HEADER CELL CYCLE 23-MAY-09 3HKC
TITLE TUBULIN-ABT751: RB3 STATHMIN-LIKE DOMAIN COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TUBULIN ALPHA CHAIN;
COMPND 3 CHAIN: A, C;
COMPND 4 MOL_ID: 2;
COMPND 5 MOLECULE: TUBULIN BETA CHAIN;
COMPND 6 CHAIN: B, D;
COMPND 7 MOL_ID: 3;
COMPND 8 MOLECULE: STATHMIN-4;
COMPND 9 CHAIN: E;
COMPND 10 FRAGMENT: RB3 STATHMIN-LIKE DOMAIN;
COMPND 11 SYNONYM: STATHMIN-LIKE PROTEIN B3, RB3;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: OVIS ARIES;
SOURCE 3 ORGANISM_COMMON: SHEEP;
SOURCE 4 ORGANISM_TAXID: 9940;
SOURCE 5 ORGAN: BRAIN;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: OVIS ARIES;
SOURCE 8 ORGANISM_COMMON: SHEEP;
SOURCE 9 ORGANISM_TAXID: 9940;
SOURCE 10 ORGAN: BRAIN;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 13 ORGANISM_COMMON: RAT;
SOURCE 14 ORGANISM_TAXID: 10116;
SOURCE 15 GENE: STMN4;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET-8C
KEYWDS ALPHA-TUBULIN, BETA-TUBULIN, COLCHICINE DOMAIN, GTPASE MICROTUBULE,
KEYWDS 2 STATHMIN, TUBULIN, CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.DORLEANS,B.GIGANT,R.B.G.RAVELLI,P.MAILLIET,V.MIKOL,M.KNOSSOW
REVDAT 2 01-NOV-23 3HKC 1 REMARK DBREF SEQADV
REVDAT 1 01-SEP-09 3HKC 0
JRNL AUTH A.DORLEANS,B.GIGANT,R.B.G.RAVELLI,P.MAILLIET,V.MIKOL,
JRNL AUTH 2 M.KNOSSOW
JRNL TITL VARIATIONS IN THE COLCHICINE-BINDING DOMAIN PROVIDE INSIGHT
JRNL TITL 2 INTO THE STRUCTURAL SWITCH OF TUBULIN
JRNL REF PROC.NATL.ACAD.SCI.USA V. 106 13775 2009
JRNL REFN ISSN 0027-8424
JRNL PMID 19666559
JRNL DOI 10.1073/PNAS.0904223106
REMARK 2
REMARK 2 RESOLUTION. 3.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 3.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 31204
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1664
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) : 3.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1789
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3500
REMARK 3 BIN FREE R VALUE SET COUNT : 104
REMARK 3 BIN FREE R VALUE : 0.3390
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 13970
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 175
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) : 50.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.57000
REMARK 3 B22 (A**2) : 1.57000
REMARK 3 B33 (A**2) : -2.35000
REMARK 3 B12 (A**2) : 0.78000
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): 0.658
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.647
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 50.161
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.956
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 14457 ; 0.016 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 19660 ; 1.738 ; 1.954
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1805 ; 8.561 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2168 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11111 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 7191 ; 0.285 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 521 ; 0.206 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 2 ; 0.420 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 44 ; 0.340 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 3 ; 0.301 ; 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): 9028 ; 0.222 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 14467 ; 0.441 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 5429 ; 0.703 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5193 ; 1.154 ; 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 : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 2 A 437
REMARK 3 RESIDUE RANGE : E 4 E 64
REMARK 3 ORIGIN FOR THE GROUP (A): 136.1550 105.6250 17.1480
REMARK 3 T TENSOR
REMARK 3 T11: 1.4401 T22: 1.4466
REMARK 3 T33: 1.7508 T12: -0.1208
REMARK 3 T13: 0.0509 T23: 0.0296
REMARK 3 L TENSOR
REMARK 3 L11: 9.0535 L22: 3.2498
REMARK 3 L33: 3.0341 L12: 1.5620
REMARK 3 L13: 0.1196 L23: -0.4806
REMARK 3 S TENSOR
REMARK 3 S11: 0.0788 S12: -0.4401 S13: 0.8621
REMARK 3 S21: 0.0753 S22: -0.1320 S23: -0.0110
REMARK 3 S31: -0.4350 S32: 0.1119 S33: 0.0532
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 2 B 438
REMARK 3 RESIDUE RANGE : E 65 E 89
REMARK 3 ORIGIN FOR THE GROUP (A): 102.3620 81.3780 5.3180
REMARK 3 T TENSOR
REMARK 3 T11: 1.5179 T22: 2.0264
REMARK 3 T33: 1.5267 T12: -0.3591
REMARK 3 T13: -0.1792 T23: 0.1711
REMARK 3 L TENSOR
REMARK 3 L11: 8.9840 L22: 4.9319
REMARK 3 L33: 3.9266 L12: 2.0932
REMARK 3 L13: -1.3401 L23: -0.6263
REMARK 3 S TENSOR
REMARK 3 S11: -0.1708 S12: 0.1360 S13: -0.5835
REMARK 3 S21: -0.3907 S22: 0.0339 S23: -0.3789
REMARK 3 S31: 0.3362 S32: -0.2624 S33: 0.1369
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 2 C 437
REMARK 3 RESIDUE RANGE : E 90 E 115
REMARK 3 ORIGIN FOR THE GROUP (A): 64.2340 61.6400 -2.9810
REMARK 3 T TENSOR
REMARK 3 T11: 1.7095 T22: 2.4058
REMARK 3 T33: 1.8160 T12: -0.3788
REMARK 3 T13: -0.4771 T23: 0.4132
REMARK 3 L TENSOR
REMARK 3 L11: 9.3224 L22: 4.6052
REMARK 3 L33: 4.4302 L12: 2.4231
REMARK 3 L13: 0.1908 L23: -0.4134
REMARK 3 S TENSOR
REMARK 3 S11: -0.1406 S12: 0.6039 S13: -0.4396
REMARK 3 S21: -0.5742 S22: 0.3485 S23: -0.4644
REMARK 3 S31: 0.0837 S32: 0.4925 S33: -0.2079
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 2 D 438
REMARK 3 RESIDUE RANGE : E 116 E 141
REMARK 3 ORIGIN FOR THE GROUP (A): 24.6080 48.2320 -5.6970
REMARK 3 T TENSOR
REMARK 3 T11: 1.1668 T22: 2.5206
REMARK 3 T33: 2.0510 T12: -0.1500
REMARK 3 T13: -1.0808 T23: 0.1989
REMARK 3 L TENSOR
REMARK 3 L11: 8.2088 L22: 5.6228
REMARK 3 L33: 7.5163 L12: 2.0734
REMARK 3 L13: -1.0016 L23: 0.4180
REMARK 3 S TENSOR
REMARK 3 S11: -0.3446 S12: 0.5736 S13: 0.2396
REMARK 3 S21: -0.1861 S22: -0.4627 S23: 0.7692
REMARK 3 S31: 0.3136 S32: -0.5122 S33: 0.8073
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3HKC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 28-MAY-09.
