HEADER STRUCTURAL PROTEIN 14-DEC-10 2L7N
TITLE SOLUTION STRUCTURE OF THE R5 DOMAIN OF TALIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TALIN-1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: SEQUENCE DATABASE RESIDUES 1046-1207;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: TLN1, TLN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR: PET 151
KEYWDS INTEGRIN, BUNDLE, FOCAL ADHESION, STRUCTURAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR B.T.GOULT,A.R.GINGRAS,N.BATE,I.L.BARSUKOV,G.C.K.ROBERTS,D.R.CRITCHLEY
REVDAT 4 14-JUN-23 2L7N 1 REMARK
REVDAT 3 25-AUG-21 2L7N 1 TITLE REMARK SEQADV
REVDAT 2 15-JAN-14 2L7N 1 JRNL
REVDAT 1 14-DEC-11 2L7N 0
JRNL AUTH B.T.GOULT,T.ZACHARCHENKO,N.BATE,R.TSANG,F.HEY,A.R.GINGRAS,
JRNL AUTH 2 P.R.ELLIOTT,G.C.ROBERTS,C.BALLESTREM,D.R.CRITCHLEY,
JRNL AUTH 3 I.L.BARSUKOV
JRNL TITL RIAM AND VINCULIN BINDING TO TALIN ARE MUTUALLY EXCLUSIVE
JRNL TITL 2 AND REGULATE ADHESION ASSEMBLY AND TURNOVER.
JRNL REF J.BIOL.CHEM. V. 288 8238 2013
JRNL REFN ISSN 0021-9258
JRNL PMID 23389036
JRNL DOI 10.1074/JBC.M112.438119
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : TOPSPIN 2.1, ARIA 1.2
REMARK 3 AUTHORS : BRUKER BIOSPIN (TOPSPIN), LINGE, O'DONOGHUE AND
REMARK 3 NILGES (ARIA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: FINAL STRUCTURES REFINED IN EXPLICIT
REMARK 3 WATER BATH AS IMPLEMENTED IN ARIA 1.2/CNS 1.1. 20 LOWEST ENERGY
REMARK 3 STRUCTURES SELECTED FROM WATER REFINEMENT, CNS, INITIAL
REMARK 3 STRUCTURES GENERATED WITH CYANA
REMARK 4
REMARK 4 2L7N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-DEC-10.
REMARK 100 THE DEPOSITION ID IS D_1000102058.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : 50
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM [U-100% 15N] DOMB, 10 % [U
REMARK 210 -100% 2H] D2O, 90 % H2O, 2 MM
REMARK 210 DTT, 50 MM SODIUM CHLORIDE, 20
REMARK 210 MM SODIUM PHOSPHATE, 90% H2O/10%
REMARK 210 D2O; 1 MM [U-100% 13C; U-100%
REMARK 210 15N] DOMB, 10 % [U-100% 2H] D2O,
REMARK 210 90 % H2O, 2 MM DTT, 50 MM SODIUM
REMARK 210 CHLORIDE, 20 MM SODIUM PHOSPHATE,
REMARK 210 90% H2O/10% D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D 1H-15N HSQC; 2D 1H-13C HSQC;
REMARK 210 3D 1H-15N NOESY; 3D 1H-13C NOESY;
REMARK 210 3D HNCO; 3D HNCA; 3D HNCACB; 3D
REMARK 210 HCCH-TOCSY; 3D HN(CO)CA; 3D
REMARK 210 CBCA(CO)NH
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : TOPSPIN 2.1, TALOS, CYANA, ARIA
REMARK 210 1.2
REMARK 210 METHOD USED : SIMULATED ANNEALING, MOLECULAR
REMARK 210 DYNAMICS, TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 200
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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: 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 ILE A1041 78.14 54.96
REMARK 500 1 PRO A1047 35.94 -82.89
REMARK 500 1 LYS A1075 -84.06 -90.09
REMARK 500 1 LEU A1076 -164.51 47.97
REMARK 500 1 PRO A1080 30.12 -83.72
REMARK 500 1 GLU A1108 -160.65 63.61
REMARK 500 1 ALA A1146 -55.48 -164.43
REMARK 500 1 PRO A1176 56.07 -68.96
REMARK 500 2 PRO A1043 88.35 -57.29
REMARK 500 2 PHE A1044 93.71 -177.04
REMARK 500 2 PRO A1047 39.34 -87.24
