HEADER MOTOR PROTEIN 05-JUL-17 5WDH
TITLE MOTOR DOMAIN OF HUMAN KINESIN FAMILY MEMBER C1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KINESIN-LIKE PROTEIN KIFC1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MOTOR DOMAIN (UNP RESIDUES 307-663);
COMPND 5 SYNONYM: KINESIN-LIKE PROTEIN 2,KINESIN-RELATED PROTEIN HSET;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: KIFC1, HSET, KNSL2;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HIGHFIVE;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PFBOH-LIC
KEYWDS KINESIN, STRUCTURAL GENOMICS CONSORTIUM, MOTOR DOMAIN, ADP, SGC,
KEYWDS 2 MOTOR PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.ZHU,W.TEMPEL,H.HE,Y.SHEN,J.WANG,G.BROTHERS,R.LANDRY,C.H.ARROWSMITH,
AUTHOR 2 A.M.EDWARDS,H.PARK,STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 3 04-OCT-23 5WDH 1 LINK
REVDAT 2 20-DEC-17 5WDH 1 JRNL
REVDAT 1 09-AUG-17 5WDH 0
SPRSDE 09-AUG-17 5WDH 2REP
JRNL AUTH H.W.PARK,Z.MA,H.ZHU,S.JIANG,R.C.ROBINSON,S.A.ENDOW
JRNL TITL STRUCTURAL BASIS OF SMALL MOLECULE ATPASE INHIBITION OF A
JRNL TITL 2 HUMAN MITOTIC KINESIN MOTOR PROTEIN.
JRNL REF SCI REP V. 7 15121 2017
JRNL REFN ESSN 2045-2322
JRNL PMID 29123223
JRNL DOI 10.1038/S41598-017-14754-6
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1_2575
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.35
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.920
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 45145
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.226
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120
REMARK 3 FREE R VALUE TEST SET COUNT : 2310
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 39.3559 - 5.7741 0.99 2512 128 0.2172 0.2216
REMARK 3 2 5.7741 - 4.5853 1.00 2546 123 0.1879 0.1991
REMARK 3 3 4.5853 - 4.0064 1.00 2562 119 0.1749 0.2229
REMARK 3 4 4.0064 - 3.6403 1.00 2557 107 0.2039 0.2368
REMARK 3 5 3.6403 - 3.3796 1.00 2517 136 0.2132 0.2974
REMARK 3 6 3.3796 - 3.1804 1.00 2513 139 0.2508 0.3080
REMARK 3 7 3.1804 - 3.0212 1.00 2509 157 0.2789 0.3806
REMARK 3 8 3.0212 - 2.8897 1.00 2542 148 0.3024 0.3590
REMARK 3 9 2.8897 - 2.7785 1.00 2527 125 0.2746 0.3585
REMARK 3 10 2.7785 - 2.6826 1.00 2530 152 0.2750 0.2688
REMARK 3 11 2.6826 - 2.5988 1.00 2528 133 0.2755 0.3228
REMARK 3 12 2.5988 - 2.5245 1.00 2519 133 0.2637 0.3506
REMARK 3 13 2.5245 - 2.4581 0.99 2474 141 0.2694 0.2866
REMARK 3 14 2.4581 - 2.3981 1.00 2546 152 0.2986 0.3222
REMARK 3 15 2.3981 - 2.3436 0.99 2494 135 0.2992 0.3128
REMARK 3 16 2.3436 - 2.2937 0.99 2511 143 0.3270 0.3264
REMARK 3 17 2.2937 - 2.2478 0.96 2448 139 0.3559 0.3816
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.550
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 61.21
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 84.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.009 2215