REMARK 100 THE DEPOSITION ID IS D_1000053239.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-FEB-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 7.00
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) : 0.978
REMARK 200 MONOCHROMATOR : CHANNEL CUT ESRF MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33069
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.800
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 (%) : 97.6
REMARK 200 DATA REDUNDANCY : 4.170
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.1
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.65500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.940
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1SA0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 68.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.88
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG, PIPES BUFFER, PH 7.00, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 35.91333
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 17.95667
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 26.93500
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 8.97833
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 44.89167
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: PENTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17150 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 64690 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -118.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E
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 1
REMARK 465 SER A 38
REMARK 465 ASP A 39
REMARK 465 LYS A 40
REMARK 465 THR A 41
REMARK 465 ILE A 42
REMARK 465 GLY A 43
REMARK 465 GLY A 44
REMARK 465 GLY A 45
REMARK 465 ASP A 46
REMARK 465 ASP A 438
REMARK 465 SER A 439
REMARK 465 VAL A 440
REMARK 465 GLU A 441
REMARK 465 GLY A 442
REMARK 465 GLU A 443
REMARK 465 GLY A 444
REMARK 465 GLU A 445
REMARK 465 GLU A 446
REMARK 465 GLU A 447
REMARK 465 GLY A 448
REMARK 465 GLU A 449
REMARK 465 GLU A 450
REMARK 465 TYR A 451
REMARK 465 MET B 1
REMARK 465 ARG B 278
REMARK 465 GLY B 279
REMARK 465 SER B 280
REMARK 465 GLN B 281
REMARK 465 GLN B 282
REMARK 465 TYR B 283
REMARK 465 ARG B 284
REMARK 465 ALA B 285
REMARK 465 THR B 439
REMARK 465 ALA B 440
REMARK 465 ASP B 441
REMARK 465 GLU B 442
REMARK 465 GLN B 443
REMARK 465 GLY B 444
REMARK 465 GLU B 445
REMARK 465 PHE B 446
REMARK 465 GLU B 447
REMARK 465 GLU B 448
REMARK 465 GLU B 449
REMARK 465 GLU B 450
REMARK 465 GLY B 451
REMARK 465 GLU B 452
REMARK 465 ASP B 453
REMARK 465 GLU B 454
REMARK 465 ALA B 455
REMARK 465 MET C 1
REMARK 465 GLY C 44
REMARK 465 GLY C 45
REMARK 465 ASP C 46
REMARK 465 LYS C 280
REMARK 465 ALA C 281
REMARK 465 TYR C 282
REMARK 465 HIS C 283
REMARK 465 GLU C 284
REMARK 465 ASP C 438
REMARK 465 SER C 439
REMARK 465 VAL C 440
REMARK 465 GLU C 441
REMARK 465 GLY C 442
REMARK 465 GLU C 443
REMARK 465 GLY C 444
REMARK 465 GLU C 445
REMARK 465 GLU C 446
REMARK 465 GLU C 447
REMARK 465 GLY C 448
REMARK 465 GLU C 449
REMARK 465 GLU C 450
REMARK 465 TYR C 451
REMARK 465 MET D 1
REMARK 465 ARG D 278
REMARK 465 GLY D 279
REMARK 465 SER D 280
REMARK 465 GLN D 281
REMARK 465 GLN D 282
REMARK 465 TYR D 283
REMARK 465 ARG D 284
REMARK 465 ALA D 285
REMARK 465 THR D 439
REMARK 465 ALA D 440
REMARK 465 ASP D 441
REMARK 465 GLU D 442
REMARK 465 GLN D 443
REMARK 465 GLY D 444
REMARK 465 GLU D 445
REMARK 465 PHE D 446
REMARK 465 GLU D 447
REMARK 465 GLU D 448
REMARK 465 GLU D 449
REMARK 465 GLU D 450
REMARK 465 GLY D 451
REMARK 465 GLU D 452
REMARK 465 ASP D 453
REMARK 465 GLU D 454
REMARK 465 ALA D 455
REMARK 465 GLY E 31
REMARK 465 VAL E 32
REMARK 465 PRO E 33
REMARK 465 GLU E 34
REMARK 465 PHE E 35
REMARK 465 ASN E 36
REMARK 465 ALA E 37
REMARK 465 SER E 38
REMARK 465 LEU E 39
REMARK 465 PRO E 40
REMARK 465 ARG E 41
REMARK 465 ARG E 42
REMARK 465 ARG E 43
REMARK 465 ASP E 44
REMARK 465 GLU E 142
REMARK 465 ALA E 143
REMARK 465 SER E 144
REMARK 465 ARG E 145
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 GLN A 35 CG CD OE1 NE2
REMARK 470 ASP A 47 CG OD1 OD2
REMARK 470 THR A 51 OG1 CG2
REMARK 470 THR A 56 OG1 CG2
REMARK 470 GLU A 77 CG CD OE1 OE2
REMARK 470 ARG A 221 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 285 CG CD OE1 NE2
REMARK 470 ARG A 308 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 335 CG1 CG2 CD1
REMARK 470 LYS A 336 CG CD CE NZ
REMARK 470 LYS A 338 CG CD CE NZ
REMARK 470 GLN A 342 CG CD OE1 NE2
REMARK 470 VAL A 437 N CG1 CG2
REMARK 470 HIS B 37 CG ND1 CD2 CE1 NE2
REMARK 470 THR B 57 OG1 CG2
REMARK 470 ASN B 59 CG OD1 ND2
REMARK 470 LYS B 124 CG CD CE NZ
REMARK 470 SER B 126 OG
REMARK 470 MET B 172 CG SD CE
REMARK 470 LYS B 218 CG CD CE NZ
REMARK 470 LEU B 219 CG CD1 CD2
REMARK 470 SER B 298 OG
REMARK 470 ARG B 322 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 326 CG CD CE NZ
REMARK 470 LYS B 338 CG CD CE NZ
REMARK 470 ARG B 369 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 372 CG CD CE NZ
REMARK 470 ASP B 437 CG OD1 OD2
REMARK 470 ASP C 33 CG OD1 OD2
REMARK 470 GLN C 35 CG CD OE1 NE2
REMARK 470 MET C 36 CG SD CE
REMARK 470 SER C 38 OG
REMARK 470 ASP C 39 CG OD1 OD2
REMARK 470 LYS C 40 CG CD CE NZ
REMARK 470 ILE C 42 CG1 CG2 CD1
REMARK 470 ASP C 47 CG OD1 OD2
REMARK 470 SER C 48 OG
REMARK 470 GLU C 55 CG CD OE1 OE2
REMARK 470 THR C 56 OG1 CG2
REMARK 470 ARG C 221 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 279 CG CD OE1 OE2
REMARK 470 GLN C 285 CG CD OE1 NE2