REMARK 500 2 PRO A1078 30.92 -88.28
REMARK 500 2 GLU A1114 78.91 -103.34
REMARK 500 2 ALA A1146 -56.02 -164.74
REMARK 500 2 GLN A1206 76.00 58.55
REMARK 500 3 PRO A1047 32.44 -70.41
REMARK 500 3 LEU A1048 31.59 -89.09
REMARK 500 3 PRO A1080 -154.64 -71.26
REMARK 500 3 GLU A1082 -157.09 62.56
REMARK 500 3 GLU A1108 -153.08 -90.27
REMARK 500 3 SER A1143 -39.98 73.07
REMARK 500 3 ALA A1146 -55.66 -167.45
REMARK 500 3 GLN A1206 95.03 58.50
REMARK 500 4 PHE A1044 -113.97 -120.49
REMARK 500 4 THR A1045 -32.26 62.28
REMARK 500 4 PRO A1078 -67.39 -94.16
REMARK 500 4 ALA A1110 -61.23 -90.41
REMARK 500 4 GLN A1111 -75.52 -122.56
REMARK 500 4 GLU A1114 92.27 -61.19
REMARK 500 4 ASN A1115 -39.98 173.27
REMARK 500 4 ALA A1146 -56.66 -165.45
REMARK 500 4 PRO A1176 23.22 -78.96
REMARK 500 5 LEU A1076 -168.50 53.92
REMARK 500 5 LEU A1079 85.78 58.64
REMARK 500 5 ALA A1110 -38.71 175.45
REMARK 500 5 GLN A1111 143.15 -175.57
REMARK 500 5 GLU A1114 144.57 68.75
REMARK 500 5 ASN A1115 -63.33 68.95
REMARK 500 5 ALA A1146 -58.33 -168.04
REMARK 500 5 SER A1173 106.86 -59.08
REMARK 500 5 PRO A1176 31.03 -92.99
REMARK 500 5 PRO A1204 103.04 -57.11
REMARK 500 6 ILE A1041 -53.98 73.89
REMARK 500 6 ASP A1042 95.92 61.10
REMARK 500 6 ALA A1146 -48.57 -162.35
REMARK 500 6 PRO A1204 109.19 -58.11
REMARK 500 7 THR A1045 88.02 -152.22
REMARK 500 7 GLU A1108 76.67 55.84
REMARK 500 7 ALA A1110 174.57 64.78
REMARK 500 7 ALA A1146 -55.24 -170.37
REMARK 500
REMARK 500 THIS ENTRY HAS 151 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 17142 RELATED DB: BMRB
REMARK 900 CHEMICAL SHIFT ASSIGNMENTS OF DOMAIN B
REMARK 900 RELATED ID: 17363 RELATED DB: BMRB
DBREF 2L7N A 1046 1207 UNP P26039 TLN1_MOUSE 1046 1207
SEQADV 2L7N GLY A 1040 UNP P26039 EXPRESSION TAG
SEQADV 2L7N ILE A 1041 UNP P26039 EXPRESSION TAG
SEQADV 2L7N ASP A 1042 UNP P26039 EXPRESSION TAG
SEQADV 2L7N PRO A 1043 UNP P26039 EXPRESSION TAG
SEQADV 2L7N PHE A 1044 UNP P26039 EXPRESSION TAG
SEQADV 2L7N THR A 1045 UNP P26039 EXPRESSION TAG
SEQRES 1 A 168 GLY ILE ASP PRO PHE THR GLY PRO LEU GLU MET ASP SER
SEQRES 2 A 168 ALA LEU SER VAL VAL GLN ASN LEU GLU LYS ASP LEU GLN
SEQRES 3 A 168 GLU ILE LYS ALA ALA ALA ARG ASP GLY LYS LEU LYS PRO
SEQRES 4 A 168 LEU PRO GLY GLU THR MET GLU LYS CYS THR GLN ASP LEU
SEQRES 5 A 168 GLY ASN SER THR LYS ALA VAL SER SER ALA ILE ALA LYS
SEQRES 6 A 168 LEU LEU GLY GLU ILE ALA GLN GLY ASN GLU ASN TYR ALA
SEQRES 7 A 168 GLY ILE ALA ALA ARG ASP VAL ALA GLY GLY LEU ARG SER
SEQRES 8 A 168 LEU ALA GLN ALA ALA ARG GLY VAL ALA ALA LEU THR SER
SEQRES 9 A 168 ASP PRO ALA VAL GLN ALA ILE VAL LEU ASP THR ALA SER
SEQRES 10 A 168 ASP VAL LEU ASP LYS ALA SER SER LEU ILE GLU GLU ALA
SEQRES 11 A 168 LYS LYS ALA SER GLY HIS PRO GLY ASP PRO GLU SER GLN
SEQRES 12 A 168 GLN ARG LEU ALA GLN VAL ALA LYS ALA VAL THR GLN ALA
SEQRES 13 A 168 LEU ASN ARG CYS VAL SER CYS LEU PRO GLY GLN ARG
HELIX 1 1 LEU A 1048 GLY A 1074 1 27
HELIX 2 2 THR A 1083 LEU A 1106 1 24
HELIX 3 3 GLU A 1114 THR A 1142 1 29
HELIX 4 4 ALA A 1146 SER A 1173 1 28
HELIX 5 5 ASP A 1178 CYS A 1202 1 25
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
(ATOM LINES ARE NOT SHOWN.)
END
