HEADER CELL CYCLE/SIGNALING PROTEIN 12-SEP-11 3VHX
TITLE THE CRYSTAL STRUCTURE OF ARF6-MKLP1 (MITOTIC KINESIN-LIKE PROTEIN 1)
TITLE 2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADP-RIBOSYLATION FACTOR 6;
COMPND 3 CHAIN: A, C, E, G;
COMPND 4 FRAGMENT: UNP RESIDUES 13-175;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: KINESIN-LIKE PROTEIN KIF23;
COMPND 9 CHAIN: B, D, F, H;
COMPND 10 FRAGMENT: UNP RESIDUES 794-911;
COMPND 11 SYNONYM: KINESIN-LIKE PROTEIN 5, MITOTIC KINESIN-LIKE PROTEIN 1;
COMPND 12 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: ARF6;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: KIF23, KNSL5, MKLP1;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SMALL GTPASE, GTP BINDING, FLEMMING BODY, CYTOKINESIS, CELL CYCLE-
KEYWDS 2 SIGNALING PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.MAKYIO,T.TAKEI,H.OHGI,S.TAKAHASHI,H.TAKATSU,T.UEDA,Y.KANAHO,Y.XIE,
AUTHOR 2 H.W.SHIN,H.KAMIKUBO,M.KATAOKA,M.KAWASAKI,R.KATO,S.WAKATSUKI,
AUTHOR 3 K.NAKAYAMA
REVDAT 3 08-NOV-23 3VHX 1 REMARK SEQADV LINK
REVDAT 2 19-JUN-13 3VHX 1 JRNL
REVDAT 1 16-MAY-12 3VHX 0
JRNL AUTH H.MAKYIO,M.OHGI,T.TAKEI,S.TAKAHASHI,H.TAKATSU,Y.KATOH,
JRNL AUTH 2 A.HANAI,T.UEDA,Y.KANAHO,Y.XIE,H.W.SHIN,H.KAMIKUBO,M.KATAOKA,
JRNL AUTH 3 M.KAWASAKI,R.KATO,S.WAKATSUKI,K.NAKAYAMA
JRNL TITL STRUCTURAL BASIS FOR ARF6-MKLP1 COMPLEX FORMATION ON THE
JRNL TITL 2 FLEMMING BODY RESPONSIBLE FOR CYTOKINESIS
JRNL REF EMBO J. V. 31 2590 2012
JRNL REFN ISSN 0261-4189
JRNL PMID 22522702
JRNL DOI 10.1038/EMBOJ.2012.89
REMARK 2
REMARK 2 RESOLUTION. 2.81 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
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) : 2.81
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 28749
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) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.232
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1461
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) : 2.81
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.88
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1855
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.22
REMARK 3 BIN R VALUE (WORKING SET) : 0.3110
REMARK 3 BIN FREE R VALUE SET COUNT : 99
REMARK 3 BIN FREE R VALUE : 0.3060
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 8416
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 138
REMARK 3 SOLVENT ATOMS : 105
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.51000
REMARK 3 B22 (A**2) : -1.47000
REMARK 3 B33 (A**2) : 1.34000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -2.09000
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): 0.370
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.285
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 32.573
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 8541 ; 0.007 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 11584 ; 1.061 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1017 ; 5.394 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 399 ;36.153 ;24.185
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1533 ;13.126 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 63 ;15.056 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1289 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 6323 ; 0.003 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 5099 ; 0.285 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8273 ; 0.558 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3442 ; 0.792 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 3311 ; 1.380 ; 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 : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 12 A 173
REMARK 3 RESIDUE RANGE : A 184 A 185
REMARK 3 RESIDUE RANGE : A 186 A 193
REMARK 3 ORIGIN FOR THE GROUP (A): -15.9070 -26.0405 -6.6730
REMARK 3 T TENSOR
REMARK 3 T11: 0.3755 T22: 0.1157
REMARK 3 T33: 0.2476 T12: -0.0283
REMARK 3 T13: -0.0203 T23: -0.0438
REMARK 3 L TENSOR
REMARK 3 L11: 3.9801 L22: 5.7288
REMARK 3 L33: 4.0166 L12: -1.4730
REMARK 3 L13: 0.5354 L23: 1.0355
REMARK 3 S TENSOR
REMARK 3 S11: 0.0144 S12: -0.0317 S13: -0.1714
REMARK 3 S21: 0.3410 S22: 0.1607 S23: -0.2817
