HEADER PROTEIN BINDING 03-JUN-05 1ZW3
TITLE VINCULIN HEAD (0-258) IN COMPLEX WITH THE TALIN ROD RESIDUES 1630-1652
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VINCULIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 0-258;
COMPND 5 SYNONYM: METAVINCULIN;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: TALIN 1;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: RESIDUES 1630-1652;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 GENE: VCL, VINC1;
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: PET-15B;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 OTHER_DETAILS: THE PEPTIDE WAS CHEMICALLY SYNTHESIZED. THE SEQUENCE
SOURCE 14 OF THE PEPTIDE IS NATURALLY FOUND IN MUS MUSCULUS (MOUSE).
KEYWDS TALIN, VINCULIN, COMPLEX, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR A.R.GINGRAS,W.H.ZIEGLER,I.L.BARSUKOV,G.C.ROBERTS,D.R.CRITCHLEY,
AUTHOR 2 J.EMSLEY
REVDAT 4 23-AUG-23 1ZW3 1 SEQADV
REVDAT 3 24-FEB-09 1ZW3 1 VERSN
REVDAT 2 14-MAR-06 1ZW3 1 JRNL
REVDAT 1 20-SEP-05 1ZW3 0
JRNL AUTH A.R.GINGRAS,W.H.ZIEGLER,R.FRANK,I.L.BARSUKOV,G.C.ROBERTS,
JRNL AUTH 2 D.R.CRITCHLEY,J.EMSLEY
JRNL TITL MAPPING AND CONSENSUS SEQUENCE IDENTIFICATION FOR MULTIPLE
JRNL TITL 2 VINCULIN BINDING SITES WITHIN THE TALIN ROD
JRNL REF J.BIOL.CHEM. V. 280 37217 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 16135522
JRNL DOI 10.1074/JBC.M508060200
REMARK 2
REMARK 2 RESOLUTION. 3.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 3.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 5533
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) : 0.228
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.307
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 265
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) : 3.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.39
REMARK 3 REFLECTION IN BIN (WORKING SET) : 398
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2230
REMARK 3 BIN FREE R VALUE SET COUNT : 16
REMARK 3 BIN FREE R VALUE : 0.3880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2136
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.03000
REMARK 3 B22 (A**2) : 5.02000
REMARK 3 B33 (A**2) : -3.99000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.640
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.431
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.832
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.927
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.853
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2161 ; 0.026 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2081 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2921 ; 2.286 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4849 ; 1.085 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 272 ;10.437 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 86 ;38.597 ;24.884
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 424 ;25.179 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 14 ;18.836 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 361 ; 0.204 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2321 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 376 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 748 ; 0.298 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2381 ; 0.208 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1129 ; 0.219 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1469 ; 0.106 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 85 ; 0.190 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 1 ; 0.005 ; 0.200
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): 13 ; 0.267 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 39 ; 0.209 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.258 ; 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): 1680 ; 1.136 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 553 ; 0.151 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2236 ; 1.451 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 883 ; 1.908 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 685 ; 2.910 ; 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 : NULL
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 1ZW3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUN-05.
