Header list of 2g35.pdb file
Complete list - r 9 2 Bytes
HEADER STRUCTURAL PROTEIN 17-FEB-06 2G35
TITLE NMR STRUCTURE OF TALIN-PTB IN COMPLEX WITH PIPKI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TALIN-1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: PEPTIDE;
COMPND 7 CHAIN: B;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: TLN1, TLN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
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: PET15B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES
KEYWDS TALIN, PTB DOMAIN, PIPKI, STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR X.KONG,X.WANG,S.MISRA,J.QIN
REVDAT 4 09-MAR-22 2G35 1 REMARK LINK
REVDAT 3 24-FEB-09 2G35 1 VERSN
REVDAT 2 23-MAY-06 2G35 1 JRNL
REVDAT 1 02-MAY-06 2G35 0
JRNL AUTH X.KONG,X.WANG,S.MISRA,J.QIN
JRNL TITL STRUCTURAL BASIS FOR THE PHOSPHORYLATION-REGULATED FOCAL
JRNL TITL 2 ADHESION TARGETING OF TYPE IGAMMA PHOSPHATIDYLINOSITOL
JRNL TITL 3 PHOSPHATE KINASE (PIPKIGAMMA) BY TALIN.
JRNL REF J.MOL.BIOL. V. 359 47 2006
JRNL REFN ISSN 0022-2836
JRNL PMID 16616931
JRNL DOI 10.1016/J.JMB.2006.02.048
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TALOS, X-PLOR
REMARK 3 AUTHORS : BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2G35 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-FEB-06.
REMARK 100 THE DEPOSITION ID IS D_1000036629.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.3
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : 20MM PHOSPHATE BUFFER, 5MM CA2+,
REMARK 210 PH 6.3, 10% D2O, 90% H2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : HNCACB; CBCA(CO)NH; HCCH-TOCSY;
REMARK 210 HNCO; EDITED NOESY; FILTERED
REMARK 210 NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 50
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 11
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: 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 O ARG A 35 H ILE A 44 1.48
REMARK 500 O GLN A 83 H LEU A 87 1.48
REMARK 500 H LYS A 53 O ASP A 65 1.56
REMARK 500 OE2 GLU A 80 HE22 GLN A 83 1.59
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 THR A 3 62.56 -170.27
REMARK 500 1 LYS A 16 -72.77 5.00
REMARK 500 1 PRO A 59 22.51 -60.78
REMARK 500 1 LYS A 60 -39.10 -145.60
REMARK 500 1 TRP B 2 -178.72 52.75
REMARK 500 1 PTR B 4 -165.43 -114.42
REMARK 500 1 LEU B 7 93.96 -46.57
REMARK 500 2 THR A 3 59.18 -167.78
REMARK 500 2 TYR A 4 170.19 -54.30
REMARK 500 2 LYS A 16 -77.23 -26.13
REMARK 500 2 LYS A 20 -173.72 -67.39
REMARK 500 2 PRO A 59 29.08 -60.82
REMARK 500 2 LYS A 60 -41.27 -150.64
REMARK 500 2 GLU A 80 -70.50 -105.75
REMARK 500 2 LEU B 7 95.71 -47.27
REMARK 500 3 LYS A 2 15.45 -61.84
REMARK 500 3 THR A 3 47.73 -140.28
REMARK 500 3 LYS A 16 -72.19 -2.79
REMARK 500 3 PRO A 59 3.22 -59.83
REMARK 500 3 LYS A 60 -20.23 -153.07
REMARK 500 3 LEU B 7 -175.14 -52.81
REMARK 500 4 LYS A 2 17.93 46.57
REMARK 500 4 THR A 3 59.06 -161.21
REMARK 500 4 LYS A 16 -68.46 -28.95
REMARK 500 4 ASN A 19 -7.30 -57.90
REMARK 500 4 LYS A 20 -175.38 -67.61
REMARK 500 4 PRO A 59 7.01 -59.19
REMARK 500 4 LYS A 60 -23.11 -147.26
REMARK 500 4 GLN A 70 -73.51 -55.97
REMARK 500 4 LYS A 99 -6.12 -56.35
REMARK 500 4 TRP B 2 -177.38 -68.74
REMARK 500 4 PTR B 4 -169.11 -118.08
REMARK 500 5 THR A 3 59.86 -170.10
REMARK 500 5 LYS A 16 -73.43 -10.87
REMARK 500 5 LYS A 41 18.83 49.75
REMARK 500 5 PRO A 59 3.09 -60.58
REMARK 500 5 LYS A 60 -11.15 -148.47
REMARK 500 5 GLU A 80 52.11 -149.71
REMARK 500 5 TRP B 2 -172.69 50.28
REMARK 500 5 PTR B 4 -164.99 -110.55
REMARK 500 6 LYS A 2 10.72 -69.29
REMARK 500 6 LYS A 16 -91.32 -55.01
REMARK 500 6 LYS A 20 -173.25 -69.85
REMARK 500 6 PRO A 59 -1.17 -58.39
REMARK 500 6 LYS A 60 -61.98 -107.43
REMARK 500 6 TRP B 2 -173.29 52.84
REMARK 500 6 LEU B 7 171.19 -46.56
REMARK 500 7 LYS A 2 15.07 47.59
REMARK 500 7 THR A 3 48.42 -153.01
REMARK 500 7 LYS A 16 -69.08 -5.45
REMARK 500
REMARK 500 THIS ENTRY HAS 162 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2G35 A 1 100 UNP P26039 TLN1_MOUSE 305 404
DBREF 2G35 B 1 8 PDB 2G35 2G35 1 8
SEQRES 1 A 100 LEU LYS THR TYR GLY VAL SER PHE PHE LEU VAL LYS GLU
SEQRES 2 A 100 LYS MET LYS GLY LYS ASN LYS LEU VAL PRO ARG LEU LEU
SEQRES 3 A 100 GLY ILE THR LYS GLU CYS VAL MET ARG VAL ASP GLU LYS
SEQRES 4 A 100 THR LYS GLU VAL ILE GLN GLU TRP SER LEU THR ASN ILE
SEQRES 5 A 100 LYS ARG TRP ALA ALA SER PRO LYS SER PHE THR LEU ASP
SEQRES 6 A 100 PHE GLY ASP TYR GLN ASP GLY TYR TYR SER VAL GLN THR
SEQRES 7 A 100 THR GLU GLY GLU GLN ILE ALA GLN LEU ILE ALA GLY TYR
SEQRES 8 A 100 ILE ASP ILE ILE LEU LYS LYS LYS LYS
SEQRES 1 B 8 SER TRP VAL PTR SER PRO LEU HIS
MODRES 2G35 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 1 GLU A 80 LYS A 100 1 21
SHEET 1 A 4 SER A 7 GLU A 13 0
SHEET 2 A 4 VAL A 22 ILE A 28 -1 O ARG A 24 N VAL A 11
SHEET 3 A 4 CYS A 32 ASP A 37 -1 O VAL A 36 N LEU A 25
SHEET 4 A 4 VAL A 43 SER A 48 -1 O ILE A 44 N ARG A 35
SHEET 1 B 3 ARG A 54 ALA A 57 0
SHEET 2 B 3 SER A 61 ASP A 65 -1 O ASP A 65 N ARG A 54
SHEET 3 B 3 TYR A 74 GLN A 77 -1 O VAL A 76 N PHE A 62
LINK C VAL B 3 N PTR B 4 1555 1555 1.31
LINK C PTR B 4 N SER 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 - r 9 2 Bytes