REMARK 3 S31: 0.4589 S32: 0.0528 S33: -0.1751
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 695 B 800
REMARK 3 RESIDUE RANGE : B 808 B 814
REMARK 3 ORIGIN FOR THE GROUP (A): -21.2260 -5.3758 2.4201
REMARK 3 T TENSOR
REMARK 3 T11: 0.2211 T22: 0.1678
REMARK 3 T33: 0.3620 T12: 0.0153
REMARK 3 T13: 0.0462 T23: -0.0168
REMARK 3 L TENSOR
REMARK 3 L11: 3.9347 L22: 7.6363
REMARK 3 L33: 7.7445 L12: 3.1423
REMARK 3 L13: 3.4358 L23: 5.0487
REMARK 3 S TENSOR
REMARK 3 S11: 0.1872 S12: -0.0912 S13: -0.0217
REMARK 3 S21: -0.0477 S22: -0.0049 S23: -0.2468
REMARK 3 S31: -0.0650 S32: -0.0751 S33: -0.1823
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 12 C 173
REMARK 3 RESIDUE RANGE : C 184 C 185
REMARK 3 RESIDUE RANGE : C 186 C 213
REMARK 3 ORIGIN FOR THE GROUP (A): 7.294 30.793 18.428
REMARK 3 T TENSOR
REMARK 3 T11: 0.0480 T22: 0.1196
REMARK 3 T33: 0.0307 T12: 0.0029
REMARK 3 T13: 0.0167 T23: 0.0287
REMARK 3 L TENSOR
REMARK 3 L11: 6.2509 L22: 4.1649
REMARK 3 L33: 2.9917 L12: -1.3878
REMARK 3 L13: 0.2271 L23: 0.3117
REMARK 3 S TENSOR
REMARK 3 S11: -0.0600 S12: -0.1405 S13: 0.2810
REMARK 3 S21: 0.2876 S22: 0.1625 S23: 0.0890
REMARK 3 S31: -0.2545 S32: -0.0558 S33: -0.1025
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 695 D 800
REMARK 3 RESIDUE RANGE : D 808 D 819
REMARK 3 ORIGIN FOR THE GROUP (A): -9.652 14.601 19.921
REMARK 3 T TENSOR
REMARK 3 T11: 0.0790 T22: 0.1778
REMARK 3 T33: 0.2406 T12: 0.0240
REMARK 3 T13: 0.0106 T23: -0.0034
REMARK 3 L TENSOR
REMARK 3 L11: 4.5665 L22: 7.2104
REMARK 3 L33: 9.1100 L12: -3.1438
REMARK 3 L13: 4.6375 L23: -4.5358
REMARK 3 S TENSOR
REMARK 3 S11: 0.1807 S12: 0.1078 S13: -0.6585
REMARK 3 S21: 0.1824 S22: 0.0200 S23: -0.0776
REMARK 3 S31: 0.2706 S32: -0.0189 S33: -0.2007
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 12 E 173
REMARK 3 RESIDUE RANGE : E 184 E 185
REMARK 3 RESIDUE RANGE : E 186 E 207
REMARK 3 ORIGIN FOR THE GROUP (A): -21.8023 -54.7038 -55.6046
REMARK 3 T TENSOR
REMARK 3 T11: 0.1022 T22: 0.2199
REMARK 3 T33: 0.1522 T12: 0.0074
REMARK 3 T13: 0.0239 T23: 0.1246
REMARK 3 L TENSOR
REMARK 3 L11: 5.5892 L22: 3.6167
REMARK 3 L33: 3.6113 L12: -0.5145
REMARK 3 L13: 0.4979 L23: -0.0811
REMARK 3 S TENSOR
REMARK 3 S11: -0.0144 S12: -0.0543 S13: 0.4029
REMARK 3 S21: 0.2375 S22: 0.2063 S23: 0.4284
REMARK 3 S31: -0.2037 S32: -0.2717 S33: -0.1918
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 699 F 800
REMARK 3 RESIDUE RANGE : F 808 F 824
REMARK 3 ORIGIN FOR THE GROUP (A): -3.8840 -71.0509 -55.5683
REMARK 3 T TENSOR
REMARK 3 T11: 0.0497 T22: 0.2265
REMARK 3 T33: 0.0684 T12: -0.0551
REMARK 3 T13: -0.0004 T23: 0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 3.3559 L22: 6.6733
REMARK 3 L33: 5.5284 L12: -2.5912
REMARK 3 L13: 1.6508 L23: -2.1309
REMARK 3 S TENSOR
REMARK 3 S11: 0.1687 S12: 0.2733 S13: -0.0784
REMARK 3 S21: -0.2738 S22: -0.1247 S23: -0.1157
REMARK 3 S31: 0.3044 S32: 0.2583 S33: -0.0440
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 12 G 173
REMARK 3 RESIDUE RANGE : G 184 G 185
REMARK 3 RESIDUE RANGE : G 186 G 188
REMARK 3 ORIGIN FOR THE GROUP (A): -1.882 -113.089 -32.909
REMARK 3 T TENSOR
REMARK 3 T11: 0.4453 T22: 0.2100
REMARK 3 T33: 0.6862 T12: 0.0284
REMARK 3 T13: -0.1011 T23: -0.1934
REMARK 3 L TENSOR
REMARK 3 L11: 4.8226 L22: 6.5855
REMARK 3 L33: 5.6065 L12: -1.8712
REMARK 3 L13: 0.4838 L23: 1.2893
REMARK 3 S TENSOR
REMARK 3 S11: -0.0207 S12: 0.2306 S13: -0.8206
REMARK 3 S21: -0.3120 S22: -0.4056 S23: 0.3816
REMARK 3 S31: 0.4191 S32: -0.0946 S33: 0.4263
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 713 H 800
REMARK 3 RESIDUE RANGE : H 808 H 815
REMARK 3 ORIGIN FOR THE GROUP (A): 4.597 -92.077 -44.881
REMARK 3 T TENSOR
REMARK 3 T11: 0.2232 T22: 0.2139
REMARK 3 T33: 0.3020 T12: -0.0062
REMARK 3 T13: -0.0325 T23: -0.0429
REMARK 3 L TENSOR
REMARK 3 L11: 4.2822 L22: 7.7555
REMARK 3 L33: 5.9024 L12: 0.4829
REMARK 3 L13: 1.1935 L23: 2.7794
REMARK 3 S TENSOR
REMARK 3 S11: 0.1679 S12: 0.0041 S13: -0.5739
REMARK 3 S21: -0.0815 S22: -0.3030 S23: 0.5489
REMARK 3 S31: 0.0572 S32: -0.4934 S33: 0.1351
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES: WITH TLS ADDED
REMARK 4
REMARK 4 3VHX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-SEP-11.
