HEADER STRUCTURAL PROTEIN 28-JUL-08 3DYJ
TITLE CRYSTAL STRUCTURE OF THE R11R12 DOMAINS OF TALIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TALIN-1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: TALIN ROD (UNP RESIDUES:1974-2293);
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: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-151
KEYWDS TALIN, HELIX BUNDLES, CYTOSKELETAL PROTEIN, INTEGRIN-BINDIN SITE,
KEYWDS 2 IBS2, CELL MEMBRANE, CELL PROJECTION, CYTOPLASM, CYTOSKELETON,
KEYWDS 3 MEMBRANE, PHOSPHOPROTEIN, STRUCTURAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.R.GINGRAS,M.G.JOYCE,D.R.CRITCHLEY,J.EMSLEY
REVDAT 3 25-AUG-21 3DYJ 1 TITLE SEQADV LINK
REVDAT 2 07-APR-09 3DYJ 1 JRNL
REVDAT 1 27-JAN-09 3DYJ 0
JRNL AUTH A.R.GINGRAS,W.H.ZIEGLER,A.A.BOBKOV,M.G.JOYCE,D.FASCI,
JRNL AUTH 2 M.HIMMEL,S.ROTHEMUND,A.RITTER,J.G.GROSSMANN,B.PATEL,N.BATE,
JRNL AUTH 3 B.T.GOULT,J.EMSLEY,I.L.BARSUKOV,G.C.ROBERTS,R.C.LIDDINGTON,
JRNL AUTH 4 M.H.GINSBERG,D.R.CRITCHLEY
JRNL TITL STRUCTURAL DETERMINANTS OF INTEGRIN BINDING TO THE TALIN ROD
JRNL REF J.BIOL.CHEM. V. 284 8866 2009
JRNL REFN ISSN 0021-9258
JRNL PMID 19176533
JRNL DOI 10.1074/JBC.M805937200
REMARK 2
REMARK 2 RESOLUTION. 1.85 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.57
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 3 NUMBER OF REFLECTIONS : 49457
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.260
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.600
REMARK 3 FREE R VALUE TEST SET COUNT : 1300
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.85
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3184
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.30
REMARK 3 BIN R VALUE (WORKING SET) : 0.2870
REMARK 3 BIN FREE R VALUE SET COUNT : 87
REMARK 3 BIN FREE R VALUE : 0.4120
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4678
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 332
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.18000
REMARK 3 B33 (A**2) : -0.31000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.27000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.166
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.155
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.115
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.774
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.933
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4726 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6410 ; 1.454 ; 1.971
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 632 ; 4.839 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 176 ;40.945 ;25.227
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 840 ;15.849 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;15.169 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 800 ; 0.099 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3422 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2657 ; 0.215 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3425 ; 0.294 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 322 ; 0.168 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 101 ; 0.304 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 19 ; 0.178 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3238 ; 1.074 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 5056 ; 1.683 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1626 ; 3.280 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1354 ; 5.068 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 5
