HEADER PROTEIN BINDING 09-JUL-07 2QK0
TITLE STRUCTURAL BASIS OF MICROTUBULE PLUS END TRACKING BY XMAP215, CLIP-170
TITLE 2 AND EB1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CAP-GLY DOMAIN-CONTAINING LINKER PROTEIN 1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: CAP-GLY DOMAIN 1;
COMPND 5 SYNONYM: RESTIN, CYTOPLASMIC LINKER PROTEIN 170 ALPHA-2, CLIP-170,
COMPND 6 REED-STERNBERG INTERMEDIATE FILAMENT-ASSOCIATED PROTEIN, CYTOPLASMIC
COMPND 7 LINKER PROTEIN 1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CLIP1, CYLN1, RSN;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 DE3 PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS CLIP-170, CAP-GLY DOMAIN, MICROTUBULE PLUS END, +TIP, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR K.C.SLEP,R.D.VALE
REVDAT 4 20-OCT-21 2QK0 1 SEQADV LINK
REVDAT 3 18-OCT-17 2QK0 1 REMARK
REVDAT 2 24-FEB-09 2QK0 1 VERSN
REVDAT 1 02-OCT-07 2QK0 0
JRNL AUTH K.C.SLEP,R.D.VALE
JRNL TITL STRUCTURAL BASIS OF MICROTUBULE PLUS END TRACKING BY
JRNL TITL 2 XMAP215, CLIP-170, AND EB1.
JRNL REF MOL.CELL V. 27 976 2007
JRNL REFN ISSN 1097-2765
JRNL PMID 17889670
JRNL DOI 10.1016/J.MOLCEL.2007.07.023
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.88
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 7778
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 10%
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.300
REMARK 3 FREE R VALUE TEST SET COUNT : 814
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 571
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 66
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 11.09
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.00700
REMARK 3 B22 (A**2) : -0.46000
REMARK 3 B33 (A**2) : -0.54800
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): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.204 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 1.637 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.276 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.325 ; 2.500
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2QK0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUL-07.
REMARK 100 THE DEPOSITION ID IS D_1000043694.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-JUL-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.2.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97964, 1.12713
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
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 : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7855
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : 4.60000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 37.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.07900
REMARK 200 R SYM FOR SHELL (I) : 7.90000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 15.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 32.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.82
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M SODIUM MALONATE, 100 MM GLYCINE,
REMARK 280 1.1 MM LANTHANUM CHLORIDE, PROTEIN CONCENTRATION 15 MG/ML, PH
REMARK 280 9.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 13.62100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 25.90300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 21.26650
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 25.90300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 13.62100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 21.26650
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 300 REMARK: CLIP-170 IS A HOMODIMER FORMED VIA A LARGE CENTRAL COILED
REMARK 300 COIL REGION NOT INCLUDED IN THIS CONSTRUCT. THIS CONSTRUCT EMBODIES
REMARK 300 ONLY CAP-GLY DOMAIN 1.
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 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 VAL A 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2QJX RELATED DB: PDB
REMARK 900 RELATED ID: 2QJZ RELATED DB: PDB
REMARK 900 RELATED ID: 2QK1 RELATED DB: PDB
REMARK 900 RELATED ID: 2QK2 RELATED DB: PDB
DBREF 2QK0 A 30 101 UNP P30622 CLIP1_HUMAN 57 128
SEQADV 2QK0 GLY A 28 UNP P30622 EXPRESSION TAG
SEQADV 2QK0 SER A 29 UNP P30622 EXPRESSION TAG
SEQADV 2QK0 MSE A 97 UNP P30622 LEU 124 ENGINEERED MUTATION
SEQRES 1 A 74 GLY SER ASP PHE ARG VAL GLY GLU ARG VAL TRP VAL ASN
SEQRES 2 A 74 GLY ASN LYS PRO GLY PHE ILE GLN PHE LEU GLY GLU THR
SEQRES 3 A 74 GLN PHE ALA PRO GLY GLN TRP ALA GLY ILE VAL LEU ASP
SEQRES 4 A 74 GLU PRO ILE GLY LYS ASN ASP GLY SER VAL ALA GLY VAL
SEQRES 5 A 74 ARG TYR PHE GLN CYS GLU PRO LEU LYS GLY ILE PHE THR
SEQRES 6 A 74 ARG PRO SER LYS MSE THR ARG LYS VAL
MODRES 2QK0 MSE A 97 MET SELENOMETHIONINE
HET MSE A 97 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE C5 H11 N O2 SE
FORMUL 2 HOH *66(H2 O)
HELIX 1 1 ARG A 93 SER A 95 5 3
SHEET 1 A 5 GLY A 89 THR A 92 0
SHEET 2 A 5 TRP A 60 LEU A 65 -1 N ILE A 63 O ILE A 90
SHEET 3 A 5 LYS A 43 GLY A 51 -1 N GLN A 48 O GLY A 62
SHEET 4 A 5 ARG A 36 VAL A 39 -1 N VAL A 37 O GLY A 45
SHEET 5 A 5 MSE A 97 THR A 98 -1 O THR A 98 N TRP A 38
SHEET 1 B 2 SER A 75 VAL A 76 0
SHEET 2 B 2 VAL A 79 ARG A 80 -1 O VAL A 79 N VAL A 76
LINK C LYS A 96 N MSE A 97 1555 1555 1.33
LINK C MSE A 97 N THR A 98 1555 1555 1.33
CRYST1 27.242 42.533 51.806 90.00 90.00 90.00 P 21 21 21 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 0.036708 0.000000 0.000000 0.00000
SCALE2 0.000000 0.023511 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019303 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
