HEADER CELL ADHESION 31-MAY-11 3S90
TITLE HUMAN VINCULIN HEAD DOMAIN VH1 (RESIDUES 1-252) IN COMPLEX WITH MURINE
TITLE 2 TALIN (VBS33; RESIDUES 1512-1546)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VINCULIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 1-252;
COMPND 5 SYNONYM: METAVINCULIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: TALIN-1;
COMPND 9 CHAIN: C, D;
COMPND 10 FRAGMENT: UNP RESIDUES 1512-1546;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: VCL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 10 ORGANISM_COMMON: MOUSE;
SOURCE 11 ORGANISM_TAXID: 10090;
SOURCE 12 GENE: TLN1, TLN;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS FOUR-HELIX BUNDLE, CELL ADHESION, FOCAL ADHESION
EXPDTA X-RAY DIFFRACTION
AUTHOR S.D.YOGESHA,A.SHARFF,G.BRICOGNE,T.IZARD
REVDAT 6 13-SEP-23 3S90 1 REMARK SEQADV
REVDAT 5 08-NOV-17 3S90 1 REMARK
REVDAT 4 29-OCT-14 3S90 1 AUTHOR
REVDAT 3 19-DEC-12 3S90 1 JRNL
REVDAT 2 25-APR-12 3S90 1 JRNL VERSN
REVDAT 1 22-JUN-11 3S90 0
JRNL AUTH S.D.YOGESHA,A.SHARFF,G.BRICOGNE,T.IZARD
JRNL TITL INTERMOLECULAR VERSUS INTRAMOLECULAR INTERACTIONS OF THE
JRNL TITL 2 VINCULIN BINDING SITE 33 OF TALIN.
JRNL REF PROTEIN SCI. V. 20 1471 2011
JRNL REFN ISSN 0961-8368
JRNL PMID 21648001
JRNL DOI 10.1002/PRO.671
REMARK 2
REMARK 2 RESOLUTION. 1.97 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.13.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.97
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 70.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.2
REMARK 3 NUMBER OF REFLECTIONS : 51740
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.210
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 2625
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.97
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.02
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.24
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 3547
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2187
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3388
REMARK 3 BIN R VALUE (WORKING SET) : 0.2181
REMARK 3 BIN FREE R VALUE : 0.2331
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.48
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 159
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4288
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 406
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.76
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.11
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.324
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.140
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4333 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 5856 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2130 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 124 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 602 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4333 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 616 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 5644 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.97
