HEADER HYDROLASE 02-MAR-17 5NBT
TITLE APO STRUCTURE OF P60N/P80C KATANIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: KATANIN P80 WD40 REPEAT-CONTAINING SUBUNIT B1;
COMPND 3 CHAIN: A, C;
COMPND 4 SYNONYM: KATANIN P80 SUBUNIT B1,P80 KATANIN;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: KATANIN P60 ATPASE-CONTAINING SUBUNIT A1;
COMPND 8 CHAIN: B, D;
COMPND 9 SYNONYM: KATANIN P60 SUBUNIT A1,LIPOTRANSIN,P60 KATANIN;
COMPND 10 EC: 3.6.4.3;
COMPND 11 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: KATNB1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 10 ORGANISM_COMMON: MOUSE;
SOURCE 11 ORGANISM_TAXID: 10090;
SOURCE 12 GENE: KATNA1;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS KATANIN, SEVERING ENZYME, MICROTUBULE, CYTOSKELETON, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.JIANG,L.REZABKOVA,S.HUA,Q.LIU,G.CAPITANI,A.F.M.ALTELAAR,A.J.R.HECK,
AUTHOR 2 R.A.KAMMERER,M.O.STEINMETZ,A.AKHMANOVA
REVDAT 3 10-MAY-17 5NBT 1 JRNL
REVDAT 2 03-MAY-17 5NBT 1 JRNL
REVDAT 1 26-APR-17 5NBT 0
JRNL AUTH K.JIANG,L.REZABKOVA,S.HUA,Q.LIU,G.CAPITANI,
JRNL AUTH 2 A.F.MAARTEN ALTELAAR,A.J.R.HECK,R.A.KAMMERER,M.O.STEINMETZ,
JRNL AUTH 3 A.AKHMANOVA
JRNL TITL MICROTUBULE MINUS-END REGULATION AT SPINDLE POLES BY AN
JRNL TITL 2 ASPM-KATANIN COMPLEX.
JRNL REF NAT. CELL BIOL. V. 19 480 2017
JRNL REFN ISSN 1476-4679
JRNL PMID 28436967
JRNL DOI 10.1038/NCB3511
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???)
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.26
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 22494
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.247
REMARK 3 R VALUE (WORKING SET) : 0.245
REMARK 3 FREE R VALUE : 0.294
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1126
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 43.2689 - 4.7982 1.00 2793 148 0.2470 0.3100
REMARK 3 2 4.7982 - 3.8092 1.00 2698 142 0.2034 0.2400
REMARK 3 3 3.8092 - 3.3279 1.00 2677 140 0.2192 0.2474
REMARK 3 4 3.3279 - 3.0237 1.00 2657 141 0.2647 0.3179
REMARK 3 5 3.0237 - 2.8070 1.00 2651 139 0.2775 0.3508
REMARK 3 6 2.8070 - 2.6416 1.00 2640 139 0.2917 0.3431
REMARK 3 7 2.6416 - 2.5093 1.00 2609 138 0.2986 0.3653
REMARK 3 8 2.5093 - 2.4001 0.99 2643 139 0.3250 0.3897
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) : 0.410
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.070
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.003 3499
REMARK 3 ANGLE : 0.582 4709
REMARK 3 CHIRALITY : 0.034 569
REMARK 3 PLANARITY : 0.003 572
REMARK 3 DIHEDRAL : 13.852 2147
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 68.5247 16.3926 25.4615
REMARK 3 T TENSOR
REMARK 3 T11: 0.3813 T22: 0.2510
REMARK 3 T33: 0.3225 T12: -0.0022
REMARK 3 T13: -0.0049 T23: 0.0417
REMARK 3 L TENSOR
REMARK 3 L11: 0.9433 L22: 0.6171
REMARK 3 L33: 1.8788 L12: -0.0490
REMARK 3 L13: 0.0982 L23: 0.3845
REMARK 3 S TENSOR
REMARK 3 S11: -0.0096 S12: 0.0179 S13: 0.0415
REMARK 3 S21: -0.0123 S22: 0.1079 S23: -0.0056
REMARK 3 S31: 0.0225 S32: 0.0876 S33: -0.1181
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5NBT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1200003850.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-OCT-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000020
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M-F
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22520
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 43.262
