Header list of 1gl5.pdb file
Complete list - b 28 2 Bytes
HEADER TRANSFERASE 28-AUG-01 1GL5
TITLE NMR STRUCTURE OF THE SH3 DOMAIN FROM THE TEC PROTEIN TYROSINE KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE TEC;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SH3 DOMAIN (181-245);
COMPND 5 EC: 2.7.1.112;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: N-TERMINAL GLY-SER FROM GLUTATHIONE S-TRANSFERASE
COMPND 8 FUSION PARTNER
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PGEX-4T-2;
SOURCE 8 OTHER_DETAILS: GST-FUSION
KEYWDS TRANSFERASE, TYROSINE-PROTEIN KINASE, ATP-BINDING, SH3 DOMAIN,
KEYWDS 2 PHOSPHORYLATION
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR T.D.MULHERN,S.E.PURSGLOVE,G.W.BOOKER
REVDAT 4 28-FEB-18 1GL5 1 SOURCE JRNL
REVDAT 3 24-FEB-09 1GL5 1 VERSN
REVDAT 2 20-DEC-06 1GL5 1 JRNL
REVDAT 1 28-NOV-01 1GL5 0
JRNL AUTH S.E.PURSGLOVE,T.D.MULHERN,J.P.MACKAY,M.G.HINDS,G.W.BOOKER
JRNL TITL THE SOLUTION STRUCTURE AND INTRAMOLECULAR ASSOCIATIONS OF
JRNL TITL 2 THE TEC KINASE SRC HOMOLOGY 3 DOMAIN.
JRNL REF J. BIOL. CHEM. V. 277 755 2002
JRNL REFN ISSN 0021-9258
JRNL PMID 11684687
JRNL DOI 10.1074/JBC.M108318200
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR 3.851
REMARK 3 AUTHORS : BRUNGER
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THESE COORDINATE SETS WERE REFINED IN
REMARK 3 EXPLICIT SOLVENT USING THE HYBRID CSDX/OPLS PARAMETER SET.
REMARK 3 DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE.
REMARK 4
REMARK 4 1GL5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-AUG-01.
REMARK 100 THE DEPOSITION ID IS D_1290008504.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : 1 ATM
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : COSY; TOCSY; NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : X-PLOR
REMARK 210 METHOD USED : ARIA
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING HETERONUCLEAR NMR
REMARK 210 SPECTROSCOPY ON 15N-LABELED SAMPLES
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: 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
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 GLU A 193 -96.64 -99.43
REMARK 500 1 ALA A 194 -38.11 -179.84
REMARK 500 1 LYS A 210 -102.47 -103.16
REMARK 500 1 ASN A 211 86.62 78.67
REMARK 500 1 ASP A 212 -165.51 63.82
REMARK 500 1 HIS A 214 -86.74 -85.28
REMARK 500 1 ASP A 220 -99.87 -77.78
REMARK 500 1 LYS A 221 -101.14 -91.92
REMARK 500 1 PRO A 229 98.24 -66.28
REMARK 500 1 LYS A 236 36.60 -82.93
REMARK 500 1 LYS A 237 62.41 38.55
REMARK 500 1 SER A 238 -130.15 60.45
REMARK 500 1 LEU A 241 47.61 -87.11
REMARK 500 1 TYR A 244 -57.74 73.64
REMARK 500 2 SER A 180 -179.15 63.68
REMARK 500 2 GLU A 193 -99.32 -114.39
REMARK 500 2 ALA A 194 -23.67 -167.81
REMARK 500 2 ASN A 211 -103.34 63.26
REMARK 500 2 ASP A 212 -150.92 -110.36
REMARK 500 2 LYS A 221 -140.32 -79.98
REMARK 500 2 LYS A 236 45.38 -98.82
REMARK 500 2 SER A 238 35.77 -84.97
REMARK 500 2 LEU A 241 -118.20 -161.60
REMARK 500 2 ASP A 242 -105.39 -171.43
REMARK 500 3 GLU A 193 -132.05 -124.80
REMARK 500 3 ALA A 194 -17.40 -142.06
REMARK 500 3 ASN A 211 -116.79 59.42
REMARK 500 3 LYS A 221 -92.58 -91.80
REMARK 500 3 TYR A 222 40.33 -155.71
REMARK 500 3 LYS A 236 51.78 -98.27
REMARK 500 3 LYS A 237 70.19 32.09
REMARK 500 3 ASN A 240 -82.46 63.74
REMARK 500 3 LEU A 241 110.88 67.99
REMARK 500 3 GLN A 243 -53.29 76.17
REMARK 500 4 GLU A 193 -100.47 -141.37
REMARK 500 4 ALA A 194 -16.02 -165.34
REMARK 500 4 LEU A 208 -66.80 -103.20
REMARK 500 4 ASN A 211 -71.65 -97.20
REMARK 500 4 ASP A 220 -74.07 -112.23
REMARK 500 4 LYS A 221 -141.88 -86.23
REMARK 500 4 TYR A 222 36.77 -79.08
REMARK 500 4 GLU A 225 -164.96 -121.69
REMARK 500 4 PRO A 229 98.82 -69.53
REMARK 500 4 LYS A 236 37.37 -85.06
REMARK 500 4 SER A 238 40.08 70.70
REMARK 500 4 TYR A 244 -77.46 -134.16
REMARK 500 5 SER A 180 -163.92 -165.71
REMARK 500 5 GLU A 181 159.78 72.34
REMARK 500 5 GLU A 193 -95.47 -126.11
REMARK 500 5 ALA A 194 -28.13 -174.15
REMARK 500
REMARK 500 THIS ENTRY HAS 232 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 N-TERMINAL GLY-SER FROM FUSION PARTNER
DBREF 1GL5 A 179 180 PDB 1GL5 1GL5 179 180
DBREF 1GL5 A 181 245 UNP P24604 TEC_MOUSE 181 245
SEQADV 1GL5 ASP A 245 UNP P24604 GLU 245 CONFLICT
SEQRES 1 A 67 GLY SER GLU ILE VAL VAL ALA MET TYR ASP PHE GLN ALA
SEQRES 2 A 67 THR GLU ALA HIS ASP LEU ARG LEU GLU ARG GLY GLN GLU
SEQRES 3 A 67 TYR ILE ILE LEU GLU LYS ASN ASP LEU HIS TRP TRP ARG
SEQRES 4 A 67 ALA ARG ASP LYS TYR GLY SER GLU GLY TYR ILE PRO SER
SEQRES 5 A 67 ASN TYR VAL THR GLY LYS LYS SER ASN ASN LEU ASP GLN
SEQRES 6 A 67 TYR ASP
SHEET 1 AA 5 GLU A 225 PRO A 229 0
SHEET 2 AA 5 TRP A 215 ARG A 219 -1 O TRP A 216 N ILE A 228
SHEET 3 AA 5 GLU A 204 GLU A 209 -1 O ILE A 206 N ARG A 219
SHEET 4 AA 5 VAL A 183 ALA A 185 -1 O VAL A 183 N TYR A 205
SHEET 5 AA 5 VAL A 233 THR A 234 -1 O THR A 234 N VAL A 184
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 28 2 Bytes