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1977 A 2001
REMARK 3 RESIDUE RANGE : A 2012 A 2037
REMARK 3 RESIDUE RANGE : A 2041 A 2069
REMARK 3 RESIDUE RANGE : A 2074 A 2102
REMARK 3 RESIDUE RANGE : A 2109 A 2136
REMARK 3 ORIGIN FOR THE GROUP (A): 34.3896 32.4070 4.4452
REMARK 3 T TENSOR
REMARK 3 T11: -0.1191 T22: -0.2000
REMARK 3 T33: -0.1262 T12: -0.0054
REMARK 3 T13: 0.0260 T23: -0.0372
REMARK 3 L TENSOR
REMARK 3 L11: 1.5505 L22: 1.7147
REMARK 3 L33: 4.1034 L12: 0.3415
REMARK 3 L13: 0.8600 L23: -0.3874
REMARK 3 S TENSOR
REMARK 3 S11: 0.0246 S12: -0.1086 S13: -0.0301
REMARK 3 S21: 0.1512 S22: 0.0276 S23: -0.0183
REMARK 3 S31: 0.0758 S32: 0.1268 S33: -0.0523
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 5
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2140 A 2161
REMARK 3 RESIDUE RANGE : A 2172 A 2194
REMARK 3 RESIDUE RANGE : A 2199 A 2224
REMARK 3 RESIDUE RANGE : A 2230 A 2259
REMARK 3 RESIDUE RANGE : A 2264 A 2289
REMARK 3 ORIGIN FOR THE GROUP (A): 19.7736 20.1333 -39.1872
REMARK 3 T TENSOR
REMARK 3 T11: -0.1469 T22: -0.0567
REMARK 3 T33: -0.1061 T12: 0.0002
REMARK 3 T13: 0.0153 T23: 0.0233
REMARK 3 L TENSOR
REMARK 3 L11: 0.9228 L22: 3.0154
REMARK 3 L33: 4.0151 L12: 1.0413
REMARK 3 L13: 1.2000 L23: 3.3131
REMARK 3 S TENSOR
REMARK 3 S11: 0.0336 S12: 0.0700 S13: 0.0203
REMARK 3 S21: 0.0842 S22: -0.0762 S23: 0.0447
REMARK 3 S31: 0.0820 S32: -0.3274 S33: 0.0427
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 5
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1977 B 2001
REMARK 3 RESIDUE RANGE : B 2012 B 2037
REMARK 3 RESIDUE RANGE : B 2041 B 2069
REMARK 3 RESIDUE RANGE : B 2074 B 2102
REMARK 3 RESIDUE RANGE : B 2109 B 2136
REMARK 3 ORIGIN FOR THE GROUP (A): 35.0512 2.9583 -49.7518
REMARK 3 T TENSOR
REMARK 3 T11: -0.1352 T22: -0.1555
REMARK 3 T33: -0.1110 T12: -0.0142
REMARK 3 T13: 0.0460 T23: 0.0255
REMARK 3 L TENSOR
REMARK 3 L11: 1.4879 L22: 1.7613
REMARK 3 L33: 3.4692 L12: -0.3600
REMARK 3 L13: 0.4145 L23: 0.6437
REMARK 3 S TENSOR
REMARK 3 S11: 0.0275 S12: 0.0419 S13: -0.0814
REMARK 3 S21: 0.0217 S22: -0.0219 S23: -0.0111
REMARK 3 S31: 0.1253 S32: -0.2540 S33: -0.0056
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 5
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2140 B 2161
REMARK 3 RESIDUE RANGE : B 2172 B 2194
REMARK 3 RESIDUE RANGE : B 2199 B 2224
REMARK 3 RESIDUE RANGE : B 2230 B 2259
REMARK 3 RESIDUE RANGE : B 2264 B 2289
REMARK 3 ORIGIN FOR THE GROUP (A): 49.3447 -6.9696 -5.7673
REMARK 3 T TENSOR
REMARK 3 T11: -0.1081 T22: 0.0038
REMARK 3 T33: -0.0661 T12: -0.0338
REMARK 3 T13: -0.0093 T23: -0.0026
REMARK 3 L TENSOR
REMARK 3 L11: 1.8257 L22: 2.1967
REMARK 3 L33: 3.3783 L12: -0.4312
REMARK 3 L13: 0.8125 L23: -2.0900
REMARK 3 S TENSOR
REMARK 3 S11: -0.0716 S12: 0.1948 S13: 0.2259
REMARK 3 S21: 0.0332 S22: -0.0723 S23: -0.1284
REMARK 3 S31: -0.0984 S32: 0.3598 S33: 0.1440
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 3DYJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUL-08.