REMARK 3 ANGLE : 0.895 3010
REMARK 3 CHIRALITY : 0.051 349
REMARK 3 PLANARITY : 0.005 391
REMARK 3 DIHEDRAL : 18.085 1314
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 309 THROUGH 451 )
REMARK 3 ORIGIN FOR THE GROUP (A): 47.3023 17.8187 107.0414
REMARK 3 T TENSOR
REMARK 3 T11: 0.5591 T22: 0.9520
REMARK 3 T33: 0.6150 T12: 0.0190
REMARK 3 T13: 0.0262 T23: -0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 2.1471 L22: 0.4842
REMARK 3 L33: 2.4526 L12: -0.4821
REMARK 3 L13: -0.9042 L23: 0.5896
REMARK 3 S TENSOR
REMARK 3 S11: 0.4097 S12: 0.4544 S13: -0.1588
REMARK 3 S21: -0.1161 S22: -0.3396 S23: 0.1236
REMARK 3 S31: 0.6409 S32: -0.9159 S33: 0.0029
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 452 THROUGH 509 )
REMARK 3 ORIGIN FOR THE GROUP (A): 68.6000 27.3227 103.3423
REMARK 3 T TENSOR
REMARK 3 T11: 0.6657 T22: 0.7787
REMARK 3 T33: 0.7607 T12: 0.1415
REMARK 3 T13: 0.2195 T23: 0.1599
REMARK 3 L TENSOR
REMARK 3 L11: 0.7765 L22: 1.0512
REMARK 3 L33: 1.3702 L12: 0.7747
REMARK 3 L13: -0.0972 L23: 0.4950
REMARK 3 S TENSOR
REMARK 3 S11: 0.2223 S12: 0.4285 S13: 0.4665
REMARK 3 S21: -0.3192 S22: 0.0790 S23: -0.3776
REMARK 3 S31: 0.0910 S32: 0.3323 S33: -0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 510 THROUGH 550 )
REMARK 3 ORIGIN FOR THE GROUP (A): 63.3959 26.2454 110.3065
REMARK 3 T TENSOR
REMARK 3 T11: 0.6256 T22: 0.6870
REMARK 3 T33: 0.7627 T12: 0.0805
REMARK 3 T13: 0.1605 T23: 0.0819
REMARK 3 L TENSOR
REMARK 3 L11: 0.8203 L22: 0.4491
REMARK 3 L33: 1.7928 L12: -0.1056
REMARK 3 L13: 0.8960 L23: -0.7064
REMARK 3 S TENSOR
REMARK 3 S11: 0.2908 S12: 0.3512 S13: 0.1374
REMARK 3 S21: -0.1180 S22: -0.0025 S23: 0.0302
REMARK 3 S31: -0.0356 S32: -0.0223 S33: -0.0004
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 551 THROUGH 663 )
REMARK 3 ORIGIN FOR THE GROUP (A): 51.7277 25.9436 95.6297
REMARK 3 T TENSOR
REMARK 3 T11: 0.6904 T22: 1.1943
REMARK 3 T33: 0.7294 T12: 0.2980
REMARK 3 T13: 0.1345 T23: 0.1596
REMARK 3 L TENSOR
REMARK 3 L11: 0.6637 L22: 0.5462
REMARK 3 L33: 1.7056 L12: 0.0469
REMARK 3 L13: -0.0181 L23: -0.2366
REMARK 3 S TENSOR
REMARK 3 S11: 0.5619 S12: 1.1681 S13: 0.3476
REMARK 3 S21: -0.5706 S22: -0.4676 S23: -0.0345
REMARK 3 S31: 0.0502 S32: -0.7660 S33: 0.0003
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: MERGING STATISTICS INDICATE SIGNIFICANT
REMARK 3 ANISOTROPY OF CRYSTAL DIFFRACTION. NOTWITHSTANDING THE NOMINAL
REMARK 3 RESOLUTION CUT-OFF, ELECTRON DENSITY WAS NOT CLEAR ENOUGH TO
REMARK 3 CONFIRM CORRECTNESS OF THE SEQUENCE REGISTER OUTRIGHT. THE
REMARK 3 HIGHER RESOLUTION PDB ENTRY 1F9T OF A YEAST KINESIN-LIKE PROTEIN
REMARK 3 WAS USED TO VALIDATE REGISTER AND CONFORMATION OF SOME SIDE
REMARK 3 CHAINS. NEVERTHELESS, THE CURRENT MODEL CONTAINS SEGMENTS WHERE
REMARK 3 THE ALIGNMENT OF THE AMINO ACID SEQUENCE REMAINS UNCERTAIN.