REMARK 100 THE DEPOSITION ID IS D_1000095065.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JAN-10
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : PHOTON FACTORY
REMARK 200 BEAMLINE : AR-NW12A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28794
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.809
REMARK 200 RESOLUTION RANGE LOW (A) : 87.286
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.700
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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 2J5X
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.62
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 4000, 0.05M AMMONIUM SULFATE,
REMARK 280 0.005M MAGNESIUM CHLORIDE, 0.1M SODIUM CACODYLATE, 0.25-1.0% V/V
REMARK 280 ETHYL ACETATE , PH 6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 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 87.28650
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24470 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8320 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23370 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H
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 LYS A 174
REMARK 465 SER A 175
REMARK 465 LEU A 176
REMARK 465 GLU A 177
REMARK 465 HIS A 178
REMARK 465 HIS A 179
REMARK 465 HIS A 180
REMARK 465 HIS A 181
REMARK 465 HIS A 182
REMARK 465 HIS A 183
REMARK 465 GLY B 688
REMARK 465 SER B 689
REMARK 465 LEU B 690
REMARK 465 LEU B 691
REMARK 465 PHE B 692
REMARK 465 GLN B 693
REMARK 465 PRO B 694
REMARK 465 GLY B 801
REMARK 465 SER B 802
REMARK 465 ARG B 803
REMARK 465 LYS B 804
REMARK 465 ARG B 805
REMARK 465 ARG B 806
REMARK 465 SER B 807
REMARK 465 LYS C 174
REMARK 465 SER C 175
REMARK 465 LEU C 176
REMARK 465 GLU C 177
REMARK 465 HIS C 178
REMARK 465 HIS C 179
REMARK 465 HIS C 180
REMARK 465 HIS C 181
REMARK 465 HIS C 182
REMARK 465 HIS C 183
REMARK 465 GLY D 688
REMARK 465 SER D 689
REMARK 465 LEU D 690
REMARK 465 LEU D 691
REMARK 465 PHE D 692
REMARK 465 GLN D 693
REMARK 465 PRO D 694
REMARK 465 GLY D 801
REMARK 465 SER D 802
REMARK 465 ARG D 803
REMARK 465 LYS D 804
REMARK 465 ARG D 805
REMARK 465 ARG D 806
REMARK 465 SER D 807
REMARK 465 LYS E 174
REMARK 465 SER E 175
REMARK 465 LEU E 176
REMARK 465 GLU E 177
REMARK 465 HIS E 178
REMARK 465 HIS E 179
REMARK 465 HIS E 180
REMARK 465 HIS E 181
REMARK 465 HIS E 182
REMARK 465 HIS E 183
REMARK 465 GLY F 688
REMARK 465 SER F 689
REMARK 465 LEU F 690
REMARK 465 LEU F 691
REMARK 465 PHE F 692
REMARK 465 GLN F 693
REMARK 465 PRO F 694
REMARK 465 ASP F 695
REMARK 465 GLN F 696
REMARK 465 ASN F 697
REMARK 465 ALA F 698
REMARK 465 GLY F 801
REMARK 465 SER F 802
REMARK 465 ARG F 803
REMARK 465 LYS F 804
REMARK 465 ARG F 805
REMARK 465 ARG F 806
REMARK 465 SER F 807
REMARK 465 LYS G 174
REMARK 465 SER G 175
REMARK 465 LEU G 176
REMARK 465 GLU G 177
REMARK 465 HIS G 178
REMARK 465 HIS G 179
REMARK 465 HIS G 180
REMARK 465 HIS G 181
REMARK 465 HIS G 182
REMARK 465 HIS G 183
REMARK 465 GLY H 688
REMARK 465 SER H 689
REMARK 465 LEU H 690
REMARK 465 LEU H 691
REMARK 465 PHE H 692
REMARK 465 GLN H 693
REMARK 465 PRO H 694
REMARK 465 ASP H 695
REMARK 465 GLN H 696
REMARK 465 ASN H 697
REMARK 465 ALA H 698
REMARK 465 PRO H 699
REMARK 465 PRO H 700
REMARK 465 ILE H 701
REMARK 465 ARG H 702
REMARK 465 LEU H 703
REMARK 465 ARG H 704
REMARK 465 HIS H 705
REMARK 465 ARG H 706
REMARK 465 ARG H 707
REMARK 465 SER H 708
REMARK 465 ARG H 709
REMARK 465 SER H 710
REMARK 465 ALA H 711
REMARK 465 GLY H 712
REMARK 465 GLY H 801
REMARK 465 SER H 802
REMARK 465 ARG H 803
REMARK 465 LYS H 804