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.24
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 2.89
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 47.6171 23.6830 40.2706
REMARK 3 T TENSOR
REMARK 3 T11: -0.2119 T22: 0.2187
REMARK 3 T33: -0.2282 T12: 0.0940
REMARK 3 T13: 0.0100 T23: -0.1302
REMARK 3 L TENSOR
REMARK 3 L11: 4.3543 L22: 0.1955
REMARK 3 L33: 2.1197 L12: 0.7569
REMARK 3 L13: 3.0720 L23: 0.5950
REMARK 3 S TENSOR
REMARK 3 S11: 0.1400 S12: 0.5652 S13: 0.1374
REMARK 3 S21: -0.0075 S22: -0.1288 S23: -0.0246
REMARK 3 S31: 0.1268 S32: 0.0588 S33: -0.0113
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 61.3864 3.3091 70.4037
REMARK 3 T TENSOR
REMARK 3 T11: -0.1048 T22: -0.1529
REMARK 3 T33: 0.1239 T12: 0.0469
REMARK 3 T13: 0.0145 T23: -0.0777
REMARK 3 L TENSOR
REMARK 3 L11: 4.1502 L22: 3.1313
REMARK 3 L33: 0.1781 L12: 3.5490
REMARK 3 L13: 0.1170 L23: 0.1309
REMARK 3 S TENSOR
REMARK 3 S11: 0.0493 S12: 0.1566 S13: -0.0494
REMARK 3 S21: 0.1347 S22: -0.0018 S23: 0.1417
REMARK 3 S31: 0.0005 S32: 0.0022 S33: -0.0475
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { C|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 33.8092 9.7839 32.2293
REMARK 3 T TENSOR
REMARK 3 T11: -0.0268 T22: 0.1611
REMARK 3 T33: -0.2050 T12: 0.1778
REMARK 3 T13: -0.1623 T23: -0.1344
REMARK 3 L TENSOR
REMARK 3 L11: 2.7388 L22: 2.4248
REMARK 3 L33: 1.8555 L12: -2.9720
REMARK 3 L13: -3.2695 L23: -0.2730
REMARK 3 S TENSOR
REMARK 3 S11: 0.0365 S12: 0.0917 S13: -0.2659
REMARK 3 S21: 0.0911 S22: -0.1601 S23: -0.2917
REMARK 3 S31: 0.0761 S32: -0.0284 S33: 0.1236
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { D|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 48.1408 -8.1335 80.7742
REMARK 3 T TENSOR
REMARK 3 T11: -0.0646 T22: -0.0713
REMARK 3 T33: 0.0633 T12: -0.0374
REMARK 3 T13: 0.0707 T23: -0.1650
REMARK 3 L TENSOR
REMARK 3 L11: 3.3684 L22: 0.0409
REMARK 3 L33: 3.7059 L12: -0.9541
REMARK 3 L13: 2.5596 L23: -1.5343
REMARK 3 S TENSOR
REMARK 3 S11: -0.0455 S12: -0.3069 S13: -0.0668
REMARK 3 S21: 0.1658 S22: 0.1491 S23: -0.0456
REMARK 3 S31: -0.0253 S32: 0.1038 S33: -0.1036
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3S90 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JUN-11.
REMARK 100 THE DEPOSITION ID IS D_1000065912.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-APR-10
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 5.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AUTOPROC, SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51772
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.970
REMARK 200 RESOLUTION RANGE LOW (A) : 70.010
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.7
REMARK 200 DATA REDUNDANCY : 2.800
REMARK 200 R MERGE (I) : 0.04300
REMARK 200 R SYM (I) : 0.04300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.97
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.90
REMARK 200 R MERGE FOR SHELL (I) : 0.53300
REMARK 200 R SYM FOR SHELL (I) : 0.53300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 2IBF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M CITRATE 5.3, 15% (W/V) PEG 10K,