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : 0.16500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.60
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.00
REMARK 200 R MERGE FOR SHELL (I) : 1.40400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.460
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.05
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 27% PEG 3350, 0.1 M BISTRIS PROPANE
REMARK 280 (6.0), 0.2 M MGCL2, PH 6.0, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 73.07000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 18.88000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 73.07000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 18.88000
REMARK 290 SMTRY3 4 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 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 447
REMARK 465 GLY A 448
REMARK 465 SER A 449
REMARK 465 SER A 450
REMARK 465 HIS A 451
REMARK 465 HIS A 452
REMARK 465 HIS A 453
REMARK 465 HIS A 454
REMARK 465 HIS A 455
REMARK 465 HIS A 456
REMARK 465 SER A 457
REMARK 465 SER A 458
REMARK 465 GLY A 459
REMARK 465 LEU A 460
REMARK 465 VAL A 461
REMARK 465 PRO A 462
REMARK 465 ARG A 463
REMARK 465 GLY A 464
REMARK 465 SER A 465
REMARK 465 HIS A 466
REMARK 465 MET A 467
REMARK 465 ALA A 468
REMARK 465 SER A 469
REMARK 465 MET A 470
REMARK 465 THR A 471
REMARK 465 GLY A 472
REMARK 465 GLY A 473
REMARK 465 GLN A 474
REMARK 465 GLN A 475
REMARK 465 MET A 476
REMARK 465 GLY A 477
REMARK 465 ARG A 478
REMARK 465 GLY A 479
REMARK 465 SER A 480
REMARK 465 GLN A 481
REMARK 465 GLN A 482
REMARK 465 ALA A 483
REMARK 465 GLU A 484
REMARK 465 LEU A 485
REMARK 465 VAL A 486
REMARK 465 LEU A 600
REMARK 465 ALA A 601
REMARK 465 ALA A 602
REMARK 465 PRO A 603
REMARK 465 PRO A 604
REMARK 465 SER A 605
REMARK 465 VAL A 606
REMARK 465 GLY A 607
REMARK 465 VAL A 608
REMARK 465 ASP A 609
REMARK 465 ILE A 610
REMARK 465 SER A 611
REMARK 465 ARG A 612
REMARK 465 GLU A 613
REMARK 465 GLU A 614
REMARK 465 LYS A 636
REMARK 465 SER A 637
REMARK 465 GLY A 638
REMARK 465 LEU A 639
REMARK 465 SER A 640
REMARK 465 GLY A 641
REMARK 465 ARG A 642
REMARK 465 HIS A 643
REMARK 465 GLY A 644
REMARK 465 LEU A 657
REMARK 465 ASP A 658
REMARK 465 MET B -1
REMARK 465 GLY B 0
REMARK 465 MET B 1
REMARK 465 ASN B 37
REMARK 465 LYS B 38
REMARK 465 TYR B 39
REMARK 465 PRO B 40
REMARK 465 TYR B 41
REMARK 465 SER B 42
REMARK 465 VAL B 43
REMARK 465 LYS B 44
REMARK 465 ASP B 45
REMARK 465 THR B 46
REMARK 465 HIS B 47
REMARK 465 LEU B 48
REMARK 465 MET C 447
REMARK 465 GLY C 448
REMARK 465 SER C 449
REMARK 465 SER C 450
REMARK 465 HIS C 451
REMARK 465 HIS C 452
REMARK 465 HIS C 453
REMARK 465 HIS C 454
REMARK 465 HIS C 455
REMARK 465 HIS C 456
REMARK 465 SER C 457
REMARK 465 SER C 458
REMARK 465 GLY C 459
REMARK 465 LEU C 460
REMARK 465 VAL C 461
REMARK 465 PRO C 462
REMARK 465 ARG C 463
REMARK 465 GLY C 464
REMARK 465 SER C 465
REMARK 465 HIS C 466
REMARK 465 MET C 467
REMARK 465 ALA C 468
REMARK 465 SER C 469
REMARK 465 MET C 470
REMARK 465 THR C 471
REMARK 465 GLY C 472
REMARK 465 GLY C 473
REMARK 465 GLN C 474
REMARK 465 GLN C 475
REMARK 465 MET C 476
REMARK 465 GLY C 477
REMARK 465 ARG C 478
REMARK 465 GLY C 479
REMARK 465 SER C 480
REMARK 465 GLN C 481
REMARK 465 GLN C 482
REMARK 465 ALA C 483
REMARK 465 GLU C 484
REMARK 465 LEU C 485
REMARK 465 VAL C 486
REMARK 465 ASP C 487
REMARK 465 GLU C 488
REMARK 465 ALA C 601