REMARK 470 ARG C 308 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 326 CG CD CE NZ
REMARK 470 ILE C 335 CG1 CG2 CD1
REMARK 470 LYS C 338 CG CD CE NZ
REMARK 470 ARG C 339 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 342 CG CD OE1 NE2
REMARK 470 LYS C 352 CG CD CE NZ
REMARK 470 HIS D 37 CG ND1 CD2 CE1 NE2
REMARK 470 THR D 57 OG1 CG2
REMARK 470 ASN D 59 CG OD1 ND2
REMARK 470 SER D 126 OG
REMARK 470 MET D 172 CG SD CE
REMARK 470 ARG D 215 CG CD NE CZ NH1 NH2
REMARK 470 LEU D 217 CG CD1 CD2
REMARK 470 LEU D 219 CG CD1 CD2
REMARK 470 SER D 298 OG
REMARK 470 ARG D 322 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 326 CG CD CE NZ
REMARK 470 LYS D 338 CG CD CE NZ
REMARK 470 ARG D 369 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 372 CG CD CE NZ
REMARK 470 ASP D 437 CG OD1 OD2
REMARK 470 GLU E 7 CG CD OE1 OE2
REMARK 470 VAL E 8 CG1 CG2
REMARK 470 ILE E 9 CG1 CG2 CD1
REMARK 470 SER E 19 OG
REMARK 470 ILE E 23 CG1 CG2 CD1
REMARK 470 LYS E 25 CG CD CE NZ
REMARK 470 PHE E 29 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ASP E 30 CG OD1 OD2
REMARK 470 SER E 46 OG
REMARK 470 LEU E 47 CG CD1 CD2
REMARK 470 ILE E 50 CG1 CG2 CD1
REMARK 470 LEU E 68 CG CD1 CD2
REMARK 470 VAL E 82 CG1 CG2
REMARK 470 ILE E 83 CG1 CG2 CD1
REMARK 470 LYS E 85 CG CD CE NZ
REMARK 470 GLU E 88 CG CD OE1 OE2
REMARK 470 LYS E 95 CG CD CE NZ
REMARK 470 LYS E 100 CG CD CE NZ
REMARK 470 GLN E 103 CG CD OE1 NE2
REMARK 470 GLU E 110 CG CD OE1 OE2
REMARK 470 LEU E 116 CG CD1 CD2
REMARK 470 LYS E 128 CG CD CE NZ
REMARK 470 GLU E 131 CG CD OE1 OE2
REMARK 470 GLU E 132 CG CD OE1 OE2
REMARK 470 LYS E 135 CG CD CE NZ
REMARK 470 LYS E 137 CG CD CE NZ
REMARK 470 GLU E 138 CG CD OE1 OE2
REMARK 470 LEU E 139 CG CD1 CD2
REMARK 470 LYS E 140 CG CD CE NZ
REMARK 470 GLU E 141 CG CD OE1 OE2
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 O2B GTP A 600 MG MG A 601 1.56
REMARK 500 O2B GTP C 600 MG MG C 601 1.58
REMARK 500 OH TYR D 36 O SER D 40 2.05
REMARK 500 O PHE A 296 NH2 ARG A 339 2.06
REMARK 500 O ASP B 306 N ARG B 308 2.07
REMARK 500 NH2 ARG B 401 O GLU C 434 2.09
REMARK 500 OH TYR B 36 O SER B 40 2.13
REMARK 500 O ARG E 76 N HIS E 78 2.13
REMARK 500 O ASP D 306 N ARG D 308 2.14
REMARK 500 O LEU B 114 N ASP B 116 2.17
REMARK 500 O ALA B 403 N LEU B 405 2.18
REMARK 500 O LEU D 114 N ASP D 116 2.19
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 CYS A 20 CA - CB - SG ANGL. DEV. = 11.4 DEGREES
REMARK 500 ASP A 76 CB - CG - OD2 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ASP A 120 CB - CG - OD2 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ASP A 160 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP A 211 CB - CG - OD2 ANGL. DEV. = 5.9 DEGREES
REMARK 500 HIS A 266 CB - CA - C ANGL. DEV. = -13.0 DEGREES
REMARK 500 LEU A 397 CA - CB - CG ANGL. DEV. = 15.5 DEGREES
REMARK 500 ASP B 39 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP B 116 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP B 205 CB - CG - OD2 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ASP B 427 CB - CG - OD2 ANGL. DEV. = 7.7 DEGREES
REMARK 500 ASP C 76 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP C 120 CB - CG - OD2 ANGL. DEV. = 6.7 DEGREES
REMARK 500 ASP C 211 CB - CG - OD2 ANGL. DEV. = 7.6 DEGREES
REMARK 500 HIS C 266 CB - CA - C ANGL. DEV. = -12.2 DEGREES
REMARK 500 LEU C 397 CA - CB - CG ANGL. DEV. = 15.0 DEGREES
REMARK 500 ASP D 120 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP D 163 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG D 164 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ASP D 226 CB - CG - OD2 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP D 427 CB - CG - OD2 ANGL. DEV. = 5.6 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 CYS A 4 97.11 -174.90
REMARK 500 ASN A 18 -32.74 -36.03
REMARK 500 PRO A 32 -42.84 -21.98
REMARK 500 SER A 48 -84.54 100.42
REMARK 500 HIS A 61 28.47 -154.41
REMARK 500 VAL A 62 133.65 -32.51
REMARK 500 PRO A 72 -78.18 -67.24
REMARK 500 THR A 73 -77.15 21.74
REMARK 500 ARG A 79 32.45 -84.33
REMARK 500 TYR A 83 -29.88 102.08
REMARK 500 ARG A 84 -37.40 -35.31
REMARK 500 PRO A 89 -32.68 -39.53
REMARK 500 LYS A 96 -53.99 65.85
REMARK 500 THR A 109 -68.73 -96.20
REMARK 500 LYS A 112 -34.46 -28.85
REMARK 500 GLN A 128 57.43 -101.43
REMARK 500 GLN A 133 -67.27 -94.57
REMARK 500 SER A 151 -71.50 -50.79
REMARK 500 LYS A 163 -78.34 -73.04
REMARK 500 LYS A 164 99.74 16.20
REMARK 500 PRO A 175 -66.93 -24.76
REMARK 500 THR A 191 -26.91 -28.65
REMARK 500 ALA A 240 -55.49 -29.24
REMARK 500 ASP A 245 119.65 90.20
REMARK 500 ALA A 247 154.80 45.81
REMARK 500 LEU A 248 108.70 37.36
REMARK 500 PRO A 263 -32.17 -36.47
REMARK 500 ILE A 265 81.34 -55.42
REMARK 500 ALA A 273 -94.28 -79.93
REMARK 500 GLU A 279 -35.00 122.35
REMARK 500 ALA A 281 -11.44 -47.20
REMARK 500 HIS A 283 -122.77 -97.12
REMARK 500 VAL A 288 -38.29 -37.51
REMARK 500 ASN A 293 4.08 -66.90
REMARK 500 GLU A 297 114.32 177.72
REMARK 500 GLN A 301 -170.98 -68.07
REMARK 500 MET A 302 -7.07 -143.17
REMARK 500 LYS A 304 100.99 -49.95
REMARK 500 CYS A 305 -130.16 -147.56
REMARK 500 ASP A 306 101.47 175.94
REMARK 500 ALA A 314 126.26 171.37
REMARK 500 LYS A 326 -27.10 -37.37
REMARK 500 ARG A 339 -171.72 -175.24
REMARK 500 ILE A 341 -85.41 -45.75
REMARK 500 ASP A 345 -64.42 23.88
REMARK 500 CYS A 347 113.69 -170.27
REMARK 500 PRO A 348 -106.38 -14.39
REMARK 500 THR A 349 28.28 -161.90
REMARK 500 PHE A 351 63.56 78.25
REMARK 500 GLN A 358 105.41 -52.92
REMARK 500
REMARK 500 THIS ENTRY HAS 271 RAMACHANDRAN OUTLIERS.