REMARK 465 ARG H 805
REMARK 465 ARG H 806
REMARK 465 SER H 807
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 ARG B 707
REMARK 475 SER B 708
REMARK 475 ARG B 709
REMARK 475 SER B 710
REMARK 475 ALA B 711
REMARK 475 GLY B 712
REMARK 475 ARG D 707
REMARK 475 SER D 708
REMARK 475 ARG D 709
REMARK 475 SER D 710
REMARK 475 ALA D 711
REMARK 475 GLY D 712
REMARK 475 LEU F 703
REMARK 475 ARG F 704
REMARK 475 HIS F 705
REMARK 475 ARG F 706
REMARK 475 ARG F 707
REMARK 475 SER F 708
REMARK 475 ARG F 709
REMARK 475 SER F 710
REMARK 475 ALA F 711
REMARK 475 GLY F 712
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 NE2 HIS F 733 NE2 HIS H 733 1.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE1 GLU D 727 CB HIS F 705 2454 1.98
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 PRO A 72 -8.90 -59.93
REMARK 500 HIS B 705 -70.03 -45.33
REMARK 500 HIS B 736 47.77 38.85
REMARK 500 GLU B 797 148.33 -175.53
REMARK 500 PRO B 799 42.49 -68.47
REMARK 500 HIS C 76 0.17 -67.75
REMARK 500 ASN D 697 35.00 -88.42
REMARK 500 HIS D 705 -75.39 -51.17
REMARK 500 GLU D 727 54.63 -96.21
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 185 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 27 OG1
REMARK 620 2 THR A 44 OG1 92.4
REMARK 620 3 GTP A 184 O1B 96.0 164.1
REMARK 620 4 GTP A 184 O1G 166.7 86.9 81.9
REMARK 620 5 HOH A 193 O 98.1 85.1 80.3 68.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 185 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 27 OG1
REMARK 620 2 THR C 44 OG1 88.6
REMARK 620 3 GTP C 184 O1G 161.6 94.4
REMARK 620 4 GTP C 184 O1B 87.3 162.5 84.4
REMARK 620 5 HOH C 210 O 97.5 107.5 98.9 90.0
REMARK 620 6 HOH C 211 O 80.4 83.9 81.8 78.6 168.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG E 185 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR E 27 OG1
REMARK 620 2 THR E 44 OG1 84.0
REMARK 620 3 GTP E 184 O1G 155.2 90.3
REMARK 620 4 GTP E 184 O1B 84.7 153.6 90.0
REMARK 620 5 HOH E 201 O 72.3 71.6 83.0 82.2
REMARK 620 6 HOH E 204 O 105.9 108.1 98.9 98.0 178.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG G 185 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR G 27 OG1
REMARK 620 2 THR G 44 OG1 87.9
REMARK 620 3 GTP G 184 O1G 159.3 95.0
REMARK 620 4 GTP G 184 O1B 77.8 142.7 87.7
REMARK 620 N 1 2 3
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 184
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 185
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP C 184
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 185
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP E 184
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 185
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP G 184
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 185
DBREF 3VHX A 13 175 UNP P62331 ARF6_MOUSE 13 175
DBREF 3VHX B 690 807 UNP Q02241 KIF23_HUMAN 794 911
DBREF 3VHX C 13 175 UNP P62331 ARF6_MOUSE 13 175
DBREF 3VHX D 690 807 UNP Q02241 KIF23_HUMAN 794 911
DBREF 3VHX E 13 175 UNP P62331 ARF6_MOUSE 13 175
DBREF 3VHX F 690 807 UNP Q02241 KIF23_HUMAN 794 911
DBREF 3VHX G 13 175 UNP P62331 ARF6_MOUSE 13 175
DBREF 3VHX H 690 807 UNP Q02241 KIF23_HUMAN 794 911
SEQADV 3VHX MET A 12 UNP P62331 EXPRESSION TAG
SEQADV 3VHX LEU A 67 UNP P62331 GLN 67 ENGINEERED MUTATION
SEQADV 3VHX LEU A 176 UNP P62331 EXPRESSION TAG
SEQADV 3VHX GLU A 177 UNP P62331 EXPRESSION TAG
SEQADV 3VHX HIS A 178 UNP P62331 EXPRESSION TAG
SEQADV 3VHX HIS A 179 UNP P62331 EXPRESSION TAG
SEQADV 3VHX HIS A 180 UNP P62331 EXPRESSION TAG
SEQADV 3VHX HIS A 181 UNP P62331 EXPRESSION TAG
SEQADV 3VHX HIS A 182 UNP P62331 EXPRESSION TAG