REMARK 465 ALA C 602
REMARK 465 PRO C 603
REMARK 465 PRO C 604
REMARK 465 SER C 605
REMARK 465 VAL C 606
REMARK 465 GLY C 607
REMARK 465 VAL C 608
REMARK 465 ASP C 609
REMARK 465 LYS C 636
REMARK 465 SER C 637
REMARK 465 GLY C 638
REMARK 465 LEU C 639
REMARK 465 SER C 640
REMARK 465 GLY C 641
REMARK 465 ARG C 642
REMARK 465 HIS C 643
REMARK 465 LEU C 657
REMARK 465 ASP C 658
REMARK 465 MET D -1
REMARK 465 GLY D 0
REMARK 465 MET D 1
REMARK 465 ASN D 37
REMARK 465 LYS D 38
REMARK 465 TYR D 39
REMARK 465 PRO D 40
REMARK 465 TYR D 41
REMARK 465 SER D 42
REMARK 465 VAL D 43
REMARK 465 LYS D 44
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 ILE C 610 CG1 CG2 CD1
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 O LYS C 496 O HOH C 701 2.17
REMARK 500 OG1 THR C 580 O HOH C 702 2.19
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 LEU A 595 -53.61 81.03
REMARK 500 LEU C 595 -54.37 81.10
REMARK 500 SER C 611 -30.10 62.58
REMARK 500 GLN D 4 -46.37 70.73
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 724 DISTANCE = 7.08 ANGSTROMS
REMARK 525 HOH B 108 DISTANCE = 6.63 ANGSTROMS
DBREF 5NBT A 481 658 UNP Q8BG40 KTNB1_MOUSE 481 658
DBREF 5NBT B 1 78 UNP Q9WV86 KTNA1_MOUSE 1 78
DBREF 5NBT C 481 658 UNP Q8BG40 KTNB1_MOUSE 481 658
DBREF 5NBT D 1 78 UNP Q9WV86 KTNA1_MOUSE 1 78
SEQADV 5NBT MET A 447 UNP Q8BG40 INITIATING METHIONINE
SEQADV 5NBT GLY A 448 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT SER A 449 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT SER A 450 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT HIS A 451 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT HIS A 452 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT HIS A 453 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT HIS A 454 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT HIS A 455 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT HIS A 456 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT SER A 457 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT SER A 458 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT GLY A 459 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT LEU A 460 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT VAL A 461 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT PRO A 462 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT ARG A 463 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT GLY A 464 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT SER A 465 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT HIS A 466 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT MET A 467 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT ALA A 468 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT SER A 469 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT MET A 470 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT THR A 471 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT GLY A 472 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT GLY A 473 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT GLN A 474 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT GLN A 475 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT MET A 476 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT GLY A 477 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT ARG A 478 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT GLY A 479 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT SER A 480 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT MET B -1 UNP Q9WV86 INITIATING METHIONINE