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 THR A 82 TYR A 83 -147.55
REMARK 500 HIS A 283 GLU A 284 149.08
REMARK 500 PRO B 162 ASP B 163 129.80
REMARK 500 LEU B 248 ASN B 249 145.94
REMARK 500 PRO D 162 ASP D 163 134.72
REMARK 500 LEU D 248 ASN D 249 139.70
REMARK 500 ASP E 5 MET E 6 -138.15
REMARK 500 ILE E 50 GLN E 51 141.51
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP A 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE E70 B 700
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP C 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP D 600
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE E70 D 700
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1SA0 RELATED DB: PDB
REMARK 900 TUBULIN-COLCHICINE: RB3 STATHMIN-LIKE DOMAIN COMPLEX
REMARK 900 RELATED ID: 1SA1 RELATED DB: PDB
REMARK 900 TUBULIN-PODOPHYLLOTOXIN: RB3 STATHMIN-LIKE DOMAIN COMPLEX
REMARK 900 RELATED ID: 3HKB RELATED DB: PDB
REMARK 900 TUBULIN: RB3 STATHMIN-LIKE DOMAIN COMPLEX
REMARK 900 RELATED ID: 3HKD RELATED DB: PDB
REMARK 900 TUBULIN-TN16 : RB3 STATHMIN-LIKE DOMAIN COMPLEX
REMARK 900 RELATED ID: 3HKE RELATED DB: PDB
REMARK 900 TUBULIN-T138067: RB3 STATHMIN-LIKE DOMAIN COMPLEX
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THERE IS ONE COMPLEX IN THE ASYMMETRIC UNIT, WHICH CONSISTS OF TWO
REMARK 999 ALPHA-BETA TUBULIN HETERODIMERS (CHAINS A-B AND C-D), AND ONE
REMARK 999 STATHMIN-LIKE DOMAIN OF RB3 (RB3-SLD) WHICH CORRESPONDS TO STAHMIN
REMARK 999 RESIDUES 5 TO 145 WITH THE ADDITION OF ONE ACETYLATED ALANINE AT
REMARK 999 THE N-TERMINUS. THE NUMBERING OF RB3-SLD IS ACCORDING TO THE
REMARK 999 STATHMIN SEQUENCE. ALPHA-TUBULIN AND BETA-TUBULIN HAVE BEEN ALIGNED
REMARK 999 AS IN NOGALES ET AL., NATURE VOL 391,199-203. IN THIS ALIGNMENT,
REMARK 999 RESIDUES 45-46 AND 361-368 OF ALPHA-TUBULIN ARE MISSING IN BETA-
REMARK 999 TUBULIN. AS THE SEQUENCE OF OVIS ARIES(SHEEP) TUBULIN IS NOT
REMARK 999 AVAILABLE, THE BOS TAURUS TUBULIN SEQUENCES (ALPHA: ISOTYPE 1A, GI:
REMARK 999 194666935, BETA: ISOTYPE 2, GI:51491829) WERE USED AS A REFERENCE
REMARK 999 BUT FOR THE ILE TO VAL SUBSTITUTION AT POSITION 318 ON BETA
REMARK 999 TUBULIN. THIS IS BASED ON DIFFERENCES BETWEEN TUBULIN ISOTYPES AND
REMARK 999 ON THE RELATIVE EXPRESSION ON THESE ISOTYPES IN MAMMALIAN BRAIN.
DBREF 3HKC A 1 451 PDB 3HKC 3HKC 1 451
DBREF 3HKC B 1 455 PDB 3HKC 3HKC 1 455
DBREF 3HKC C 1 451 PDB 3HKC 3HKC 1 451
DBREF 3HKC D 1 455 PDB 3HKC 3HKC 1 455
DBREF 3HKC E 5 145 UNP P63043 STMN4_RAT 49 189
SEQADV 3HKC ALA E 4 UNP P63043 EXPRESSION TAG
SEQRES 1 A 451 MET ARG GLU CYS ILE SER ILE HIS VAL GLY GLN ALA GLY
SEQRES 2 A 451 VAL GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR CYS LEU
SEQRES 3 A 451 GLU HIS GLY ILE GLN PRO ASP GLY GLN MET PRO SER ASP
SEQRES 4 A 451 LYS THR ILE GLY GLY GLY ASP ASP SER PHE ASN THR PHE
SEQRES 5 A 451 PHE SER GLU THR GLY ALA GLY LYS HIS VAL PRO ARG ALA
SEQRES 6 A 451 VAL PHE VAL ASP LEU GLU PRO THR VAL ILE ASP GLU VAL
SEQRES 7 A 451 ARG THR GLY THR TYR ARG GLN LEU PHE HIS PRO GLU GLN
SEQRES 8 A 451 LEU ILE THR GLY LYS GLU ASP ALA ALA ASN ASN TYR ALA
SEQRES 9 A 451 ARG GLY HIS TYR THR ILE GLY LYS GLU ILE ILE ASP LEU
SEQRES 10 A 451 VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS THR
SEQRES 11 A 451 GLY LEU GLN GLY PHE LEU VAL PHE HIS SER PHE GLY GLY
SEQRES 12 A 451 GLY THR GLY SER GLY PHE THR SER LEU LEU MET GLU ARG
SEQRES 13 A 451 LEU SER VAL ASP TYR GLY LYS LYS SER LYS LEU GLU PHE
SEQRES 14 A 451 SER ILE TYR PRO ALA PRO GLN VAL SER THR ALA VAL VAL
SEQRES 15 A 451 GLU PRO TYR ASN SER ILE LEU THR THR HIS THR THR LEU
SEQRES 16 A 451 GLU HIS SER ASP CYS ALA PHE MET VAL ASP ASN GLU ALA
SEQRES 17 A 451 ILE TYR ASP ILE CYS ARG ARG ASN LEU ASP ILE GLU ARG
SEQRES 18 A 451 PRO THR TYR THR ASN LEU ASN ARG LEU ILE GLY GLN ILE
SEQRES 19 A 451 VAL SER SER ILE THR ALA SER LEU ARG PHE ASP GLY ALA
SEQRES 20 A 451 LEU ASN VAL ASP LEU THR GLU PHE GLN THR ASN LEU VAL
SEQRES 21 A 451 PRO TYR PRO ARG ILE HIS PHE PRO LEU ALA THR TYR ALA
SEQRES 22 A 451 PRO VAL ILE SER ALA GLU LYS ALA TYR HIS GLU GLN LEU