REMARK 100 THE DEPOSITION ID IS D_1000048649.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-DEC-05
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-4
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9757
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : GE(220) CRYSTAL AND MULTILAYER
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : DENZO
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52439
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.08500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.92
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.44900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.700
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 8000, 1% PEG 3350, 100MM HEPES
REMARK 280 (PH 7.5), 10MM SODIUM THIOCYANATE, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 273K, PH 7.50, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-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 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 28.82400
REMARK 290 SMTRY3 2 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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. (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 GLY A 1962
REMARK 465 ILE A 1963
REMARK 465 ASP A 1964
REMARK 465 PRO A 1965
REMARK 465 PHE A 1966
REMARK 465 THR A 1967
REMARK 465 GLY A 1968
REMARK 465 ILE A 1969
REMARK 465 ASP A 1970
REMARK 465 PRO A 1971
REMARK 465 PHE A 1972
REMARK 465 THR A 1973
REMARK 465 GLY A 1974
REMARK 465 GLY A 2292
REMARK 465 THR A 2293
REMARK 465 GLY B 1962
REMARK 465 ILE B 1963
REMARK 465 ASP B 1964
REMARK 465 PRO B 1965
REMARK 465 PHE B 1966
REMARK 465 THR B 1967
REMARK 465 GLY B 1968
REMARK 465 ILE B 1969
REMARK 465 ASP B 1970
REMARK 465 PRO B 1971
REMARK 465 PHE B 1972
REMARK 465 THR B 1973
REMARK 465 GLY B 1974
REMARK 465 GLY B 2292
REMARK 465 THR B 2293
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 HOH A 299 O HOH A 330 1.89
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 MSE B1997 CG - SE - CE ANGL. DEV. = -14.7 DEGREES
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 SER A2040 138.94 -38.85
REMARK 500 ALA A2102 109.15 -50.87
REMARK 500 LYS B2260 87.84 -174.28
REMARK 500
REMARK 500 REMARK: NULL
DBREF 3DYJ A 1974 2293 UNP P26039 TLN1_MOUSE 1974 2293
DBREF 3DYJ B 1974 2293 UNP P26039 TLN1_MOUSE 1974 2293
SEQADV 3DYJ GLY A 1962 UNP P26039 EXPRESSION TAG
SEQADV 3DYJ ILE A 1963 UNP P26039 EXPRESSION TAG
SEQADV 3DYJ ASP A 1964 UNP P26039 EXPRESSION TAG