REMARK 4
REMARK 4 5WDH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1000228248.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-JUN-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.5.32
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24875
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 48.490
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 14.00
REMARK 200 R MERGE (I) : 0.04600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 29.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.32
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.4
REMARK 200 DATA REDUNDANCY IN SHELL : 13.80
REMARK 200 R MERGE FOR SHELL (I) : 1.33600
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 2NCD
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.43
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.5M SODIUM CHLORIDE, 0.1M BIS-TRIS
REMARK 280 PROPANE, 5% GLYCEROL, PH 7.5, VAPOR DIFFUSION, TEMPERATURE 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z+1/2
REMARK 290 7555 Y,X,-Z+3/4
REMARK 290 8555 -Y,-X,-Z+1/4
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 121.21600
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 60.60800
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 181.82400
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 121.21600
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 181.82400
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 60.60800
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: 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 MET A 288
REMARK 465 GLY A 289
REMARK 465 SER A 290
REMARK 465 SER A 291
REMARK 465 HIS A 292
REMARK 465 HIS A 293
REMARK 465 HIS A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 465 SER A 298
REMARK 465 SER A 299
REMARK 465 GLY A 300
REMARK 465 LEU A 301
REMARK 465 VAL A 302
REMARK 465 PRO A 303
REMARK 465 ARG A 304
REMARK 465 GLY A 305
REMARK 465 SER A 306
REMARK 465 LEU A 307
REMARK 465 LYS A 308
REMARK 465 PRO A 338
REMARK 465 GLY A 339
REMARK 465 GLY A 340
REMARK 465 PRO A 341
REMARK 465 SER A 342
REMARK 465 SER A 353
REMARK 465 ASP A 354
REMARK 465 GLU A 355
REMARK 465 ARG A 356
REMARK 465 ARG A 357
REMARK 465 GLY A 358
REMARK 465 THR A 359
REMARK 465 LEU A 360
REMARK 465 SER A 361
REMARK 465 GLY A 362
REMARK 465 ALA A 363
REMARK 465 PRO A 364
REMARK 465 ALA A 365
REMARK 465 PRO A 366
REMARK 465 PRO A 367
REMARK 465 THR A 477
REMARK 465 ARG A 478
REMARK 465 LYS A 479
REMARK 465 GLY A 480
REMARK 465 GLN A 481
REMARK 465 GLY A 482
REMARK 465 GLY A 483
REMARK 465 GLY A 491
REMARK 465 PRO A 492
REMARK 465 GLY A 493
REMARK 465 ALA A 530
REMARK 465 GLN A 531
REMARK 465 ASN A 532
REMARK 465 GLU A 533
REMARK 465 LEU A 572
REMARK 465 ASP A 573
REMARK 465 PRO A 574
REMARK 465 GLY A 575
REMARK 465 LEU A 576