SEQRES 23 A 451 SER VAL ALA GLU ILE THR ASN ALA CYS PHE GLU PRO ALA
SEQRES 24 A 451 ASN GLN MET VAL LYS CYS ASP PRO ARG HIS GLY LYS TYR
SEQRES 25 A 451 MET ALA CYS CYS LEU LEU TYR ARG GLY ASP VAL VAL PRO
SEQRES 26 A 451 LYS ASP VAL ASN ALA ALA ILE ALA THR ILE LYS THR LYS
SEQRES 27 A 451 ARG THR ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE
SEQRES 28 A 451 LYS VAL GLY ILE ASN TYR GLN PRO PRO THR VAL VAL PRO
SEQRES 29 A 451 GLY GLY ASP LEU ALA LYS VAL GLN ARG ALA VAL CYS MET
SEQRES 30 A 451 LEU SER ASN THR THR ALA ILE ALA GLU ALA TRP ALA ARG
SEQRES 31 A 451 LEU ASP HIS LYS PHE ASP LEU MET TYR ALA LYS ARG ALA
SEQRES 32 A 451 PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU GLY
SEQRES 33 A 451 GLU PHE SER GLU ALA ARG GLU ASP MET ALA ALA LEU GLU
SEQRES 34 A 451 LYS ASP TYR GLU GLU VAL GLY VAL ASP SER VAL GLU GLY
SEQRES 35 A 451 GLU GLY GLU GLU GLU GLY GLU GLU TYR
SEQRES 1 B 445 MET ARG GLU ILE VAL HIS ILE GLN ALA GLY GLN CYS GLY
SEQRES 2 B 445 ASN GLN ILE GLY ALA LYS PHE TRP GLU VAL ILE SER ASP
SEQRES 3 B 445 GLU HIS GLY ILE ASP PRO THR GLY SER TYR HIS GLY ASP
SEQRES 4 B 445 SER ASP LEU GLN LEU GLU ARG ILE ASN VAL TYR TYR ASN
SEQRES 5 B 445 GLU ALA THR GLY ASN LYS TYR VAL PRO ARG ALA ILE LEU
SEQRES 6 B 445 VAL ASP LEU GLU PRO GLY THR MET ASP SER VAL ARG SER
SEQRES 7 B 445 GLY PRO PHE GLY GLN ILE PHE ARG PRO ASP ASN PHE VAL
SEQRES 8 B 445 PHE GLY GLN SER GLY ALA GLY ASN ASN TRP ALA LYS GLY
SEQRES 9 B 445 HIS TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL LEU
SEQRES 10 B 445 ASP VAL VAL ARG LYS GLU SER GLU SER CYS ASP CYS LEU
SEQRES 11 B 445 GLN GLY PHE GLN LEU THR HIS SER LEU GLY GLY GLY THR
SEQRES 12 B 445 GLY SER GLY MET GLY THR LEU LEU ILE SER LYS ILE ARG
SEQRES 13 B 445 GLU GLU TYR PRO ASP ARG ILE MET ASN THR PHE SER VAL
SEQRES 14 B 445 MET PRO SER PRO LYS VAL SER ASP THR VAL VAL GLU PRO
SEQRES 15 B 445 TYR ASN ALA THR LEU SER VAL HIS GLN LEU VAL GLU ASN
SEQRES 16 B 445 THR ASP GLU THR TYR SER ILE ASP ASN GLU ALA LEU TYR
SEQRES 17 B 445 ASP ILE CYS PHE ARG THR LEU LYS LEU THR THR PRO THR
SEQRES 18 B 445 TYR GLY ASP LEU ASN HIS LEU VAL SER ALA THR MET SER
SEQRES 19 B 445 GLY VAL THR THR CYS LEU ARG PHE PRO GLY GLN LEU ASN
SEQRES 20 B 445 ALA ASP LEU ARG LYS LEU ALA VAL ASN MET VAL PRO PHE
SEQRES 21 B 445 PRO ARG LEU HIS PHE PHE MET PRO GLY PHE ALA PRO LEU
SEQRES 22 B 445 THR SER ARG GLY SER GLN GLN TYR ARG ALA LEU THR VAL
SEQRES 23 B 445 PRO GLU LEU THR GLN GLN MET PHE ASP SER LYS ASN MET
SEQRES 24 B 445 MET ALA ALA CYS ASP PRO ARG HIS GLY ARG TYR LEU THR
SEQRES 25 B 445 VAL ALA ALA VAL PHE ARG GLY ARG MET SER MET LYS GLU
SEQRES 26 B 445 VAL ASP GLU GLN MET LEU ASN VAL GLN ASN LYS ASN SER
SEQRES 27 B 445 SER TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL LYS THR
SEQRES 28 B 445 ALA VAL CYS ASP ILE PRO PRO ARG GLY LEU LYS MET SER
SEQRES 29 B 445 ALA THR PHE ILE GLY ASN SER THR ALA ILE GLN GLU LEU
SEQRES 30 B 445 PHE LYS ARG ILE SER GLU GLN PHE THR ALA MET PHE ARG
SEQRES 31 B 445 ARG LYS ALA PHE LEU HIS TRP TYR THR GLY GLU GLY MET
SEQRES 32 B 445 ASP GLU MET GLU PHE THR GLU ALA GLU SER ASN MET ASN
SEQRES 33 B 445 ASP LEU VAL SER GLU TYR GLN GLN TYR GLN ASP ALA THR
SEQRES 34 B 445 ALA ASP GLU GLN GLY GLU PHE GLU GLU GLU GLU GLY GLU
SEQRES 35 B 445 ASP GLU ALA
SEQRES 1 C 451 MET ARG GLU CYS ILE SER ILE HIS VAL GLY GLN ALA GLY
SEQRES 2 C 451 VAL GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR CYS LEU
SEQRES 3 C 451 GLU HIS GLY ILE GLN PRO ASP GLY GLN MET PRO SER ASP
SEQRES 4 C 451 LYS THR ILE GLY GLY GLY ASP ASP SER PHE ASN THR PHE
SEQRES 5 C 451 PHE SER GLU THR GLY ALA GLY LYS HIS VAL PRO ARG ALA
SEQRES 6 C 451 VAL PHE VAL ASP LEU GLU PRO THR VAL ILE ASP GLU VAL
SEQRES 7 C 451 ARG THR GLY THR TYR ARG GLN LEU PHE HIS PRO GLU GLN
SEQRES 8 C 451 LEU ILE THR GLY LYS GLU ASP ALA ALA ASN ASN TYR ALA
SEQRES 9 C 451 ARG GLY HIS TYR THR ILE GLY LYS GLU ILE ILE ASP LEU
SEQRES 10 C 451 VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS THR
SEQRES 11 C 451 GLY LEU GLN GLY PHE LEU VAL PHE HIS SER PHE GLY GLY
SEQRES 12 C 451 GLY THR GLY SER GLY PHE THR SER LEU LEU MET GLU ARG