REMARK 280 1.5% (V/V) DIOXANE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 277K, PH 5.3
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14410 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 0
REMARK 465 MET A 1
REMARK 465 PRO A 2
REMARK 465 THR A 251
REMARK 465 SER A 252
REMARK 465 MET B 0
REMARK 465 MET B 1
REMARK 465 GLY C 1507
REMARK 465 PRO C 1508
REMARK 465 LEU C 1509
REMARK 465 GLY C 1510
REMARK 465 SER C 1511
REMARK 465 ALA C 1512
REMARK 465 SER C 1513
REMARK 465 ALA C 1514
REMARK 465 ARG C 1515
REMARK 465 THR C 1516
REMARK 465 ALA C 1517
REMARK 465 ASN C 1518
REMARK 465 PRO C 1519
REMARK 465 GLY D 1507
REMARK 465 PRO D 1508
REMARK 465 LEU D 1509
REMARK 465 GLY D 1510
REMARK 465 SER D 1511
REMARK 465 ALA D 1512
REMARK 465 SER D 1513
REMARK 465 ALA D 1514
REMARK 465 ARG D 1515
REMARK 465 THR D 1516
REMARK 465 ALA D 1517
REMARK 465 ASN D 1518
REMARK 465 PRO D 1519
REMARK 465 LEU D 1546
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
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 ASP A 33 O HOH A 322 2.17
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 ALA C1545 124.49 -36.10
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2X0C RELATED DB: PDB
REMARK 900 RELATED ID: 1SYQ RELATED DB: PDB
REMARK 900 RELATED ID: 1T01 RELATED DB: PDB
REMARK 900 RELATED ID: 1RKC RELATED DB: PDB
REMARK 900 RELATED ID: 2BIF RELATED DB: PDB
REMARK 900 RELATED ID: 3RF3 RELATED DB: PDB
DBREF 3S90 A 1 252 UNP P18206 VINC_HUMAN 1 252
DBREF 3S90 B 1 252 UNP P18206 VINC_HUMAN 1 252
DBREF 3S90 C 1512 1546 UNP P26039 TLN1_MOUSE 1512 1546
DBREF 3S90 D 1512 1546 UNP P26039 TLN1_MOUSE 1512 1546
SEQADV 3S90 MET A 0 UNP P18206 INITIATING METHIONINE
SEQADV 3S90 MET B 0 UNP P18206 INITIATING METHIONINE
SEQADV 3S90 GLY C 1507 UNP P26039 EXPRESSION TAG
SEQADV 3S90 PRO C 1508 UNP P26039 EXPRESSION TAG
SEQADV 3S90 LEU C 1509 UNP P26039 EXPRESSION TAG
SEQADV 3S90 GLY C 1510 UNP P26039 EXPRESSION TAG
SEQADV 3S90 SER C 1511 UNP P26039 EXPRESSION TAG
SEQADV 3S90 GLY D 1507 UNP P26039 EXPRESSION TAG
SEQADV 3S90 PRO D 1508 UNP P26039 EXPRESSION TAG
SEQADV 3S90 LEU D 1509 UNP P26039 EXPRESSION TAG
SEQADV 3S90 GLY D 1510 UNP P26039 EXPRESSION TAG
SEQADV 3S90 SER D 1511 UNP P26039 EXPRESSION TAG
SEQRES 1 A 253 MET MET PRO VAL PHE HIS THR ARG THR ILE GLU SER ILE
SEQRES 2 A 253 LEU GLU PRO VAL ALA GLN GLN ILE SER HIS LEU VAL ILE
SEQRES 3 A 253 MET HIS GLU GLU GLY GLU VAL ASP GLY LYS ALA ILE PRO
SEQRES 4 A 253 ASP LEU THR ALA PRO VAL ALA ALA VAL GLN ALA ALA VAL
SEQRES 5 A 253 SER ASN LEU VAL ARG VAL GLY LYS GLU THR VAL GLN THR
SEQRES 6 A 253 THR GLU ASP GLN ILE LEU LYS ARG ASP MET PRO PRO ALA
SEQRES 7 A 253 PHE ILE LYS VAL GLU ASN ALA CYS THR LYS LEU VAL GLN
SEQRES 8 A 253 ALA ALA GLN MET LEU GLN SER ASP PRO TYR SER VAL PRO
SEQRES 9 A 253 ALA ARG ASP TYR LEU ILE ASP GLY SER ARG GLY ILE LEU
SEQRES 10 A 253 SER GLY THR SER ASP LEU LEU LEU THR PHE ASP GLU ALA
SEQRES 11 A 253 GLU VAL ARG LYS ILE ILE ARG VAL CYS LYS GLY ILE LEU
SEQRES 12 A 253 GLU TYR LEU THR VAL ALA GLU VAL VAL GLU THR MET GLU
SEQRES 13 A 253 ASP LEU VAL THR TYR THR LYS ASN LEU GLY PRO GLY MET
SEQRES 14 A 253 THR LYS MET ALA LYS MET ILE ASP GLU ARG GLN GLN GLU