SEQADV 3VHX HIS A 183 UNP P62331 EXPRESSION TAG
SEQADV 3VHX GLY B 688 UNP Q02241 EXPRESSION TAG
SEQADV 3VHX SER B 689 UNP Q02241 EXPRESSION TAG
SEQADV 3VHX MET C 12 UNP P62331 EXPRESSION TAG
SEQADV 3VHX LEU C 67 UNP P62331 GLN 67 ENGINEERED MUTATION
SEQADV 3VHX LEU C 176 UNP P62331 EXPRESSION TAG
SEQADV 3VHX GLU C 177 UNP P62331 EXPRESSION TAG
SEQADV 3VHX HIS C 178 UNP P62331 EXPRESSION TAG
SEQADV 3VHX HIS C 179 UNP P62331 EXPRESSION TAG
SEQADV 3VHX HIS C 180 UNP P62331 EXPRESSION TAG
SEQADV 3VHX HIS C 181 UNP P62331 EXPRESSION TAG
SEQADV 3VHX HIS C 182 UNP P62331 EXPRESSION TAG
SEQADV 3VHX HIS C 183 UNP P62331 EXPRESSION TAG
SEQADV 3VHX GLY D 688 UNP Q02241 EXPRESSION TAG
SEQADV 3VHX SER D 689 UNP Q02241 EXPRESSION TAG
SEQADV 3VHX MET E 12 UNP P62331 EXPRESSION TAG
SEQADV 3VHX LEU E 67 UNP P62331 GLN 67 ENGINEERED MUTATION
SEQADV 3VHX LEU E 176 UNP P62331 EXPRESSION TAG
SEQADV 3VHX GLU E 177 UNP P62331 EXPRESSION TAG
SEQADV 3VHX HIS E 178 UNP P62331 EXPRESSION TAG
SEQADV 3VHX HIS E 179 UNP P62331 EXPRESSION TAG
SEQADV 3VHX HIS E 180 UNP P62331 EXPRESSION TAG
SEQADV 3VHX HIS E 181 UNP P62331 EXPRESSION TAG
SEQADV 3VHX HIS E 182 UNP P62331 EXPRESSION TAG
SEQADV 3VHX HIS E 183 UNP P62331 EXPRESSION TAG
SEQADV 3VHX GLY F 688 UNP Q02241 EXPRESSION TAG
SEQADV 3VHX SER F 689 UNP Q02241 EXPRESSION TAG
SEQADV 3VHX MET G 12 UNP P62331 EXPRESSION TAG
SEQADV 3VHX LEU G 67 UNP P62331 GLN 67 ENGINEERED MUTATION
SEQADV 3VHX LEU G 176 UNP P62331 EXPRESSION TAG
SEQADV 3VHX GLU G 177 UNP P62331 EXPRESSION TAG
SEQADV 3VHX HIS G 178 UNP P62331 EXPRESSION TAG
SEQADV 3VHX HIS G 179 UNP P62331 EXPRESSION TAG
SEQADV 3VHX HIS G 180 UNP P62331 EXPRESSION TAG
SEQADV 3VHX HIS G 181 UNP P62331 EXPRESSION TAG
SEQADV 3VHX HIS G 182 UNP P62331 EXPRESSION TAG
SEQADV 3VHX HIS G 183 UNP P62331 EXPRESSION TAG
SEQADV 3VHX GLY H 688 UNP Q02241 EXPRESSION TAG
SEQADV 3VHX SER H 689 UNP Q02241 EXPRESSION TAG
SEQRES 1 A 172 MET GLU MET ARG ILE LEU MET LEU GLY LEU ASP ALA ALA
SEQRES 2 A 172 GLY LYS THR THR ILE LEU TYR LYS LEU LYS LEU GLY GLN
SEQRES 3 A 172 SER VAL THR THR ILE PRO THR VAL GLY PHE ASN VAL GLU
SEQRES 4 A 172 THR VAL THR TYR LYS ASN VAL LYS PHE ASN VAL TRP ASP
SEQRES 5 A 172 VAL GLY GLY LEU ASP LYS ILE ARG PRO LEU TRP ARG HIS
SEQRES 6 A 172 TYR TYR THR GLY THR GLN GLY LEU ILE PHE VAL VAL ASP
SEQRES 7 A 172 CYS ALA ASP ARG ASP ARG ILE ASP GLU ALA ARG GLN GLU
SEQRES 8 A 172 LEU HIS ARG ILE ILE ASN ASP ARG GLU MET ARG ASP ALA
SEQRES 9 A 172 ILE ILE LEU ILE PHE ALA ASN LYS GLN ASP LEU PRO ASP
SEQRES 10 A 172 ALA MET LYS PRO HIS GLU ILE GLN GLU LYS LEU GLY LEU
SEQRES 11 A 172 THR ARG ILE ARG ASP ARG ASN TRP TYR VAL GLN PRO SER
SEQRES 12 A 172 CYS ALA THR SER GLY ASP GLY LEU TYR GLU GLY LEU THR
SEQRES 13 A 172 TRP LEU THR SER ASN TYR LYS SER LEU GLU HIS HIS HIS
SEQRES 14 A 172 HIS HIS HIS
SEQRES 1 B 120 GLY SER LEU LEU PHE GLN PRO ASP GLN ASN ALA PRO PRO
SEQRES 2 B 120 ILE ARG LEU ARG HIS ARG ARG SER ARG SER ALA GLY ASP
SEQRES 3 B 120 ARG TRP VAL ASP HIS LYS PRO ALA SER ASN MET GLN THR
SEQRES 4 B 120 GLU THR VAL MET GLN PRO HIS VAL PRO HIS ALA ILE THR
SEQRES 5 B 120 VAL SER VAL ALA ASN GLU LYS ALA LEU ALA LYS CYS GLU
SEQRES 6 B 120 LYS TYR MET LEU THR HIS GLN GLU LEU ALA SER ASP GLY
SEQRES 7 B 120 GLU ILE GLU THR LYS LEU ILE LYS GLY ASP ILE TYR LYS
SEQRES 8 B 120 THR ARG GLY GLY GLY GLN SER VAL GLN PHE THR ASP ILE
SEQRES 9 B 120 GLU THR LEU LYS GLN GLU SER PRO ASN GLY SER ARG LYS
SEQRES 10 B 120 ARG ARG SER
SEQRES 1 C 172 MET GLU MET ARG ILE LEU MET LEU GLY LEU ASP ALA ALA
SEQRES 2 C 172 GLY LYS THR THR ILE LEU TYR LYS LEU LYS LEU GLY GLN