SEQRES 13 C 451 LEU SER VAL ASP TYR GLY LYS LYS SER LYS LEU GLU PHE
SEQRES 14 C 451 SER ILE TYR PRO ALA PRO GLN VAL SER THR ALA VAL VAL
SEQRES 15 C 451 GLU PRO TYR ASN SER ILE LEU THR THR HIS THR THR LEU
SEQRES 16 C 451 GLU HIS SER ASP CYS ALA PHE MET VAL ASP ASN GLU ALA
SEQRES 17 C 451 ILE TYR ASP ILE CYS ARG ARG ASN LEU ASP ILE GLU ARG
SEQRES 18 C 451 PRO THR TYR THR ASN LEU ASN ARG LEU ILE GLY GLN ILE
SEQRES 19 C 451 VAL SER SER ILE THR ALA SER LEU ARG PHE ASP GLY ALA
SEQRES 20 C 451 LEU ASN VAL ASP LEU THR GLU PHE GLN THR ASN LEU VAL
SEQRES 21 C 451 PRO TYR PRO ARG ILE HIS PHE PRO LEU ALA THR TYR ALA
SEQRES 22 C 451 PRO VAL ILE SER ALA GLU LYS ALA TYR HIS GLU GLN LEU
SEQRES 23 C 451 SER VAL ALA GLU ILE THR ASN ALA CYS PHE GLU PRO ALA
SEQRES 24 C 451 ASN GLN MET VAL LYS CYS ASP PRO ARG HIS GLY LYS TYR
SEQRES 25 C 451 MET ALA CYS CYS LEU LEU TYR ARG GLY ASP VAL VAL PRO
SEQRES 26 C 451 LYS ASP VAL ASN ALA ALA ILE ALA THR ILE LYS THR LYS
SEQRES 27 C 451 ARG THR ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE
SEQRES 28 C 451 LYS VAL GLY ILE ASN TYR GLN PRO PRO THR VAL VAL PRO
SEQRES 29 C 451 GLY GLY ASP LEU ALA LYS VAL GLN ARG ALA VAL CYS MET
SEQRES 30 C 451 LEU SER ASN THR THR ALA ILE ALA GLU ALA TRP ALA ARG
SEQRES 31 C 451 LEU ASP HIS LYS PHE ASP LEU MET TYR ALA LYS ARG ALA
SEQRES 32 C 451 PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU GLY
SEQRES 33 C 451 GLU PHE SER GLU ALA ARG GLU ASP MET ALA ALA LEU GLU
SEQRES 34 C 451 LYS ASP TYR GLU GLU VAL GLY VAL ASP SER VAL GLU GLY
SEQRES 35 C 451 GLU GLY GLU GLU GLU GLY GLU GLU TYR
SEQRES 1 D 445 MET ARG GLU ILE VAL HIS ILE GLN ALA GLY GLN CYS GLY
SEQRES 2 D 445 ASN GLN ILE GLY ALA LYS PHE TRP GLU VAL ILE SER ASP
SEQRES 3 D 445 GLU HIS GLY ILE ASP PRO THR GLY SER TYR HIS GLY ASP
SEQRES 4 D 445 SER ASP LEU GLN LEU GLU ARG ILE ASN VAL TYR TYR ASN
SEQRES 5 D 445 GLU ALA THR GLY ASN LYS TYR VAL PRO ARG ALA ILE LEU
SEQRES 6 D 445 VAL ASP LEU GLU PRO GLY THR MET ASP SER VAL ARG SER
SEQRES 7 D 445 GLY PRO PHE GLY GLN ILE PHE ARG PRO ASP ASN PHE VAL
SEQRES 8 D 445 PHE GLY GLN SER GLY ALA GLY ASN ASN TRP ALA LYS GLY
SEQRES 9 D 445 HIS TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL LEU
SEQRES 10 D 445 ASP VAL VAL ARG LYS GLU SER GLU SER CYS ASP CYS LEU
SEQRES 11 D 445 GLN GLY PHE GLN LEU THR HIS SER LEU GLY GLY GLY THR
SEQRES 12 D 445 GLY SER GLY MET GLY THR LEU LEU ILE SER LYS ILE ARG
SEQRES 13 D 445 GLU GLU TYR PRO ASP ARG ILE MET ASN THR PHE SER VAL
SEQRES 14 D 445 MET PRO SER PRO LYS VAL SER ASP THR VAL VAL GLU PRO
SEQRES 15 D 445 TYR ASN ALA THR LEU SER VAL HIS GLN LEU VAL GLU ASN
SEQRES 16 D 445 THR ASP GLU THR TYR SER ILE ASP ASN GLU ALA LEU TYR
SEQRES 17 D 445 ASP ILE CYS PHE ARG THR LEU LYS LEU THR THR PRO THR
SEQRES 18 D 445 TYR GLY ASP LEU ASN HIS LEU VAL SER ALA THR MET SER
SEQRES 19 D 445 GLY VAL THR THR CYS LEU ARG PHE PRO GLY GLN LEU ASN
SEQRES 20 D 445 ALA ASP LEU ARG LYS LEU ALA VAL ASN MET VAL PRO PHE
SEQRES 21 D 445 PRO ARG LEU HIS PHE PHE MET PRO GLY PHE ALA PRO LEU
SEQRES 22 D 445 THR SER ARG GLY SER GLN GLN TYR ARG ALA LEU THR VAL
SEQRES 23 D 445 PRO GLU LEU THR GLN GLN MET PHE ASP SER LYS ASN MET
SEQRES 24 D 445 MET ALA ALA CYS ASP PRO ARG HIS GLY ARG TYR LEU THR
SEQRES 25 D 445 VAL ALA ALA VAL PHE ARG GLY ARG MET SER MET LYS GLU
SEQRES 26 D 445 VAL ASP GLU GLN MET LEU ASN VAL GLN ASN LYS ASN SER
SEQRES 27 D 445 SER TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL LYS THR
SEQRES 28 D 445 ALA VAL CYS ASP ILE PRO PRO ARG GLY LEU LYS MET SER
SEQRES 29 D 445 ALA THR PHE ILE GLY ASN SER THR ALA ILE GLN GLU LEU
SEQRES 30 D 445 PHE LYS ARG ILE SER GLU GLN PHE THR ALA MET PHE ARG
SEQRES 31 D 445 ARG LYS ALA PHE LEU HIS TRP TYR THR GLY GLU GLY MET
SEQRES 32 D 445 ASP GLU MET GLU PHE THR GLU ALA GLU SER ASN MET ASN
SEQRES 33 D 445 ASP LEU VAL SER GLU TYR GLN GLN TYR GLN ASP ALA THR
SEQRES 34 D 445 ALA ASP GLU GLN GLY GLU PHE GLU GLU GLU GLU GLY GLU
SEQRES 35 D 445 ASP GLU ALA
SEQRES 1 E 142 ALA ASP MET GLU VAL ILE GLU LEU ASN LYS CYS THR SER
SEQRES 2 E 142 GLY GLN SER PHE GLU VAL ILE LEU LYS PRO PRO SER PHE