SEQADV 5NBT GLY B 0 UNP Q9WV86 EXPRESSION TAG
SEQADV 5NBT PRO B 40 UNP Q9WV86 LEU 40 CONFLICT
SEQADV 5NBT MET C 447 UNP Q8BG40 INITIATING METHIONINE
SEQADV 5NBT GLY C 448 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT SER C 449 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT SER C 450 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT HIS C 451 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT HIS C 452 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT HIS C 453 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT HIS C 454 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT HIS C 455 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT HIS C 456 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT SER C 457 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT SER C 458 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT GLY C 459 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT LEU C 460 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT VAL C 461 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT PRO C 462 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT ARG C 463 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT GLY C 464 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT SER C 465 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT HIS C 466 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT MET C 467 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT ALA C 468 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT SER C 469 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT MET C 470 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT THR C 471 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT GLY C 472 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT GLY C 473 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT GLN C 474 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT GLN C 475 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT MET C 476 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT GLY C 477 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT ARG C 478 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT GLY C 479 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT SER C 480 UNP Q8BG40 EXPRESSION TAG
SEQADV 5NBT MET D -1 UNP Q9WV86 INITIATING METHIONINE
SEQADV 5NBT GLY D 0 UNP Q9WV86 EXPRESSION TAG
SEQADV 5NBT PRO D 40 UNP Q9WV86 LEU 40 CONFLICT
SEQRES 1 A 212 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 212 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 A 212 GLY GLN GLN MET GLY ARG GLY SER GLN GLN ALA GLU LEU
SEQRES 4 A 212 VAL ASP GLU ASP ALA MET SER GLN ILE ARG LYS GLY HIS
SEQRES 5 A 212 ASP THR MET PHE VAL VAL LEU THR SER ARG HIS LYS ASN
SEQRES 6 A 212 LEU ASP THR VAL ARG ALA VAL TRP THR THR GLY ASP ILE
SEQRES 7 A 212 LYS THR SER VAL ASP SER ALA VAL ALA ILE ASN ASP LEU
SEQRES 8 A 212 SER VAL VAL VAL ASP LEU LEU ASN ILE VAL ASN GLN LYS
SEQRES 9 A 212 ALA SER LEU TRP LYS LEU ASP LEU CYS THR THR VAL LEU
SEQRES 10 A 212 PRO GLN ILE GLU LYS LEU LEU GLN SER LYS TYR GLU SER
SEQRES 11 A 212 TYR VAL GLN THR GLY CYS THR SER LEU LYS LEU ILE LEU
SEQRES 12 A 212 GLN ARG PHE LEU PRO LEU ILE THR ASP ILE LEU ALA ALA
SEQRES 13 A 212 PRO PRO SER VAL GLY VAL ASP ILE SER ARG GLU GLU ARG