SEQRES 3 C 172 SER VAL THR THR ILE PRO THR VAL GLY PHE ASN VAL GLU
SEQRES 4 C 172 THR VAL THR TYR LYS ASN VAL LYS PHE ASN VAL TRP ASP
SEQRES 5 C 172 VAL GLY GLY LEU ASP LYS ILE ARG PRO LEU TRP ARG HIS
SEQRES 6 C 172 TYR TYR THR GLY THR GLN GLY LEU ILE PHE VAL VAL ASP
SEQRES 7 C 172 CYS ALA ASP ARG ASP ARG ILE ASP GLU ALA ARG GLN GLU
SEQRES 8 C 172 LEU HIS ARG ILE ILE ASN ASP ARG GLU MET ARG ASP ALA
SEQRES 9 C 172 ILE ILE LEU ILE PHE ALA ASN LYS GLN ASP LEU PRO ASP
SEQRES 10 C 172 ALA MET LYS PRO HIS GLU ILE GLN GLU LYS LEU GLY LEU
SEQRES 11 C 172 THR ARG ILE ARG ASP ARG ASN TRP TYR VAL GLN PRO SER
SEQRES 12 C 172 CYS ALA THR SER GLY ASP GLY LEU TYR GLU GLY LEU THR
SEQRES 13 C 172 TRP LEU THR SER ASN TYR LYS SER LEU GLU HIS HIS HIS
SEQRES 14 C 172 HIS HIS HIS
SEQRES 1 D 120 GLY SER LEU LEU PHE GLN PRO ASP GLN ASN ALA PRO PRO
SEQRES 2 D 120 ILE ARG LEU ARG HIS ARG ARG SER ARG SER ALA GLY ASP
SEQRES 3 D 120 ARG TRP VAL ASP HIS LYS PRO ALA SER ASN MET GLN THR
SEQRES 4 D 120 GLU THR VAL MET GLN PRO HIS VAL PRO HIS ALA ILE THR
SEQRES 5 D 120 VAL SER VAL ALA ASN GLU LYS ALA LEU ALA LYS CYS GLU
SEQRES 6 D 120 LYS TYR MET LEU THR HIS GLN GLU LEU ALA SER ASP GLY
SEQRES 7 D 120 GLU ILE GLU THR LYS LEU ILE LYS GLY ASP ILE TYR LYS
SEQRES 8 D 120 THR ARG GLY GLY GLY GLN SER VAL GLN PHE THR ASP ILE
SEQRES 9 D 120 GLU THR LEU LYS GLN GLU SER PRO ASN GLY SER ARG LYS
SEQRES 10 D 120 ARG ARG SER
SEQRES 1 E 172 MET GLU MET ARG ILE LEU MET LEU GLY LEU ASP ALA ALA
SEQRES 2 E 172 GLY LYS THR THR ILE LEU TYR LYS LEU LYS LEU GLY GLN
SEQRES 3 E 172 SER VAL THR THR ILE PRO THR VAL GLY PHE ASN VAL GLU
SEQRES 4 E 172 THR VAL THR TYR LYS ASN VAL LYS PHE ASN VAL TRP ASP
SEQRES 5 E 172 VAL GLY GLY LEU ASP LYS ILE ARG PRO LEU TRP ARG HIS
SEQRES 6 E 172 TYR TYR THR GLY THR GLN GLY LEU ILE PHE VAL VAL ASP
SEQRES 7 E 172 CYS ALA ASP ARG ASP ARG ILE ASP GLU ALA ARG GLN GLU
SEQRES 8 E 172 LEU HIS ARG ILE ILE ASN ASP ARG GLU MET ARG ASP ALA
SEQRES 9 E 172 ILE ILE LEU ILE PHE ALA ASN LYS GLN ASP LEU PRO ASP
SEQRES 10 E 172 ALA MET LYS PRO HIS GLU ILE GLN GLU LYS LEU GLY LEU
SEQRES 11 E 172 THR ARG ILE ARG ASP ARG ASN TRP TYR VAL GLN PRO SER
SEQRES 12 E 172 CYS ALA THR SER GLY ASP GLY LEU TYR GLU GLY LEU THR
SEQRES 13 E 172 TRP LEU THR SER ASN TYR LYS SER LEU GLU HIS HIS HIS
SEQRES 14 E 172 HIS HIS HIS
SEQRES 1 F 120 GLY SER LEU LEU PHE GLN PRO ASP GLN ASN ALA PRO PRO
SEQRES 2 F 120 ILE ARG LEU ARG HIS ARG ARG SER ARG SER ALA GLY ASP
SEQRES 3 F 120 ARG TRP VAL ASP HIS LYS PRO ALA SER ASN MET GLN THR
SEQRES 4 F 120 GLU THR VAL MET GLN PRO HIS VAL PRO HIS ALA ILE THR
SEQRES 5 F 120 VAL SER VAL ALA ASN GLU LYS ALA LEU ALA LYS CYS GLU
SEQRES 6 F 120 LYS TYR MET LEU THR HIS GLN GLU LEU ALA SER ASP GLY
SEQRES 7 F 120 GLU ILE GLU THR LYS LEU ILE LYS GLY ASP ILE TYR LYS
SEQRES 8 F 120 THR ARG GLY GLY GLY GLN SER VAL GLN PHE THR ASP ILE
SEQRES 9 F 120 GLU THR LEU LYS GLN GLU SER PRO ASN GLY SER ARG LYS
SEQRES 10 F 120 ARG ARG SER
SEQRES 1 G 172 MET GLU MET ARG ILE LEU MET LEU GLY LEU ASP ALA ALA
SEQRES 2 G 172 GLY LYS THR THR ILE LEU TYR LYS LEU LYS LEU GLY GLN
SEQRES 3 G 172 SER VAL THR THR ILE PRO THR VAL GLY PHE ASN VAL GLU
SEQRES 4 G 172 THR VAL THR TYR LYS ASN VAL LYS PHE ASN VAL TRP ASP
SEQRES 5 G 172 VAL GLY GLY LEU ASP LYS ILE ARG PRO LEU TRP ARG HIS
SEQRES 6 G 172 TYR TYR THR GLY THR GLN GLY LEU ILE PHE VAL VAL ASP
SEQRES 7 G 172 CYS ALA ASP ARG ASP ARG ILE ASP GLU ALA ARG GLN GLU
SEQRES 8 G 172 LEU HIS ARG ILE ILE ASN ASP ARG GLU MET ARG ASP ALA
SEQRES 9 G 172 ILE ILE LEU ILE PHE ALA ASN LYS GLN ASP LEU PRO ASP
SEQRES 10 G 172 ALA MET LYS PRO HIS GLU ILE GLN GLU LYS LEU GLY LEU