SEQRES 3 E 142 ASP GLY VAL PRO GLU PHE ASN ALA SER LEU PRO ARG ARG
SEQRES 4 E 142 ARG ASP PRO SER LEU GLU GLU ILE GLN LYS LYS LEU GLU
SEQRES 5 E 142 ALA ALA GLU GLU ARG ARG LYS TYR GLN GLU ALA GLU LEU
SEQRES 6 E 142 LEU LYS HIS LEU ALA GLU LYS ARG GLU HIS GLU ARG GLU
SEQRES 7 E 142 VAL ILE GLN LYS ALA ILE GLU GLU ASN ASN ASN PHE ILE
SEQRES 8 E 142 LYS MET ALA LYS GLU LYS LEU ALA GLN LYS MET GLU SER
SEQRES 9 E 142 ASN LYS GLU ASN ARG GLU ALA HIS LEU ALA ALA MET LEU
SEQRES 10 E 142 GLU ARG LEU GLN GLU LYS ASP LYS HIS ALA GLU GLU VAL
SEQRES 11 E 142 ARG LYS ASN LYS GLU LEU LYS GLU GLU ALA SER ARG
HET GTP A 600 32
HET MG A 601 1
HET GDP B 600 28
HET MG B 601 1
HET E70 B 700 26
HET GTP C 600 32
HET MG C 601 1
HET GDP D 600 28
HET E70 D 700 26
HETNAM GTP GUANOSINE-5'-TRIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM E70 N-{2-[(4-HYDROXYPHENYL)AMINO]PYRIDIN-3-YL}-4-
HETNAM 2 E70 METHOXYBENZENESULFONAMIDE
FORMUL 6 GTP 2(C10 H16 N5 O14 P3)
FORMUL 7 MG 3(MG 2+)
FORMUL 8 GDP 2(C10 H15 N5 O11 P2)
FORMUL 10 E70 2(C18 H17 N3 O4 S)
HELIX 1 1 GLY A 10 HIS A 28 1 19
HELIX 2 2 PRO A 72 ARG A 79 1 8
HELIX 3 3 HIS A 88 GLU A 90 5 3
HELIX 4 4 ASN A 102 TYR A 108 1 7
HELIX 5 5 ILE A 110 GLN A 128 1 19
HELIX 6 6 GLY A 143 TYR A 161 1 19
HELIX 7 7 VAL A 182 LEU A 195 1 14
HELIX 8 8 ASN A 206 ASN A 216 1 11
HELIX 9 9 THR A 223 ASP A 245 1 23
HELIX 10 10 LEU A 252 ASN A 258 1 7
HELIX 11 11 SER A 287 PHE A 296 1 10
HELIX 12 12 VAL A 324 LYS A 338 1 15
HELIX 13 13 ILE A 384 ALA A 400 1 17
HELIX 14 14 VAL A 405 GLY A 412 1 8
HELIX 15 15 GLU A 414 GLU A 434 1 21
HELIX 16 16 GLY B 10 GLY B 29 1 20
HELIX 17 17 ASP B 41 ARG B 48 5 6
HELIX 18 18 PRO B 72 SER B 80 1 9
HELIX 19 19 PHE B 83 PHE B 87 5 5
HELIX 20 20 ARG B 88 ASP B 90 5 3
HELIX 21 21 ASN B 102 TYR B 108 1 7
HELIX 22 22 TYR B 108 GLU B 127 1 20
HELIX 23 23 GLY B 143 TYR B 161 1 19
HELIX 24 24 VAL B 182 THR B 198 1 17
HELIX 25 25 ASP B 205 ARG B 215 1 11
HELIX 26 26 LEU B 227 THR B 240 1 14
HELIX 27 27 CYS B 241 ARG B 243 5 3
HELIX 28 28 LEU B 252 VAL B 260 1 9
HELIX 29 29 PHE B 262 LEU B 265 5 4
HELIX 30 30 VAL B 288 PHE B 296 1 9
HELIX 31 31 ASP B 297 MET B 301 5 5
HELIX 32 32 MET B 325 GLN B 336 1 12
HELIX 33 33 ASN B 339 PHE B 343 5 5
HELIX 34 34 ILE B 384 THR B 396 1 13
HELIX 35 35 LEU B 405 GLY B 410 1 6
HELIX 36 36 ASP B 414 GLN B 433 1 20
HELIX 37 37 GLY C 10 GLY C 29 1 20
HELIX 38 38 SER C 48 PHE C 52 5 5
HELIX 39 39 PRO C 72 ARG C 79 1 8
HELIX 40 40 HIS C 88 GLU C 90 5 3
HELIX 41 41 ASN C 102 TYR C 108 1 7
HELIX 42 42 ILE C 110 GLN C 128 1 19
HELIX 43 43 GLY C 143 TYR C 161 1 19
HELIX 44 44 VAL C 182 LEU C 195 1 14
HELIX 45 45 ASN C 206 ASN C 216 1 11
HELIX 46 46 THR C 223 ALA C 240 1 18
HELIX 47 47 ALA C 240 ASP C 245 1 6
HELIX 48 48 ASP C 251 THR C 257 1 7
HELIX 49 49 SER C 287 ASN C 293 1 7
HELIX 50 50 VAL C 324 LYS C 338 1 15
HELIX 51 51 ILE C 384 ALA C 400 1 17
HELIX 52 52 VAL C 405 GLY C 412 1 8
HELIX 53 53 GLU C 414 GLU C 434 1 21
HELIX 54 54 GLY D 10 GLY D 29 1 20
HELIX 55 55 ASP D 41 GLU D 47 5 5
HELIX 56 56 ARG D 48 TYR D 53 1 6
HELIX 57 57 MET D 75 SER D 80 1 6
HELIX 58 58 PHE D 83 PHE D 87 5 5
HELIX 59 59 ARG D 88 ASP D 90 5 3
HELIX 60 60 ASN D 102 TYR D 108 1 7
HELIX 61 61 GLY D 111 GLU D 127 1 17
HELIX 62 62 GLY D 143 TYR D 161 1 19
HELIX 63 63 VAL D 182 THR D 198 1 17
HELIX 64 64 ASP D 205 ARG D 215 1 11
HELIX 65 65 LEU D 227 THR D 240 1 14
HELIX 66 66 CYS D 241 ARG D 243 5 3
HELIX 67 67 LEU D 252 VAL D 260 1 9
HELIX 68 68 PHE D 262 LEU D 265 5 4
HELIX 69 69 VAL D 288 PHE D 296 1 9
HELIX 70 70 ASP D 297 MET D 301 5 5
HELIX 71 71 SER D 324 GLN D 336 1 13
HELIX 72 72 ASN D 339 PHE D 343 5 5
HELIX 73 73 ILE D 384 THR D 396 1 13
HELIX 74 74 LEU D 405 GLY D 410 1 6
HELIX 75 75 ASP D 414 GLN D 433 1 20
HELIX 76 76 HIS E 78 GLU E 88 1 11
HELIX 77 77 GLU E 89 LYS E 98 1 10
HELIX 78 78 ASN E 108 GLU E 121 1 14
HELIX 79 79 HIS E 129 LYS E 135 1 7
SHEET 1 A 6 LEU A 92 THR A 94 0
SHEET 2 A 6 ALA A 65 ASP A 69 1 N PHE A 67 O ILE A 93
SHEET 3 A 6 ILE A 5 VAL A 9 1 N HIS A 8 O VAL A 66
SHEET 4 A 6 PHE A 135 SER A 140 1 O PHE A 138 N ILE A 7
SHEET 5 A 6 LYS A 166 TYR A 172 1 O LEU A 167 N PHE A 135