REMARK 100 THE DEPOSITION ID IS D_1000033190.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-NOV-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.1
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : DIAMOND (111), GE(220)
REMARK 200 OPTICS : TOROIDAL ZERODUR MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : NULL
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.07800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.8500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.37800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.030
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 1XWJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2M NAH2PO4/0.8M K2HPO4, 100MM CAPS,
REMARK 280 PH 10.5, PH 6.1, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 25.81050
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.08400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.81050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.08400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14670 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
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 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 -20
REMARK 465 GLY A -19
REMARK 465 SER A -18
REMARK 465 SER A -17
REMARK 465 HIS A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 SER A -10
REMARK 465 SER A -9
REMARK 465 GLY A -8
REMARK 465 LEU A -7
REMARK 465 VAL A -6
REMARK 465 PRO A -5
REMARK 465 ARG A -4
REMARK 465 GLY A -3
REMARK 465 SER A -2
REMARK 465 HIS A -1
REMARK 465 SER A 251
REMARK 465 TRP A 252
REMARK 465 ASP A 253
REMARK 465 GLU A 254
REMARK 465 ASP A 255
REMARK 465 ALA A 256
REMARK 465 TRP A 257
REMARK 465 ALA A 258
REMARK 465 PRO B 1628
REMARK 465 ARG B 1629
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 81 CG GLU A 81 CD 0.093
REMARK 500 CYS A 137 CB CYS A 137 SG -0.109
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 ASP A 109 CB - CG - OD2 ANGL. DEV. = -6.4 DEGREES
REMARK 500 PRO A 165 C - N - CA ANGL. DEV. = 13.1 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 GLN A 17 -75.37 -42.59
REMARK 500 GLU A 30 42.98 -147.83
REMARK 500 ALA A 35 -37.89 41.98
REMARK 500 ILE A 36 79.35 19.51
REMARK 500 ARG A 55 -59.90 -27.77
REMARK 500 THR A 63 -134.40 -77.37
REMARK 500 THR A 64 124.64 48.17
REMARK 500 THR A 85 -59.53 -27.04
REMARK 500 ALA A 91 -82.52 -62.43
REMARK 500 GLN A 92 -62.10 -8.12
REMARK 500 THR A 145 -50.25 -24.10
REMARK 500 GLU A 154 -70.78 -39.01
REMARK 500 THR A 196 -7.30 -38.36
REMARK 500 LYS A 198 -36.73 -25.61
REMARK 500 ILE A 222 -70.76 -48.97
REMARK 500 GLU A 223 -46.59 5.96
REMARK 500 THR B1649 -90.03 -39.53
REMARK 500 SER B1650 -15.68 -17.72
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 29 GLU A 30 -128.23
REMARK 500 GLU A 30 VAL A 31 143.33
REMARK 500 LYS A 34 ALA A 35 130.49
REMARK 500 ALA A 91 GLN A 92 145.02
REMARK 500 SER A 219 GLN A 220 -127.47
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ZVZ RELATED DB: PDB
REMARK 900 RELATED ID: 1ZW2 RELATED DB: PDB
DBREF 1ZW3 A 1 258 UNP P12003 VINC_CHICK 1 258
DBREF 1ZW3 B 1628 1652 UNP P26039 TLN1_MOUSE 1628 1652
SEQADV 1ZW3 MET A -20 UNP P12003 CLONING ARTIFACT