SEQRES 11 G 172 THR ARG ILE ARG ASP ARG ASN TRP TYR VAL GLN PRO SER
SEQRES 12 G 172 CYS ALA THR SER GLY ASP GLY LEU TYR GLU GLY LEU THR
SEQRES 13 G 172 TRP LEU THR SER ASN TYR LYS SER LEU GLU HIS HIS HIS
SEQRES 14 G 172 HIS HIS HIS
SEQRES 1 H 120 GLY SER LEU LEU PHE GLN PRO ASP GLN ASN ALA PRO PRO
SEQRES 2 H 120 ILE ARG LEU ARG HIS ARG ARG SER ARG SER ALA GLY ASP
SEQRES 3 H 120 ARG TRP VAL ASP HIS LYS PRO ALA SER ASN MET GLN THR
SEQRES 4 H 120 GLU THR VAL MET GLN PRO HIS VAL PRO HIS ALA ILE THR
SEQRES 5 H 120 VAL SER VAL ALA ASN GLU LYS ALA LEU ALA LYS CYS GLU
SEQRES 6 H 120 LYS TYR MET LEU THR HIS GLN GLU LEU ALA SER ASP GLY
SEQRES 7 H 120 GLU ILE GLU THR LYS LEU ILE LYS GLY ASP ILE TYR LYS
SEQRES 8 H 120 THR ARG GLY GLY GLY GLN SER VAL GLN PHE THR ASP ILE
SEQRES 9 H 120 GLU THR LEU LYS GLN GLU SER PRO ASN GLY SER ARG LYS
SEQRES 10 H 120 ARG ARG SER
HET GTP A 184 32
HET MG A 185 1
HET GTP C 184 32
HET MG C 185 1
HET GTP E 184 32
HET MG E 185 1
HET GOL F 1 6
HET GTP G 184 32
HET MG G 185 1
HETNAM GTP GUANOSINE-5'-TRIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 9 GTP 4(C10 H16 N5 O14 P3)
FORMUL 10 MG 4(MG 2+)
FORMUL 15 GOL C3 H8 O3
FORMUL 18 HOH *105(H2 O)
HELIX 1 1 GLY A 25 GLY A 36 1 12
HELIX 2 2 ILE A 70 TYR A 78 5 9
HELIX 3 3 ARG A 95 ASN A 108 1 14
HELIX 4 4 ASP A 109 ARG A 113 5 5
HELIX 5 5 LYS A 131 LEU A 139 1 9
HELIX 6 6 GLY A 161 ASN A 172 1 12
HELIX 7 7 ASN B 744 CYS B 751 1 8
HELIX 8 8 GLY C 25 GLY C 36 1 12
HELIX 9 9 ILE C 70 TYR C 78 5 9
HELIX 10 10 ARG C 95 ASN C 108 1 14
HELIX 11 11 ASP C 109 ARG C 113 5 5
HELIX 12 12 LYS C 131 LEU C 139 1 9
HELIX 13 13 GLY C 161 ASN C 172 1 12
HELIX 14 14 ASN D 744 CYS D 751 1 8
HELIX 15 15 GLY E 25 GLY E 36 1 12
HELIX 16 16 ILE E 70 TYR E 78 5 9
HELIX 17 17 ARG E 95 ASN E 108 1 14
HELIX 18 18 ASP E 109 ARG E 113 5 5
HELIX 19 19 LYS E 131 LEU E 139 1 9
HELIX 20 20 GLY E 161 ASN E 172 1 12
HELIX 21 21 ASN F 744 CYS F 751 1 8
HELIX 22 22 GLY G 25 GLY G 36 1 12
HELIX 23 23 ILE G 70 TYR G 78 5 9
HELIX 24 24 ARG G 95 ASN G 108 1 14
HELIX 25 25 ASP G 109 ARG G 113 5 5
HELIX 26 26 LYS G 131 LEU G 139 1 9
HELIX 27 27 GLY G 161 ASN G 172 1 12
HELIX 28 28 ASN H 744 CYS H 751 1 8
SHEET 1 A11 TRP A 149 PRO A 153 0
SHEET 2 A11 ILE A 116 ASN A 122 1 N ILE A 119 O GLN A 152
SHEET 3 A11 GLY A 83 ASP A 89 1 N PHE A 86 O LEU A 118
SHEET 4 A11 GLU A 13 LEU A 19 1 N LEU A 17 O ILE A 85
SHEET 5 A11 VAL A 57 VAL A 64 1 O ASN A 60 N MET A 14
SHEET 6 A11 GLY A 46 TYR A 54 -1 N VAL A 52 O PHE A 59
SHEET 7 A11 GLN B 784 LYS B 795 -1 O GLN B 784 N VAL A 49
SHEET 8 A11 ILE B 767 LYS B 778 -1 N THR B 769 O LEU B 794
SHEET 9 A11 LYS B 753 LEU B 761 -1 N HIS B 758 O LYS B 770
SHEET 10 A11 TRP B 715 HIS B 718 1 N HIS B 718 O MET B 755
SHEET 11 A11 ALA B 737 VAL B 740 1 O ILE B 738 N ASP B 717
SHEET 1 B11 TRP C 149 PRO C 153 0
SHEET 2 B11 ILE C 116 ASN C 122 1 N ILE C 119 O GLN C 152
SHEET 3 B11 GLY C 83 ASP C 89 1 N LEU C 84 O LEU C 118
SHEET 4 B11 GLU C 13 LEU C 19 1 N LEU C 17 O ILE C 85
SHEET 5 B11 VAL C 57 VAL C 64 1 O ASN C 60 N ILE C 16
SHEET 6 B11 GLY C 46 TYR C 54 -1 N VAL C 52 O PHE C 59
SHEET 7 B11 GLN D 784 LYS D 795 -1 O GLN D 784 N VAL C 49
SHEET 8 B11 ILE D 767 LYS D 778 -1 N TYR D 777 O SER D 785
SHEET 9 B11 LYS D 753 LEU D 761 -1 N HIS D 758 O LYS D 770
SHEET 10 B11 TRP D 715 HIS D 718 1 N VAL D 716 O LYS D 753
SHEET 11 B11 ALA D 737 VAL D 740 1 O ILE D 738 N ASP D 717
SHEET 1 C11 TRP E 149 PRO E 153 0
SHEET 2 C11 ILE E 116 ASN E 122 1 N ILE E 119 O GLN E 152
SHEET 3 C11 GLY E 83 ASP E 89 1 N LEU E 84 O LEU E 118
SHEET 4 C11 GLU E 13 GLY E 20 1 N LEU E 17 O ILE E 85
SHEET 5 C11 VAL E 57 VAL E 64 1 O ASN E 60 N ILE E 16