SHEET 6 A 6 CYS A 200 ASP A 205 1 O PHE A 202 N GLU A 168
SHEET 1 B 3 ARG A 373 ALA A 374 0
SHEET 2 B 3 TYR A 312 GLY A 321 -1 N ARG A 320 O ALA A 374
SHEET 3 B 3 LEU A 378 THR A 381 -1 O LEU A 378 N CYS A 316
SHEET 1 C 5 ARG A 373 ALA A 374 0
SHEET 2 C 5 TYR A 312 GLY A 321 -1 N ARG A 320 O ALA A 374
SHEET 3 C 5 LYS A 352 ASN A 356 1 O ASN A 356 N GLY A 321
SHEET 4 C 5 GLY E 17 GLU E 21 -1 O GLN E 18 N ILE A 355
SHEET 5 C 5 LYS E 13 CYS E 14 -1 N CYS E 14 O GLY E 17
SHEET 1 D10 PHE B 92 VAL B 93 0
SHEET 2 D10 ILE B 66 VAL B 68 1 N LEU B 67 O VAL B 93
SHEET 3 D10 ILE B 4 ALA B 9 1 N HIS B 6 O ILE B 66
SHEET 4 D10 GLY B 134 SER B 140 1 O GLN B 136 N ILE B 7
SHEET 5 D10 ILE B 165 VAL B 171 1 O ASN B 167 N PHE B 135
SHEET 6 D10 GLU B 200 SER B 203 1 O TYR B 202 N THR B 168
SHEET 7 D10 PHE B 267 PHE B 272 1 O PHE B 268 N SER B 203
SHEET 8 D10 SER B 374 SER B 381 -1 O GLY B 379 N MET B 269
SHEET 9 D10 TYR B 312 ARG B 320 -1 N ALA B 316 O ILE B 378
SHEET 10 D10 VAL B 351 CYS B 356 1 O CYS B 356 N PHE B 319
SHEET 1 E 6 LEU C 92 THR C 94 0
SHEET 2 E 6 ALA C 65 ASP C 69 1 N PHE C 67 O ILE C 93
SHEET 3 E 6 GLU C 3 VAL C 9 1 N HIS C 8 O VAL C 68
SHEET 4 E 6 LEU C 132 SER C 140 1 O PHE C 138 N ILE C 7
SHEET 5 E 6 LYS C 166 TYR C 172 1 O LEU C 167 N PHE C 135
SHEET 6 E 6 CYS C 200 ASP C 205 1 O PHE C 202 N GLU C 168
SHEET 1 F 3 LYS C 352 ASN C 356 0
SHEET 2 F 3 TYR C 312 GLY C 321 1 N GLY C 321 O ASN C 356
SHEET 3 F 3 ARG C 373 ALA C 374 -1 O ALA C 374 N ARG C 320
SHEET 1 G 3 LYS C 352 ASN C 356 0
SHEET 2 G 3 TYR C 312 GLY C 321 1 N GLY C 321 O ASN C 356
SHEET 3 G 3 LEU C 378 THR C 381 -1 O ASN C 380 N ALA C 314
SHEET 1 H10 PHE D 92 VAL D 93 0
SHEET 2 H10 ILE D 66 VAL D 68 1 N LEU D 67 O VAL D 93
SHEET 3 H10 ILE D 4 ALA D 9 1 N HIS D 6 O ILE D 66
SHEET 4 H10 GLY D 134 SER D 140 1 O GLN D 136 N ILE D 7
SHEET 5 H10 ILE D 165 VAL D 171 1 O ASN D 167 N PHE D 135
SHEET 6 H10 GLU D 200 SER D 203 1 O TYR D 202 N THR D 168
SHEET 7 H10 PHE D 267 PHE D 272 1 O PHE D 268 N SER D 203
SHEET 8 H10 SER D 374 SER D 381 -1 O PHE D 377 N GLY D 271
SHEET 9 H10 TYR D 312 ARG D 320 -1 N VAL D 318 O THR D 376
SHEET 10 H10 VAL D 351 CYS D 356 1 O CYS D 356 N PHE D 319
SITE 1 AC1 23 GLY A 10 GLN A 11 ALA A 12 ILE A 16
SITE 2 AC1 23 ASP A 69 GLU A 71 ASP A 98 SER A 140
SITE 3 AC1 23 GLY A 142 GLY A 143 GLY A 144 THR A 145
SITE 4 AC1 23 GLY A 146 PRO A 173 VAL A 177 SER A 178
SITE 5 AC1 23 THR A 179 GLU A 183 ASN A 206 TYR A 224
SITE 6 AC1 23 ASN A 228 MG A 601 LYS B 254
SITE 1 AC2 5 ALA A 99 ASN A 101 GLY A 144 THR A 145
SITE 2 AC2 5 GTP A 600
SITE 1 AC3 15 GLY B 10 GLN B 11 CYS B 12 ILE B 16
SITE 2 AC3 15 SER B 140 GLY B 142 GLY B 144 THR B 145
SITE 3 AC3 15 GLY B 146 VAL B 177 GLU B 183 ASN B 206
SITE 4 AC3 15 TYR B 224 ASN B 228 MG B 601
SITE 1 AC4 3 ASN B 101 GDP B 600 GLU C 254
SITE 1 AC5 14 THR A 179 VAL A 181 TYR B 202 VAL B 238
SITE 2 AC5 14 CYS B 241 LEU B 242 LEU B 248 ALA B 250
SITE 3 AC5 14 LYS B 254 LEU B 255 ASN B 258 VAL B 315
SITE 4 AC5 14 LYS B 352 ILE B 378
SITE 1 AC6 24 GLY C 10 GLN C 11 ALA C 12 ILE C 16
SITE 2 AC6 24 ASP C 69 GLU C 71 ASP C 98 ALA C 99
SITE 3 AC6 24 SER C 140 GLY C 142 GLY C 143 GLY C 144
SITE 4 AC6 24 THR C 145 GLY C 146 PRO C 173 VAL C 177
SITE 5 AC6 24 SER C 178 GLU C 183 ASN C 206 TYR C 224
SITE 6 AC6 24 ASN C 228 ILE C 231 MG C 601 LYS D 254
SITE 1 AC7 5 ALA C 99 ASN C 101 GLY C 144 THR C 145
SITE 2 AC7 5 GTP C 600
SITE 1 AC8 15 GLY D 10 GLN D 11 CYS D 12 ILE D 16
SITE 2 AC8 15 SER D 140 GLY D 142 GLY D 144 THR D 145
SITE 3 AC8 15 GLY D 146 VAL D 177 SER D 178 GLU D 183
SITE 4 AC8 15 ASN D 206 TYR D 224 ASN D 228
SITE 1 AC9 14 THR C 179 VAL C 181 TYR D 202 VAL D 238
SITE 2 AC9 14 LEU D 242 LEU D 248 ALA D 250 LYS D 254
SITE 3 AC9 14 LEU D 255 ASN D 258 VAL D 315 ALA D 316
SITE 4 AC9 14 LYS D 352 ILE D 378
CRYST1 329.240 329.240 53.870 90.00 90.00 120.00 P 65 12
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 0.003037 0.001754 0.000000 0.00000
SCALE2 0.000000 0.003507 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018563 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