SEQADV 3DYJ PRO A 1965 UNP P26039 EXPRESSION TAG
SEQADV 3DYJ PHE A 1966 UNP P26039 EXPRESSION TAG
SEQADV 3DYJ THR A 1967 UNP P26039 EXPRESSION TAG
SEQADV 3DYJ GLY A 1968 UNP P26039 EXPRESSION TAG
SEQADV 3DYJ ILE A 1969 UNP P26039 EXPRESSION TAG
SEQADV 3DYJ ASP A 1970 UNP P26039 EXPRESSION TAG
SEQADV 3DYJ PRO A 1971 UNP P26039 EXPRESSION TAG
SEQADV 3DYJ PHE A 1972 UNP P26039 EXPRESSION TAG
SEQADV 3DYJ THR A 1973 UNP P26039 EXPRESSION TAG
SEQADV 3DYJ GLY B 1962 UNP P26039 EXPRESSION TAG
SEQADV 3DYJ ILE B 1963 UNP P26039 EXPRESSION TAG
SEQADV 3DYJ ASP B 1964 UNP P26039 EXPRESSION TAG
SEQADV 3DYJ PRO B 1965 UNP P26039 EXPRESSION TAG
SEQADV 3DYJ PHE B 1966 UNP P26039 EXPRESSION TAG
SEQADV 3DYJ THR B 1967 UNP P26039 EXPRESSION TAG
SEQADV 3DYJ GLY B 1968 UNP P26039 EXPRESSION TAG
SEQADV 3DYJ ILE B 1969 UNP P26039 EXPRESSION TAG
SEQADV 3DYJ ASP B 1970 UNP P26039 EXPRESSION TAG
SEQADV 3DYJ PRO B 1971 UNP P26039 EXPRESSION TAG
SEQADV 3DYJ PHE B 1972 UNP P26039 EXPRESSION TAG
SEQADV 3DYJ THR B 1973 UNP P26039 EXPRESSION TAG
SEQRES 1 A 332 GLY ILE ASP PRO PHE THR GLY ILE ASP PRO PHE THR GLY
SEQRES 2 A 332 THR GLN ALA CYS ILE THR ALA ALA SER ALA VAL SER GLY
SEQRES 3 A 332 ILE ILE ALA ASP LEU ASP THR THR ILE MSE PHE ALA THR
SEQRES 4 A 332 ALA GLY THR LEU ASN ARG GLU GLY ALA GLU THR PHE ALA
SEQRES 5 A 332 ASP HIS ARG GLU GLY ILE LEU LYS THR ALA LYS VAL LEU
SEQRES 6 A 332 VAL GLU ASP THR LYS VAL LEU VAL GLN ASN ALA ALA GLY
SEQRES 7 A 332 SER GLN GLU LYS LEU ALA GLN ALA ALA GLN SER SER VAL
SEQRES 8 A 332 ALA THR ILE THR ARG LEU ALA ASP VAL VAL LYS LEU GLY
SEQRES 9 A 332 ALA ALA SER LEU GLY ALA GLU ASP PRO GLU THR GLN VAL
SEQRES 10 A 332 VAL LEU ILE ASN ALA VAL LYS ASP VAL ALA LYS ALA LEU
SEQRES 11 A 332 GLY ASP LEU ILE SER ALA THR LYS ALA ALA ALA GLY LYS
SEQRES 12 A 332 VAL GLY ASP ASP PRO ALA VAL TRP GLN LEU LYS ASN SER
SEQRES 13 A 332 ALA LYS VAL MSE VAL THR ASN VAL THR SER LEU LEU LYS
SEQRES 14 A 332 THR VAL LYS ALA VAL GLU ASP GLU ALA THR LYS GLY THR
SEQRES 15 A 332 ARG ALA LEU GLU ALA THR THR GLU HIS ILE ARG GLN GLU
SEQRES 16 A 332 LEU ALA VAL PHE CYS SER PRO GLU PRO PRO ALA LYS THR
SEQRES 17 A 332 SER THR PRO GLU ASP PHE ILE ARG MSE THR LYS GLY ILE
SEQRES 18 A 332 THR MSE ALA THR ALA LYS ALA VAL ALA ALA GLY ASN SER
SEQRES 19 A 332 CYS ARG GLN GLU ASP VAL ILE ALA THR ALA ASN LEU SER
SEQRES 20 A 332 ARG ARG ALA ILE ALA ASP MSE LEU ARG ALA CYS LYS GLU
SEQRES 21 A 332 ALA ALA PHE HIS PRO GLU VAL ALA PRO ASP VAL ARG LEU