SHEET 6 C11 GLY E 46 TYR E 54 -1 N ASN E 48 O ASP E 63
SHEET 7 C11 GLN F 784 LYS F 795 -1 O GLN F 784 N VAL E 49
SHEET 8 C11 ILE F 767 LYS F 778 -1 N TYR F 777 O SER F 785
SHEET 9 C11 LYS F 753 LEU F 761 -1 N HIS F 758 O LYS F 770
SHEET 10 C11 TRP F 715 HIS F 718 1 N VAL F 716 O LYS F 753
SHEET 11 C11 ALA F 737 VAL F 740 1 O ILE F 738 N ASP F 717
SHEET 1 D11 TRP G 149 SER G 154 0
SHEET 2 D11 ILE G 116 ASN G 122 1 N ILE G 119 O GLN G 152
SHEET 3 D11 GLY G 83 ASP G 89 1 N PHE G 86 O LEU G 118
SHEET 4 D11 GLU G 13 LEU G 19 1 N LEU G 17 O ILE G 85
SHEET 5 D11 VAL G 57 VAL G 64 1 O ASN G 60 N ILE G 16
SHEET 6 D11 GLY G 46 TYR G 54 -1 N VAL G 52 O PHE G 59
SHEET 7 D11 GLN H 784 LYS H 795 -1 O GLN H 784 N VAL G 49
SHEET 8 D11 ILE H 767 LYS H 778 -1 N TYR H 777 O SER H 785
SHEET 9 D11 LYS H 753 LEU H 761 -1 N LEU H 756 O ILE H 772
SHEET 10 D11 TRP H 715 HIS H 718 1 N HIS H 718 O MET H 755
SHEET 11 D11 ALA H 737 VAL H 740 1 O ILE H 738 N ASP H 717
LINK OG1 THR A 27 MG MG A 185 1555 1555 1.81
LINK OG1 THR A 44 MG MG A 185 1555 1555 2.41
LINK O1B GTP A 184 MG MG A 185 1555 1555 2.04
LINK O1G GTP A 184 MG MG A 185 1555 1555 2.33
LINK MG MG A 185 O HOH A 193 1555 1555 2.24
LINK OG1 THR C 27 MG MG C 185 1555 1555 2.26
LINK OG1 THR C 44 MG MG C 185 1555 1555 2.16
LINK O1G GTP C 184 MG MG C 185 1555 1555 1.94
LINK O1B GTP C 184 MG MG C 185 1555 1555 2.16
LINK MG MG C 185 O HOH C 210 1555 1555 1.73
LINK MG MG C 185 O HOH C 211 1555 1555 2.19
LINK OG1 THR E 27 MG MG E 185 1555 1555 2.28
LINK OG1 THR E 44 MG MG E 185 1555 1555 2.42
LINK O1G GTP E 184 MG MG E 185 1555 1555 1.94
LINK O1B GTP E 184 MG MG E 185 1555 1555 2.04
LINK MG MG E 185 O HOH E 201 1555 1555 2.23
LINK MG MG E 185 O HOH E 204 1555 1555 1.73
LINK OG1 THR G 27 MG MG G 185 1555 1555 2.13
LINK OG1 THR G 44 MG MG G 185 1555 1555 2.30
LINK O1G GTP G 184 MG MG G 185 1555 1555 1.85
LINK O1B GTP G 184 MG MG G 185 1555 1555 2.23
SITE 1 AC1 20 ASP A 22 ALA A 23 ALA A 24 GLY A 25
SITE 2 AC1 20 LYS A 26 THR A 27 THR A 28 THR A 41
SITE 3 AC1 20 THR A 44 GLY A 66 ASN A 122 LYS A 123
SITE 4 AC1 20 ASP A 125 LEU A 126 CYS A 155 ALA A 156
SITE 5 AC1 20 THR A 157 MG A 185 HOH A 186 HOH A 193
SITE 1 AC2 4 THR A 27 THR A 44 GTP A 184 HOH A 193
SITE 1 AC3 23 ASP C 22 ALA C 23 ALA C 24 GLY C 25
SITE 2 AC3 23 LYS C 26 THR C 27 THR C 28 THR C 41
SITE 3 AC3 23 PRO C 43 THR C 44 GLY C 65 GLY C 66
SITE 4 AC3 23 ASN C 122 LYS C 123 ASP C 125 LEU C 126
SITE 5 AC3 23 CYS C 155 ALA C 156 MG C 185 HOH C 204
SITE 6 AC3 23 HOH C 210 HOH C 211 HOH C 212
SITE 1 AC4 5 THR C 27 THR C 44 GTP C 184 HOH C 210
SITE 2 AC4 5 HOH C 211
SITE 1 AC5 21 ASP E 22 ALA E 23 ALA E 24 GLY E 25
SITE 2 AC5 21 LYS E 26 THR E 27 THR E 28 THR E 41
SITE 3 AC5 21 PRO E 43 THR E 44 GLY E 66 LEU E 67
SITE 4 AC5 21 ASN E 122 LYS E 123 ASP E 125 LEU E 126
SITE 5 AC5 21 CYS E 155 ALA E 156 MG E 185 HOH E 201
SITE 6 AC5 21 HOH E 204
SITE 1 AC6 5 THR E 27 THR E 44 GTP E 184 HOH E 201
SITE 2 AC6 5 HOH E 204
SITE 1 AC7 5 ARG E 75 HIS E 76 PRO F 720 ALA F 721
SITE 2 AC7 5 SER F 722
SITE 1 AC8 17 ASP G 22 ALA G 23 GLY G 25 LYS G 26
SITE 2 AC8 17 THR G 27 THR G 28 THR G 41 THR G 44
SITE 3 AC8 17 GLY G 66 ASN G 122 LYS G 123 ASP G 125
SITE 4 AC8 17 LEU G 126 CYS G 155 ALA G 156 THR G 157
SITE 5 AC8 17 MG G 185
SITE 1 AC9 3 THR G 27 THR G 44 GTP G 184
CRYST1 45.743 174.573 76.814 90.00 98.74 90.00 P 1 21 1 8
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 0.021861 0.000000 0.003361 0.00000
SCALE2 0.000000 0.005728 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013171 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