REMARK 465 ALA A 577
REMARK 465 LEU A 578
REMARK 465 GLY A 579
REMARK 465 PRO A 580
REMARK 465 GLY A 581
REMARK 465 GLU A 582
REMARK 465 ARG A 583
REMARK 465 GLU A 584
REMARK 465 ARG A 585
REMARK 465 LEU A 586
REMARK 465 ARG A 587
REMARK 465 GLU A 588
REMARK 465 THR A 589
REMARK 465 GLN A 590
REMARK 465 ALA A 591
REMARK 465 ILE A 592
REMARK 465 ASN A 593
REMARK 465 SER A 594
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 ARG A 312 NE CZ NH1 NH2
REMARK 470 LEU A 333 CG CD1 CD2
REMARK 470 SER A 336 OG
REMARK 470 GLY A 337 CA C O
REMARK 470 ASP A 343 CG OD1 OD2
REMARK 470 ARG A 352 CA C O CB CG CD NE
REMARK 470 ARG A 352 CZ NH1 NH2
REMARK 470 PRO A 368 N CB CG CD
REMARK 470 ARG A 369 CG CD NE CZ NH1 NH2
REMARK 470 SER A 382 OG
REMARK 470 GLU A 389 CD OE1 OE2
REMARK 470 GLN A 446 CD OE1 NE2
REMARK 470 GLU A 447 CD OE1 OE2
REMARK 470 GLN A 451 CD OE1 NE2
REMARK 470 ASN A 466 OD1 ND2
REMARK 470 GLU A 467 CG CD OE1 OE2
REMARK 470 ARG A 470 CD NE CZ NH1 NH2
REMARK 470 GLY A 476 C O
REMARK 470 GLU A 484 CG CD OE1 OE2
REMARK 470 GLU A 486 CG CD OE1 OE2
REMARK 470 ILE A 487 CD1
REMARK 470 ARG A 488 CD NE CZ NH1 NH2
REMARK 470 SER A 494 N CB OG
REMARK 470 GLU A 495 CG CD OE1 OE2
REMARK 470 GLU A 496 CG CD OE1 OE2
REMARK 470 LYS A 511 NZ
REMARK 470 ARG A 528 NE CZ NH1 NH2
REMARK 470 THR A 529 C O CB OG1 CG2
REMARK 470 ARG A 537 CG CD NE CZ NH1 NH2
REMARK 470 SER A 551 OG
REMARK 470 GLN A 556 OE1 NE2
REMARK 470 ARG A 571 C O CB CG CD NE CZ
REMARK 470 ARG A 571 NH1 NH2
REMARK 470 SER A 595 OG
REMARK 470 LEU A 596 CG CD1 CD2
REMARK 470 SER A 597 OG
REMARK 470 LEU A 601 CG CD1 CD2
REMARK 470 MET A 604 CG SD CE
REMARK 470 SER A 607 OG
REMARK 470 LYS A 609 CD CE NZ
REMARK 470 GLU A 610 CD OE1 OE2
REMARK 470 SER A 611 OG
REMARK 470 HIS A 612 ND1 CD2 CE1 NE2
REMARK 470 SER A 631 OG
REMARK 470 LYS A 633 NZ
REMARK 470 GLU A 644 CD OE1 OE2
REMARK 470 SER A 658 OG
REMARK 470 LYS A 659 CE NZ
REMARK 470 GLN A 662 CG CD OE1 NE2
REMARK 470 CYS A 663 SG
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 NE ARG A 439 OE1 GLU A 510 2.16
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 ASN A 310 49.32 -75.11
REMARK 500 THR A 475 -55.64 -121.85
REMARK 500 ALA A 559 147.00 -171.03
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 802 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 417 OG1
REMARK 620 2 ADP A 801 O2B 76.7
REMARK 620 3 HOH A 901 O 84.7 94.5
REMARK 620 4 HOH A 902 O 171.5 96.1 100.4
REMARK 620 5 HOH A 903 O 86.1 82.0 170.7 88.6
REMARK 620 6 HOH A 904 O 93.9 160.7 101.4 91.8 80.6
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 802
DBREF 5WDH A 307 663 UNP Q9BW19 KIFC1_HUMAN 307 663
SEQADV 5WDH MET A 288 UNP Q9BW19 INITIATING METHIONINE
SEQADV 5WDH GLY A 289 UNP Q9BW19 EXPRESSION TAG
SEQADV 5WDH SER A 290 UNP Q9BW19 EXPRESSION TAG