SEQRES 22 A 332 ARG ALA LEU HIS TYR GLY ARG GLU CYS ALA ASN GLY TYR
SEQRES 23 A 332 LEU GLU LEU LEU ASP HIS VAL LEU LEU THR LEU GLN LYS
SEQRES 24 A 332 PRO ASN PRO ASP LEU LYS GLN GLN LEU THR GLY HIS SER
SEQRES 25 A 332 LYS ARG VAL ALA GLY SER VAL THR GLU LEU ILE GLN ALA
SEQRES 26 A 332 ALA GLU ALA MSE LYS GLY THR
SEQRES 1 B 332 GLY ILE ASP PRO PHE THR GLY ILE ASP PRO PHE THR GLY
SEQRES 2 B 332 THR GLN ALA CYS ILE THR ALA ALA SER ALA VAL SER GLY
SEQRES 3 B 332 ILE ILE ALA ASP LEU ASP THR THR ILE MSE PHE ALA THR
SEQRES 4 B 332 ALA GLY THR LEU ASN ARG GLU GLY ALA GLU THR PHE ALA
SEQRES 5 B 332 ASP HIS ARG GLU GLY ILE LEU LYS THR ALA LYS VAL LEU
SEQRES 6 B 332 VAL GLU ASP THR LYS VAL LEU VAL GLN ASN ALA ALA GLY
SEQRES 7 B 332 SER GLN GLU LYS LEU ALA GLN ALA ALA GLN SER SER VAL
SEQRES 8 B 332 ALA THR ILE THR ARG LEU ALA ASP VAL VAL LYS LEU GLY
SEQRES 9 B 332 ALA ALA SER LEU GLY ALA GLU ASP PRO GLU THR GLN VAL
SEQRES 10 B 332 VAL LEU ILE ASN ALA VAL LYS ASP VAL ALA LYS ALA LEU
SEQRES 11 B 332 GLY ASP LEU ILE SER ALA THR LYS ALA ALA ALA GLY LYS
SEQRES 12 B 332 VAL GLY ASP ASP PRO ALA VAL TRP GLN LEU LYS ASN SER
SEQRES 13 B 332 ALA LYS VAL MSE VAL THR ASN VAL THR SER LEU LEU LYS
SEQRES 14 B 332 THR VAL LYS ALA VAL GLU ASP GLU ALA THR LYS GLY THR
SEQRES 15 B 332 ARG ALA LEU GLU ALA THR THR GLU HIS ILE ARG GLN GLU
SEQRES 16 B 332 LEU ALA VAL PHE CYS SER PRO GLU PRO PRO ALA LYS THR
SEQRES 17 B 332 SER THR PRO GLU ASP PHE ILE ARG MSE THR LYS GLY ILE
SEQRES 18 B 332 THR MSE ALA THR ALA LYS ALA VAL ALA ALA GLY ASN SER
SEQRES 19 B 332 CYS ARG GLN GLU ASP VAL ILE ALA THR ALA ASN LEU SER
SEQRES 20 B 332 ARG ARG ALA ILE ALA ASP MSE LEU ARG ALA CYS LYS GLU
SEQRES 21 B 332 ALA ALA PHE HIS PRO GLU VAL ALA PRO ASP VAL ARG LEU
SEQRES 22 B 332 ARG ALA LEU HIS TYR GLY ARG GLU CYS ALA ASN GLY TYR
SEQRES 23 B 332 LEU GLU LEU LEU ASP HIS VAL LEU LEU THR LEU GLN LYS
SEQRES 24 B 332 PRO ASN PRO ASP LEU LYS GLN GLN LEU THR GLY HIS SER
SEQRES 25 B 332 LYS ARG VAL ALA GLY SER VAL THR GLU LEU ILE GLN ALA
SEQRES 26 B 332 ALA GLU ALA MSE LYS GLY THR
MODRES 3DYJ MSE A 1997 MET SELENOMETHIONINE
MODRES 3DYJ MSE A 2121 MET SELENOMETHIONINE
MODRES 3DYJ MSE A 2178 MET SELENOMETHIONINE
MODRES 3DYJ MSE A 2184 MET SELENOMETHIONINE
MODRES 3DYJ MSE A 2215 MET SELENOMETHIONINE
MODRES 3DYJ MSE A 2290 MET SELENOMETHIONINE
MODRES 3DYJ MSE B 1997 MET SELENOMETHIONINE
MODRES 3DYJ MSE B 2121 MET SELENOMETHIONINE
MODRES 3DYJ MSE B 2178 MET SELENOMETHIONINE
