HEADER MOTOR PROTEIN 04-SEP-07 2VAS
TITLE MYOSIN VI (MD-INSERT2-CAM, DELTA-INSERT1) POST-RIGOR STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYOSIN VI;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MOTOR DOMAIN-INSERT2,RESIDUES 2-277,304-377,379-816;
COMPND 5 SYNONYM: UNCONVENTIONAL MYOSIN VI;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: INSERT1 DELETION (C278-A303);
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CALMODULIN;
COMPND 10 CHAIN: B;
COMPND 11 SYNONYM: CAM;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIG;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: SF9;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;
SOURCE 11 ORGANISM_COMMON: FRUIT FLY;
SOURCE 12 ORGANISM_TAXID: 7227;
SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 15 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 16 EXPRESSION_SYSTEM_PLASMID: SF9
KEYWDS CALMODULIN-BINDING, NUCLEOTIDE-BINDING, TRANSPORT, CALMODULIN,
KEYWDS 2 ENDOCYTOSIS, MG.ADP.BEFX, CAM, MYOSIN, NUCLEUS, MEMBRANE, MYOSIN VI,
KEYWDS 3 CYTOPLASM, GOLGI APPARATUS, PHOSPHORYLATION, MOLECULAR MOTOR, ATP-
KEYWDS 4 BINDING, COILED COIL, ACTIN-BINDING, MOTOR PROTEIN, POST-RIGOR
KEYWDS 5 STATE, PROTEIN TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR J.MENETREY,P.LLINAS,J.CICOLARI,G.SQUIRES,X.LIU,A.LI,H.L.SWEENEY,
AUTHOR 2 A.HOUDUSSE
REVDAT 3 13-DEC-23 2VAS 1 REMARK LINK
REVDAT 2 24-FEB-09 2VAS 1 VERSN
REVDAT 1 11-DEC-07 2VAS 0
JRNL AUTH J.MENETREY,P.LLINAS,J.CICOLARI,G.SQUIRES,X.LIU,A.LI,
JRNL AUTH 2 H.L.SWEENEY,A.HOUDUSSE
JRNL TITL THE POST-RIGOR STRUCTURE OF MYOSIN VI AND IMPLICATIONS FOR
JRNL TITL 2 THE RECOVERY STROKE.
JRNL REF EMBO J. V. 27 244 2008
JRNL REFN ISSN 0261-4189
JRNL PMID 18046460
JRNL DOI 10.1038/SJ.EMBOJ.7601937
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.28
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 48522
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) : 0.219
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2628
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3544
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2550
REMARK 3 BIN FREE R VALUE SET COUNT : 185
REMARK 3 BIN FREE R VALUE : 0.3260
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7023
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 154
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.35
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.97000
REMARK 3 B22 (A**2) : -0.89000
REMARK 3 B33 (A**2) : 1.86000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.311
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.238
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.175
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.393
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.919
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.890
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7012 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9452 ; 1.222 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 866 ; 6.554 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 342 ;35.160 ;24.327
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1205 ;16.872 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 41 ;16.770 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1027 ; 0.126 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5328 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2949 ; 0.193 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 4814 ; 0.299 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 244 ; 0.131 ; 0.200
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): 38 ; 0.217 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 10 ; 0.123 ; 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): 4432 ; 0.806 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 6893 ; 1.034 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2887 ; 1.548 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2559 ; 2.471 ; 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 : NULL
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2VAS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-SEP-07.