SEQADV 5WDH SER A 291 UNP Q9BW19 EXPRESSION TAG
SEQADV 5WDH HIS A 292 UNP Q9BW19 EXPRESSION TAG
SEQADV 5WDH HIS A 293 UNP Q9BW19 EXPRESSION TAG
SEQADV 5WDH HIS A 294 UNP Q9BW19 EXPRESSION TAG
SEQADV 5WDH HIS A 295 UNP Q9BW19 EXPRESSION TAG
SEQADV 5WDH HIS A 296 UNP Q9BW19 EXPRESSION TAG
SEQADV 5WDH HIS A 297 UNP Q9BW19 EXPRESSION TAG
SEQADV 5WDH SER A 298 UNP Q9BW19 EXPRESSION TAG
SEQADV 5WDH SER A 299 UNP Q9BW19 EXPRESSION TAG
SEQADV 5WDH GLY A 300 UNP Q9BW19 EXPRESSION TAG
SEQADV 5WDH LEU A 301 UNP Q9BW19 EXPRESSION TAG
SEQADV 5WDH VAL A 302 UNP Q9BW19 EXPRESSION TAG
SEQADV 5WDH PRO A 303 UNP Q9BW19 EXPRESSION TAG
SEQADV 5WDH ARG A 304 UNP Q9BW19 EXPRESSION TAG
SEQADV 5WDH GLY A 305 UNP Q9BW19 EXPRESSION TAG
SEQADV 5WDH SER A 306 UNP Q9BW19 EXPRESSION TAG
SEQADV 5WDH PRO A 368 UNP Q9BW19 THR 368 CONFLICT
SEQRES 1 A 376 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 376 LEU VAL PRO ARG GLY SER LEU LYS GLY ASN ILE ARG VAL
SEQRES 3 A 376 PHE CYS ARG VAL ARG PRO VAL LEU PRO GLY GLU PRO THR
SEQRES 4 A 376 PRO PRO PRO GLY LEU LEU LEU PHE PRO SER GLY PRO GLY
SEQRES 5 A 376 GLY PRO SER ASP PRO PRO THR ARG LEU SER LEU SER ARG
SEQRES 6 A 376 SER ASP GLU ARG ARG GLY THR LEU SER GLY ALA PRO ALA
SEQRES 7 A 376 PRO PRO PRO ARG HIS ASP PHE SER PHE ASP ARG VAL PHE
SEQRES 8 A 376 PRO PRO GLY SER GLY GLN ASP GLU VAL PHE GLU GLU ILE
SEQRES 9 A 376 ALA MET LEU VAL GLN SER ALA LEU ASP GLY TYR PRO VAL
SEQRES 10 A 376 CYS ILE PHE ALA TYR GLY GLN THR GLY SER GLY LYS THR
SEQRES 11 A 376 PHE THR MET GLU GLY GLY PRO GLY GLY ASP PRO GLN LEU
SEQRES 12 A 376 GLU GLY LEU ILE PRO ARG ALA LEU ARG HIS LEU PHE SER
SEQRES 13 A 376 VAL ALA GLN GLU LEU SER GLY GLN GLY TRP THR TYR SER
SEQRES 14 A 376 PHE VAL ALA SER TYR VAL GLU ILE TYR ASN GLU THR VAL
SEQRES 15 A 376 ARG ASP LEU LEU ALA THR GLY THR ARG LYS GLY GLN GLY
SEQRES 16 A 376 GLY GLU CYS GLU ILE ARG ARG ALA GLY PRO GLY SER GLU
SEQRES 17 A 376 GLU LEU THR VAL THR ASN ALA ARG TYR VAL PRO VAL SER
SEQRES 18 A 376 CYS GLU LYS GLU VAL ASP ALA LEU LEU HIS LEU ALA ARG
SEQRES 19 A 376 GLN ASN ARG ALA VAL ALA ARG THR ALA GLN ASN GLU ARG
SEQRES 20 A 376 SER SER ARG SER HIS SER VAL PHE GLN LEU GLN ILE SER
SEQRES 21 A 376 GLY GLU HIS SER SER ARG GLY LEU GLN CYS GLY ALA PRO
SEQRES 22 A 376 LEU SER LEU VAL ASP LEU ALA GLY SER GLU ARG LEU ASP
SEQRES 23 A 376 PRO GLY LEU ALA LEU GLY PRO GLY GLU ARG GLU ARG LEU
SEQRES 24 A 376 ARG GLU THR GLN ALA ILE ASN SER SER LEU SER THR LEU
SEQRES 25 A 376 GLY LEU VAL ILE MET ALA LEU SER ASN LYS GLU SER HIS
SEQRES 26 A 376 VAL PRO TYR ARG ASN SER LYS LEU THR TYR LEU LEU GLN
SEQRES 27 A 376 ASN SER LEU GLY GLY SER ALA LYS MET LEU MET PHE VAL
SEQRES 28 A 376 ASN ILE SER PRO LEU GLU GLU ASN VAL SER GLU SER LEU
SEQRES 29 A 376 ASN SER LEU ARG PHE ALA SER LYS VAL ASN GLN CYS
HET ADP A 801 27
HET MG A 802 1