SEQRES 15 A 253 LEU THR HIS GLN GLU HIS ARG VAL MET LEU VAL ASN SER
SEQRES 16 A 253 MET ASN THR VAL LYS GLU LEU LEU PRO VAL LEU ILE SER
SEQRES 17 A 253 ALA MET LYS ILE PHE VAL THR THR LYS ASN SER LYS ASN
SEQRES 18 A 253 GLN GLY ILE GLU GLU ALA LEU LYS ASN ARG ASN PHE THR
SEQRES 19 A 253 VAL GLU LYS MET SER ALA GLU ILE ASN GLU ILE ILE ARG
SEQRES 20 A 253 VAL LEU GLN LEU THR SER
SEQRES 1 B 253 MET MET PRO VAL PHE HIS THR ARG THR ILE GLU SER ILE
SEQRES 2 B 253 LEU GLU PRO VAL ALA GLN GLN ILE SER HIS LEU VAL ILE
SEQRES 3 B 253 MET HIS GLU GLU GLY GLU VAL ASP GLY LYS ALA ILE PRO
SEQRES 4 B 253 ASP LEU THR ALA PRO VAL ALA ALA VAL GLN ALA ALA VAL
SEQRES 5 B 253 SER ASN LEU VAL ARG VAL GLY LYS GLU THR VAL GLN THR
SEQRES 6 B 253 THR GLU ASP GLN ILE LEU LYS ARG ASP MET PRO PRO ALA
SEQRES 7 B 253 PHE ILE LYS VAL GLU ASN ALA CYS THR LYS LEU VAL GLN
SEQRES 8 B 253 ALA ALA GLN MET LEU GLN SER ASP PRO TYR SER VAL PRO
SEQRES 9 B 253 ALA ARG ASP TYR LEU ILE ASP GLY SER ARG GLY ILE LEU
SEQRES 10 B 253 SER GLY THR SER ASP LEU LEU LEU THR PHE ASP GLU ALA
SEQRES 11 B 253 GLU VAL ARG LYS ILE ILE ARG VAL CYS LYS GLY ILE LEU
SEQRES 12 B 253 GLU TYR LEU THR VAL ALA GLU VAL VAL GLU THR MET GLU
SEQRES 13 B 253 ASP LEU VAL THR TYR THR LYS ASN LEU GLY PRO GLY MET
SEQRES 14 B 253 THR LYS MET ALA LYS MET ILE ASP GLU ARG GLN GLN GLU
SEQRES 15 B 253 LEU THR HIS GLN GLU HIS ARG VAL MET LEU VAL ASN SER
SEQRES 16 B 253 MET ASN THR VAL LYS GLU LEU LEU PRO VAL LEU ILE SER
SEQRES 17 B 253 ALA MET LYS ILE PHE VAL THR THR LYS ASN SER LYS ASN
SEQRES 18 B 253 GLN GLY ILE GLU GLU ALA LEU LYS ASN ARG ASN PHE THR
SEQRES 19 B 253 VAL GLU LYS MET SER ALA GLU ILE ASN GLU ILE ILE ARG
SEQRES 20 B 253 VAL LEU GLN LEU THR SER
SEQRES 1 C 40 GLY PRO LEU GLY SER ALA SER ALA ARG THR ALA ASN PRO
SEQRES 2 C 40 THR ALA LYS ARG GLN PHE VAL GLN SER ALA LYS GLU VAL
SEQRES 3 C 40 ALA ASN SER THR ALA ASN LEU VAL LYS THR ILE LYS ALA
SEQRES 4 C 40 LEU
SEQRES 1 D 40 GLY PRO LEU GLY SER ALA SER ALA ARG THR ALA ASN PRO
SEQRES 2 D 40 THR ALA LYS ARG GLN PHE VAL GLN SER ALA LYS GLU VAL
SEQRES 3 D 40 ALA ASN SER THR ALA ASN LEU VAL LYS THR ILE LYS ALA
SEQRES 4 D 40 LEU
FORMUL 5 HOH *406(H2 O)
HELIX 1 1 THR A 6 GLU A 29 1 24
HELIX 2 2 LEU A 40 THR A 65 1 26
HELIX 3 3 ASP A 67 ASP A 98 1 32
HELIX 4 4 SER A 101 THR A 146 1 46
HELIX 5 5 VAL A 147 VAL A 151 5 5
HELIX 6 6 THR A 153 ASN A 163 1 11
HELIX 7 7 LEU A 164 GLN A 180 1 17
HELIX 8 8 HIS A 184 LYS A 219 1 36
HELIX 9 9 GLY A 222 LEU A 250 1 29
HELIX 10 10 THR B 6 GLU B 29 1 24
HELIX 11 11 LEU B 40 THR B 65 1 26
HELIX 12 12 ASP B 67 ASP B 98 1 32
HELIX 13 13 SER B 101 THR B 146 1 46
HELIX 14 14 VAL B 147 VAL B 151 5 5
HELIX 15 15 THR B 153 GLN B 180 1 28
HELIX 16 16 HIS B 184 THR B 215 1 32
HELIX 17 17 GLY B 222 THR B 251 1 30
HELIX 18 18 THR C 1520 ALA C 1545 1 26
HELIX 19 19 THR D 1520 ALA D 1545 1 26
CRYST1 48.830 61.180 71.420 83.27 79.05 69.79 P 1 2
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 0.020479 -0.007539 -0.003546 0.00000
SCALE2 0.000000 0.017418 -0.000976 0.00000
SCALE3 0.000000 0.000000 0.014284 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