SEQADV 1ZW3 GLY A -19 UNP P12003 CLONING ARTIFACT
SEQADV 1ZW3 SER A -18 UNP P12003 CLONING ARTIFACT
SEQADV 1ZW3 SER A -17 UNP P12003 CLONING ARTIFACT
SEQADV 1ZW3 HIS A -16 UNP P12003 EXPRESSION TAG
SEQADV 1ZW3 HIS A -15 UNP P12003 EXPRESSION TAG
SEQADV 1ZW3 HIS A -14 UNP P12003 EXPRESSION TAG
SEQADV 1ZW3 HIS A -13 UNP P12003 EXPRESSION TAG
SEQADV 1ZW3 HIS A -12 UNP P12003 EXPRESSION TAG
SEQADV 1ZW3 HIS A -11 UNP P12003 EXPRESSION TAG
SEQADV 1ZW3 SER A -10 UNP P12003 CLONING ARTIFACT
SEQADV 1ZW3 SER A -9 UNP P12003 CLONING ARTIFACT
SEQADV 1ZW3 GLY A -8 UNP P12003 CLONING ARTIFACT
SEQADV 1ZW3 LEU A -7 UNP P12003 CLONING ARTIFACT
SEQADV 1ZW3 VAL A -6 UNP P12003 CLONING ARTIFACT
SEQADV 1ZW3 PRO A -5 UNP P12003 CLONING ARTIFACT
SEQADV 1ZW3 ARG A -4 UNP P12003 CLONING ARTIFACT
SEQADV 1ZW3 GLY A -3 UNP P12003 CLONING ARTIFACT
SEQADV 1ZW3 SER A -2 UNP P12003 CLONING ARTIFACT
SEQADV 1ZW3 HIS A -1 UNP P12003 CLONING ARTIFACT
SEQADV 1ZW3 MET A 0 UNP P12003 CLONING ARTIFACT
SEQRES 1 A 279 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 279 LEU VAL PRO ARG GLY SER HIS MET PRO VAL PHE HIS THR
SEQRES 3 A 279 ARG THR ILE GLU SER ILE LEU GLU PRO VAL ALA GLN GLN
SEQRES 4 A 279 ILE SER HIS LEU VAL ILE MET HIS GLU GLU GLY GLU VAL
SEQRES 5 A 279 ASP GLY LYS ALA ILE PRO ASP LEU THR ALA PRO VAL SER
SEQRES 6 A 279 ALA VAL GLN ALA ALA VAL SER ASN LEU VAL ARG VAL GLY
SEQRES 7 A 279 LYS GLU THR VAL GLN THR THR GLU ASP GLN ILE LEU LYS
SEQRES 8 A 279 ARG ASP MET PRO PRO ALA PHE ILE LYS VAL GLU ASN ALA
SEQRES 9 A 279 CYS THR LYS LEU VAL ARG ALA ALA GLN MET LEU GLN ALA
SEQRES 10 A 279 ASP PRO TYR SER VAL PRO ALA ARG ASP TYR LEU ILE ASP
SEQRES 11 A 279 GLY SER ARG GLY ILE LEU SER GLY THR SER ASP LEU LEU
SEQRES 12 A 279 LEU THR PHE ASP GLU ALA GLU VAL ARG LYS ILE ILE ARG
SEQRES 13 A 279 VAL CYS LYS GLY ILE LEU GLU TYR LEU THR VAL ALA GLU
SEQRES 14 A 279 VAL VAL GLU THR MET GLU ASP LEU VAL THR TYR THR LYS
SEQRES 15 A 279 ASN LEU GLY PRO GLY MET THR LYS MET ALA LYS MET ILE
SEQRES 16 A 279 ASP GLU ARG GLN GLN GLU LEU THR HIS GLN GLU HIS ARG
SEQRES 17 A 279 VAL MET LEU VAL ASN SER MET ASN THR VAL LYS GLU LEU
SEQRES 18 A 279 LEU PRO VAL LEU ILE SER ALA MET LYS ILE PHE VAL THR
SEQRES 19 A 279 THR LYS ASN THR LYS SER GLN GLY ILE GLU GLU ALA LEU
SEQRES 20 A 279 LYS ASN ARG ASN PHE THR VAL GLU LYS MET SER ALA GLU
SEQRES 21 A 279 ILE ASN GLU ILE ILE ARG VAL LEU GLN LEU THR SER TRP
SEQRES 22 A 279 ASP GLU ASP ALA TRP ALA
SEQRES 1 B 25 PRO ARG TRP SER VAL LEU ALA GLY HIS SER ARG THR VAL
SEQRES 2 B 25 SER ASP SER ILE LYS LYS LEU ILE THR SER MET ARG
HELIX 1 1 THR A 5 GLU A 28 1 24
HELIX 2 2 LEU A 39 THR A 63 1 25
HELIX 3 3 ASP A 66 ASP A 97 1 32
HELIX 4 4 SER A 100 ALA A 147 1 48
HELIX 5 5 THR A 152 GLN A 179 1 28
HELIX 6 6 HIS A 183 GLU A 199 1 17
HELIX 7 7 LEU A 200 THR A 217 1 18
HELIX 8 8 GLY A 221 GLN A 248 1 28
HELIX 9 9 TRP B 1630 SER B 1650 1 21
CRYST1 51.621 72.168 96.725 90.00 90.00 90.00 P 21 21 2 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 0.019372 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013857 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010339 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
