15 ARG A 93 0.19 SIDE CHAIN
REMARK 500 15 ARG B 106 0.31 SIDE CHAIN
REMARK 500 15 ARG B 133 0.14 SIDE CHAIN
REMARK 500 16 ARG A 93 0.22 SIDE CHAIN
REMARK 500 16 ARG B 106 0.31 SIDE CHAIN
REMARK 500 16 ARG B 133 0.18 SIDE CHAIN
REMARK 500 17 ARG A 93 0.23 SIDE CHAIN
REMARK 500 17 ARG B 106 0.10 SIDE CHAIN
REMARK 500 17 ARG B 133 0.28 SIDE CHAIN
REMARK 500 18 ARG B 106 0.23 SIDE CHAIN
REMARK 500 18 ARG B 133 0.18 SIDE CHAIN
REMARK 500
REMARK 500 THIS ENTRY HAS 70 PLANE DEVIATIONS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1A0N A 91 104 UNP P27986 P85A_HUMAN 91 104
DBREF 1A0N B 80 158 UNP P06241 FYN_HUMAN 79 147
SEQADV 1A0N SER B 81 UNP P06241 GLY 80 CONFLICT
SEQRES 1 A 14 PRO PRO ARG PRO LEU PRO VAL ALA PRO GLY SER SER LYS
SEQRES 2 A 14 THR
SEQRES 1 B 69 GLY SER THR GLY VAL THR LEU PHE VAL ALA LEU TYR ASP
SEQRES 2 B 69 TYR GLU ALA ARG THR GLU ASP ASP LEU SER PHE HIS LYS
SEQRES 3 B 69 GLY GLU LYS PHE GLN ILE LEU ASN SER SER GLU GLY ASP
SEQRES 4 B 69 TRP TRP GLU ALA ARG SER LEU THR THR GLY GLU THR GLY
SEQRES 5 B 69 TYR ILE PRO SER ASN TYR VAL ALA PRO VAL ASP SER ILE
SEQRES 6 B 69 GLN ALA GLU GLU
HELIX 1 1 SER B 145 TYR B 147 5 3
SHEET 1 A 5 VAL B 148 PRO B 150 0
SHEET 2 A 5 LEU B 86 ALA B 89 -1 N VAL B 88 O ALA B 149
SHEET 3 A 5 LYS B 118 ASN B 123 -1 N PHE B 119 O PHE B 87
SHEET 4 A 5 TRP B 129 ARG B 133 -1 N ARG B 133 O GLN B 120
SHEET 5 A 5 THR B 140 PRO B 144 -1 N ILE B 143 O TRP B 130
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