REMARK 100 THE DEPOSITION ID IS D_1290033681.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 29-JUN-06
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.872600
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51218
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 48.970
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 8.200
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.2000
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) : 2.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.30
REMARK 200 R MERGE FOR SHELL (I) : 0.38000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 6.600
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 2BKH
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% PEG 8000, 50MM GLYCINE PH 9.5, 6%
REMARK 280 MPD
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 36.71000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 87.03500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 50.23500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 87.03500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.71000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 50.23500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 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: PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 5200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 49100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.9 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 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 GLU A 2
REMARK 465 ASP A 3
REMARK 465 ARG A 276
REMARK 465 GLY A 277
REMARK 465 GLY A 304
REMARK 465 SER A 305
REMARK 465 LEU A 306
REMARK 465 LYS A 307
REMARK 465 ASP A 308
REMARK 465 GLU A 353
REMARK 465 GLU A 354
REMARK 465 ALA A 355
REMARK 465 GLY A 356
REMARK 465 SER A 357
REMARK 465 THR A 358
REMARK 465 SER A 359
REMARK 465 GLY A 360
REMARK 465 GLY A 361
REMARK 465 CYS A 362
REMARK 465 ASN A 363
REMARK 465 LEU A 364
REMARK 465 LYS A 365
REMARK 465 ASN A 366
REMARK 465 LYS A 367
REMARK 465 VAL A 394
REMARK 465 MET A 395
REMARK 465 LEU A 396
REMARK 465 THR A 397
REMARK 465 THR A 398
REMARK 465 ALA A 399
REMARK 465 GLY A 400
REMARK 465 GLY A 401
REMARK 465 ALA A 402
REMARK 465 LYS A 403
REMARK 465 GLY A 404
REMARK 465 THR A 405
REMARK 465 VAL A 406
REMARK 465 ILE A 407
REMARK 465 LYS A 408
REMARK 465 VAL A 409
REMARK 465 SER A 623
REMARK 465 SER A 624
REMARK 465 THR A 625
REMARK 465 ASN A 626
REMARK 465 ASN A 627
REMARK 465 ASN A 628
REMARK 465 LYS A 629
REMARK 465 ASP A 630
REMARK 465 THR A 631
REMARK 465 LYS A 632
REMARK 465 GLN A 633
REMARK 465 LYS A 634
REMARK 465 ALA A 635
REMARK 465 GLY A 636
REMARK 465 LYS A 637
REMARK 465 LEU A 638
REMARK 465 MET B 0
REMARK 465 ALA B 1
REMARK 465 ASP B 2
REMARK 465 GLN B 3
REMARK 465 LYS B 75
REMARK 465 MET B 76
REMARK 465 LYS B 77
REMARK 465 LYS B 148
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 B 74 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 78 CG OD1 OD2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLN A 176 CB CG CD OE1 NE2
REMARK 480 LYS A 240 CB CG CD CE NZ
REMARK 480 GLU A 257 CB CG CD OE1 OE2
REMARK 480 GLU A 261 CB CG CD OE1 OE2
REMARK 480 ASP A 269 CB CG OD1 OD2
REMARK 480 LEU A 310 CB CG CD1 CD2
REMARK 480 LYS A 325 CG CD CE NZ
REMARK 480 ASP A 351 CG OD1 OD2
REMARK 480 THR A 369 CB OG1 CG2
REMARK 480 GLN A 370 CG CD OE1 NE2
REMARK 480 ARG A 393 CB CG CD NE CZ NH1 NH2
REMARK 480 LYS A 412 CB CG CD CE NZ
REMARK 480 VAL A 413 CB CG1 CG2
REMARK 480 GLU A 414 CB CG CD OE1 OE2
REMARK 480 LYS A 552 CB CG CD CE NZ
REMARK 480 GLU A 606 CG CD OE1 OE2
REMARK 480 GLU A 611 CB CG CD OE1 OE2
REMARK 480 GLU A 622 CG CD OE1 OE2
REMARK 480 LYS A 740 CD CE NZ
REMARK 480 ASN A 745 CG OD1 ND2
REMARK 480 GLU A 746 CB CG CD OE1 OE2
REMARK 480 GLN A 768 CG CD OE1 NE2
REMARK 480 GLU A 779 CG CD OE1 OE2
REMARK 480 LYS A 782 CD CE NZ
REMARK 480 LYS A 809 CB CG CD CE NZ
REMARK 480 LYS A 811 CB CG CD CE NZ
REMARK 480 TYR A 812 CB CG CD1 CD2 CE1 CE2 CZ
REMARK 480 TYR A 812 OH
REMARK 480 ARG A 813 CB CG CD NE CZ NH1 NH2
REMARK 480 GLU A 815 CB CG CD OE1 OE2
REMARK 480 GLU B 6 CG CD OE1 OE2