MODRES 3DYJ MSE B 2184 MET SELENOMETHIONINE
MODRES 3DYJ MSE B 2215 MET SELENOMETHIONINE
MODRES 3DYJ MSE B 2290 MET SELENOMETHIONINE
HET MSE A1997 8
HET MSE A2121 8
HET MSE A2178 8
HET MSE A2184 8
HET MSE A2215 8
HET MSE A2290 8
HET MSE B1997 8
HET MSE B2121 8
HET MSE B2178 8
HET MSE B2184 8
HET MSE B2215 8
HET MSE B2290 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 12(C5 H11 N O2 SE)
FORMUL 3 HOH *332(H2 O)
HELIX 1 1 THR A 1975 ALA A 2001 1 27
HELIX 2 2 THR A 2011 ASP A 2014 5 4
HELIX 3 3 HIS A 2015 ALA A 2037 1 23
HELIX 4 4 SER A 2040 LEU A 2069 1 30
HELIX 5 5 ASP A 2073 ALA A 2101 1 29
HELIX 6 6 ASP A 2108 SER A 2162 1 55
HELIX 7 7 THR A 2171 CYS A 2196 1 26
HELIX 8 8 ARG A 2197 PHE A 2224 1 28
HELIX 9 9 ALA A 2229 LYS A 2260 1 32
HELIX 10 10 ASN A 2262 ALA A 2289 1 28
HELIX 11 11 THR B 1975 ALA B 2001 1 27
HELIX 12 12 THR B 2011 ALA B 2038 1 28
HELIX 13 13 SER B 2040 LEU B 2069 1 30
HELIX 14 14 ASP B 2073 ALA B 2102 1 30
HELIX 15 15 ASP B 2108 CYS B 2161 1 54
HELIX 16 16 THR B 2171 CYS B 2196 1 26
HELIX 17 17 ARG B 2197 PHE B 2224 1 28
HELIX 18 18 ALA B 2229 LYS B 2260 1 32
HELIX 19 19 ASN B 2262 MSE B 2290 1 29
LINK C ILE A1996 N MSE A1997 1555 1555 1.34
LINK C MSE A1997 N PHE A1998 1555 1555 1.33
LINK C VAL A2120 N MSE A2121 1555 1555 1.34
LINK C MSE A2121 N VAL A2122 1555 1555 1.33
LINK C ARG A2177 N MSE A2178 1555 1555 1.34
LINK C MSE A2178 N THR A2179 1555 1555 1.33
LINK C THR A2183 N MSE A2184 1555 1555 1.34
LINK C MSE A2184 N ALA A2185 1555 1555 1.32
LINK C ASP A2214 N MSE A2215 1555 1555 1.34
LINK C MSE A2215 N LEU A2216 1555 1555 1.35
LINK C ALA A2289 N MSE A2290 1555 1555 1.33
LINK C MSE A2290 N LYS A2291 1555 1555 1.33
LINK C ILE B1996 N MSE B1997 1555 1555 1.33
LINK C MSE B1997 N PHE B1998 1555 1555 1.34
LINK C VAL B2120 N MSE B2121 1555 1555 1.32
LINK C MSE B2121 N VAL B2122 1555 1555 1.34
LINK C ARG B2177 N MSE B2178 1555 1555 1.33
LINK C MSE B2178 N THR B2179 1555 1555 1.33
LINK C THR B2183 N MSE B2184 1555 1555 1.33
LINK C MSE B2184 N ALA B2185 1555 1555 1.33
LINK C ASP B2214 N MSE B2215 1555 1555 1.34
LINK C MSE B2215 N LEU B2216 1555 1555 1.33
LINK C ALA B2289 N MSE B2290 1555 1555 1.33
LINK C MSE B2290 N LYS B2291 1555 1555 1.34
CRYST1 58.713 57.648 92.547 90.00 102.96 90.00 P 1 21 1 4
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 0.017032 0.000000 0.003920 0.00000
SCALE2 0.000000 0.017347 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011088 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