HET UNX A 803 1
HET UNX A 804 1
HET UNX A 805 1
HET UNX A 806 1
HET UNX A 807 1
HET UNX A 808 1
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM UNX UNKNOWN ATOM OR ION
FORMUL 2 ADP C10 H15 N5 O10 P2
FORMUL 3 MG MG 2+
FORMUL 4 UNX 6(X)
FORMUL 10 HOH *4(H2 O)
HELIX 1 AA1 GLY A 383 GLU A 390 1 8
HELIX 2 AA2 ILE A 391 SER A 397 1 7
HELIX 3 AA3 ALA A 398 GLY A 401 5 4
HELIX 4 AA4 GLY A 415 GLU A 421 1 7
HELIX 5 AA5 ASP A 427 GLU A 431 5 5
HELIX 6 AA6 GLY A 432 GLY A 450 1 19
HELIX 7 AA7 CYS A 509 ALA A 527 1 19
HELIX 8 AA8 ARG A 534 SER A 538 5 5
HELIX 9 AA9 LEU A 596 ASN A 608 1 13
HELIX 10 AB1 PRO A 614 ASN A 617 5 4
HELIX 11 AB2 SER A 618 GLN A 625 1 8
HELIX 12 AB3 ASN A 626 LEU A 628 5 3
HELIX 13 AB4 LEU A 643 GLU A 645 5 3
HELIX 14 AB5 ASN A 646 CYS A 663 1 18
SHEET 1 AA1 8 ARG A 376 PHE A 378 0
SHEET 2 AA1 8 ILE A 311 VAL A 317 1 N CYS A 315 O PHE A 378
SHEET 3 AA1 8 LYS A 633 ILE A 640 1 O VAL A 638 N PHE A 314
SHEET 4 AA1 8 VAL A 404 TYR A 409 1 N TYR A 409 O ASN A 639
SHEET 5 AA1 8 GLN A 556 ASP A 565 1 O SER A 562 N ILE A 406
SHEET 6 AA1 8 HIS A 539 HIS A 550 -1 N PHE A 542 O LEU A 563
SHEET 7 AA1 8 TRP A 453 TYR A 465 -1 N VAL A 462 O VAL A 541
SHEET 8 AA1 8 THR A 468 ASP A 471 -1 O ARG A 470 N GLU A 463
SHEET 1 AA2 8 ARG A 376 PHE A 378 0
SHEET 2 AA2 8 ILE A 311 VAL A 317 1 N CYS A 315 O PHE A 378
SHEET 3 AA2 8 LYS A 633 ILE A 640 1 O VAL A 638 N PHE A 314
SHEET 4 AA2 8 VAL A 404 TYR A 409 1 N TYR A 409 O ASN A 639
SHEET 5 AA2 8 GLN A 556 ASP A 565 1 O SER A 562 N ILE A 406
SHEET 6 AA2 8 HIS A 539 HIS A 550 -1 N PHE A 542 O LEU A 563
SHEET 7 AA2 8 TRP A 453 TYR A 465 -1 N VAL A 462 O VAL A 541
SHEET 8 AA2 8 VAL A 505 PRO A 506 -1 O VAL A 505 N ALA A 459
SHEET 1 AA3 3 LEU A 332 LEU A 333 0
SHEET 2 AA3 3 ARG A 347 LEU A 350 -1 O SER A 349 N LEU A 333
SHEET 3 AA3 3 ASP A 371 SER A 373 -1 O PHE A 372 N LEU A 348
SHEET 1 AA4 2 ILE A 487 ARG A 489 0
SHEET 2 AA4 2 LEU A 497 VAL A 499 -1 O THR A 498 N ARG A 488
LINK OG1 THR A 417 MG MG A 802 1555 1555 2.04
LINK O2B ADP A 801 MG MG A 802 1555 1555 2.29
LINK MG MG A 802 O HOH A 901 1555 1555 2.05
LINK MG MG A 802 O HOH A 902 1555 1555 2.06
LINK MG MG A 802 O HOH A 903 1555 1555 2.34
LINK MG MG A 802 O HOH A 904 1555 1555 2.14
SITE 1 AC1 14 ARG A 316 ARG A 318 PRO A 319 LEU A 321
SITE 2 AC1 14 THR A 412 GLY A 413 SER A 414 GLY A 415
SITE 3 AC1 14 LYS A 416 THR A 417 PHE A 418 MG A 802
SITE 4 AC1 14 HOH A 902 HOH A 903
SITE 1 AC2 6 THR A 417 ADP A 801 HOH A 901 HOH A 902
SITE 2 AC2 6 HOH A 903 HOH A 904
CRYST1 63.713 63.713 242.432 90.00 90.00 90.00 P 41 2 2 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 0.015695 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015695 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004125 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