SEQRES 14 A 212 LEU HIS LYS CYS ARG LEU CYS PHE LYS GLN LEU LYS SER
SEQRES 15 A 212 ILE SER GLY LEU VAL LYS SER LYS SER GLY LEU SER GLY
SEQRES 16 A 212 ARG HIS GLY SER ALA PHE ARG GLU LEU HIS LEU LEU MET
SEQRES 17 A 212 ALA SER LEU ASP
SEQRES 1 B 80 MET GLY MET SER LEU GLN MET ILE VAL GLU ASN VAL LYS
SEQRES 2 B 80 LEU ALA ARG GLU TYR ALA LEU LEU GLY ASN TYR ASP SER
SEQRES 3 B 80 ALA MET VAL TYR TYR GLN GLY VAL LEU ASP GLN MET ASN
SEQRES 4 B 80 LYS TYR PRO TYR SER VAL LYS ASP THR HIS LEU ARG GLN
SEQRES 5 B 80 LYS TRP GLN GLN VAL TRP GLN GLU ILE ASN VAL GLU ALA
SEQRES 6 B 80 LYS GLN VAL LYS ASP ILE MET LYS THR LEU GLU SER PHE
SEQRES 7 B 80 LYS LEU
SEQRES 1 C 212 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 212 LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY
SEQRES 3 C 212 GLY GLN GLN MET GLY ARG GLY SER GLN GLN ALA GLU LEU
SEQRES 4 C 212 VAL ASP GLU ASP ALA MET SER GLN ILE ARG LYS GLY HIS
SEQRES 5 C 212 ASP THR MET PHE VAL VAL LEU THR SER ARG HIS LYS ASN
SEQRES 6 C 212 LEU ASP THR VAL ARG ALA VAL TRP THR THR GLY ASP ILE
SEQRES 7 C 212 LYS THR SER VAL ASP SER ALA VAL ALA ILE ASN ASP LEU
SEQRES 8 C 212 SER VAL VAL VAL ASP LEU LEU ASN ILE VAL ASN GLN LYS
SEQRES 9 C 212 ALA SER LEU TRP LYS LEU ASP LEU CYS THR THR VAL LEU
SEQRES 10 C 212 PRO GLN ILE GLU LYS LEU LEU GLN SER LYS TYR GLU SER
SEQRES 11 C 212 TYR VAL GLN THR GLY CYS THR SER LEU LYS LEU ILE LEU
SEQRES 12 C 212 GLN ARG PHE LEU PRO LEU ILE THR ASP ILE LEU ALA ALA
SEQRES 13 C 212 PRO PRO SER VAL GLY VAL ASP ILE SER ARG GLU GLU ARG
SEQRES 14 C 212 LEU HIS LYS CYS ARG LEU CYS PHE LYS GLN LEU LYS SER
SEQRES 15 C 212 ILE SER GLY LEU VAL LYS SER LYS SER GLY LEU SER GLY
SEQRES 16 C 212 ARG HIS GLY SER ALA PHE ARG GLU LEU HIS LEU LEU MET
SEQRES 17 C 212 ALA SER LEU ASP
SEQRES 1 D 80 MET GLY MET SER LEU GLN MET ILE VAL GLU ASN VAL LYS
SEQRES 2 D 80 LEU ALA ARG GLU TYR ALA LEU LEU GLY ASN TYR ASP SER
SEQRES 3 D 80 ALA MET VAL TYR TYR GLN GLY VAL LEU ASP GLN MET ASN
SEQRES 4 D 80 LYS TYR PRO TYR SER VAL LYS ASP THR HIS LEU ARG GLN
SEQRES 5 D 80 LYS TRP GLN GLN VAL TRP GLN GLU ILE ASN VAL GLU ALA
SEQRES 6 D 80 LYS GLN VAL LYS ASP ILE MET LYS THR LEU GLU SER PHE
SEQRES 7 D 80 LYS LEU
FORMUL 5 HOH *74(H2 O)
HELIX 1 AA1 ASP A 487 GLY A 497 1 11
HELIX 2 AA2 GLY A 497 THR A 520 1 24
HELIX 3 AA3 ASP A 523 ASN A 535 1 13
HELIX 4 AA4 ASP A 536 ASN A 548 1 13
HELIX 5 AA5 GLN A 549 TRP A 554 5 6
HELIX 6 AA6 LYS A 555 GLN A 571 1 17
HELIX 7 AA7 TYR A 574 THR A 597 1 24
HELIX 8 AA8 LEU A 616 SER A 635 1 20
HELIX 9 AA9 ALA A 646 MET A 654 1 9
HELIX 10 AB1 LEU B 3 GLY B 20 1 18
HELIX 11 AB2 ASN B 21 MET B 36 1 16
HELIX 12 AB3 GLN B 50 SER B 75 1 26
HELIX 13 AB4 ALA C 490 LYS C 496 1 7
HELIX 14 AB5 GLY C 497 THR C 520 1 24
HELIX 15 AB6 ASP C 523 ASN C 535 1 13
HELIX 16 AB7 ASP C 536 ASN C 548 1 13
HELIX 17 AB8 GLN C 549 TRP C 554 5 6
HELIX 18 AB9 LYS C 555 GLN C 571 1 17
HELIX 19 AC1 TYR C 574 LEU C 600 1 27
HELIX 20 AC2 ARG C 612 SER C 635 1 24
HELIX 21 AC3 SER C 645 MET C 654 1 10
HELIX 22 AC4 GLN D 4 GLY D 20 1 17
HELIX 23 AC5 ASN D 21 MET D 36 1 16
HELIX 24 AC6 THR D 46 LEU D 48 5 3
HELIX 25 AC7 ARG D 49 SER D 75 1 27
CRYST1 146.140 37.760 103.090 90.00 93.37 90.00 C 1 2 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 0.006843 0.000000 0.000403 0.00000
SCALE2 0.000000 0.026483 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009717 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