REMARK 480 GLU B 7 CB CG CD OE1 OE2
REMARK 480 LYS B 21 CD CE NZ
REMARK 480 LYS B 30 CB CG CD CE NZ
REMARK 480 GLU B 45 CB CG CD OE1 OE2
REMARK 480 LEU B 48 CB CG CD1 CD2
REMARK 480 GLN B 49 CB CG CD OE1 NE2
REMARK 480 ASP B 50 CB CG OD1 OD2
REMARK 480 ASP B 64 CG OD1 OD2
REMARK 480 GLU B 83 CB CG CD OE1 OE2
REMARK 480 LYS B 94 CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASP A 269 CA ASP A 269 CB -0.144
REMARK 500 ASP A 351 CB ASP A 351 CG -0.541
REMARK 500 GLN A 370 CB GLN A 370 CG -0.166
REMARK 500 ARG A 393 CA ARG A 393 CB -0.515
REMARK 500 LYS A 412 CA LYS A 412 CB -0.136
REMARK 500 GLU A 414 CA GLU A 414 CB -0.171
REMARK 500 LYS A 740 CG LYS A 740 CD -0.325
REMARK 500 ASN A 745 CB ASN A 745 CG 0.139
REMARK 500 LYS A 782 CG LYS A 782 CD 0.269
REMARK 500 LYS A 809 CA LYS A 809 CB -0.202
REMARK 500 TYR A 812 CA TYR A 812 CB -0.442
REMARK 500 LYS B 21 CG LYS B 21 CD -0.302
REMARK 500 LEU B 48 CA LEU B 48 CB -0.204
REMARK 500 ASP B 64 CB ASP B 64 CG -0.267
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 PRO A 104 C - N - CA ANGL. DEV. = 11.5 DEGREES
REMARK 500 ILE A 178 CG1 - CB - CG2 ANGL. DEV. = 17.4 DEGREES
REMARK 500 ASP A 351 CA - CB - CG ANGL. DEV. = 21.1 DEGREES
REMARK 500 THR A 369 N - CA - CB ANGL. DEV. = 12.7 DEGREES
REMARK 500 ARG A 393 N - CA - CB ANGL. DEV. = 27.1 DEGREES
REMARK 500 ARG A 393 CA - CB - CG ANGL. DEV. = 18.5 DEGREES
REMARK 500 VAL A 413 N - CA - CB ANGL. DEV. = 15.7 DEGREES
REMARK 500 VAL A 413 CA - CB - CG1 ANGL. DEV. = 11.1 DEGREES
REMARK 500 GLU A 611 CB - CA - C ANGL. DEV. = 17.0 DEGREES
REMARK 500 GLU A 611 N - CA - CB ANGL. DEV. = -16.3 DEGREES
REMARK 500 LYS A 740 CB - CG - CD ANGL. DEV. = 19.9 DEGREES
REMARK 500 LYS A 811 CB - CA - C ANGL. DEV. = 13.0 DEGREES
REMARK 500 LYS A 811 N - CA - CB ANGL. DEV. = -12.4 DEGREES
REMARK 500 TYR A 812 CB - CA - C ANGL. DEV. = -34.2 DEGREES
REMARK 500 TYR A 812 CA - CB - CG ANGL. DEV. = -11.6 DEGREES
REMARK 500 GLU A 815 N - CA - CB ANGL. DEV. = -16.4 DEGREES
REMARK 500 GLU B 7 CB - CA - C ANGL. DEV. = 13.2 DEGREES
REMARK 500 GLU B 7 N - CA - CB ANGL. DEV. = -12.9 DEGREES
REMARK 500 GLU B 45 CB - CA - C ANGL. DEV. = 12.9 DEGREES
REMARK 500 ASP B 50 N - CA - CB ANGL. DEV. = 22.9 DEGREES
REMARK 500 ASP B 64 CA - CB - CG ANGL. DEV. = 21.7 DEGREES
REMARK 500 ASP B 64 CB - CG - OD1 ANGL. DEV. = -9.3 DEGREES
REMARK 500 ASP B 64 CB - CG - OD2 ANGL. DEV. = 10.6 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 ALA A 91 -119.66 55.36
REMARK 500 GLN A 176 -172.53 143.60
REMARK 500 ASP A 177 -31.43 -131.26
REMARK 500 LEU A 310 34.66 -97.55
REMARK 500 LYS A 325 40.31 -88.10
REMARK 500 LYS A 326 -24.02 -145.66
REMARK 500 SER A 467 -160.80 -113.66
REMARK 500 LEU A 522 -48.52 73.27
REMARK 500 GLU A 611 38.88 -91.87
REMARK 500 ASP A 730 77.59 66.19
REMARK 500 THR B 28 -169.17 -125.42
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 GLN A 176 ASP A 177 -99.97
REMARK 500 LEU A 729 ASP A 730 50.38
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 A1000 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 158 OG1
REMARK 620 2 SER A 204 OG 94.4
REMARK 620 3 ADP A 998 O1B 98.1 167.5
REMARK 620 4 BEF A 999 F2 171.9 83.5 84.1
REMARK 620 5 HOH A1001 O 90.7 95.3 84.1 81.8
REMARK 620 6 HOH A1002 O 94.5 88.9 90.6 93.2 173.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 BEF A 999 BE
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP A 998 O2B
REMARK 620 2 BEF A 999 F1 105.8
REMARK 620 3 BEF A 999 F2 103.5 116.9
REMARK 620 4 BEF A 999 F3 93.7 114.9 117.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1148 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 20 OD1
REMARK 620 2 ASP B 22 OD2 72.6
REMARK 620 3 ASP B 24 OD2 71.8 72.8
REMARK 620 4 THR B 26 O 78.6 151.1 97.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1149 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 56 OD2
REMARK 620 2 ASP B 58 OD1 93.0
REMARK 620 3 THR B 62 O 77.7 132.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1150 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 93 OD1
REMARK 620 2 ASP B 95 OD1 78.7
REMARK 620 3 ASN B 97 OD1 89.4 79.2
REMARK 620 4 PHE B 99 O 90.1 160.5 84.9
REMARK 620 5 GLU B 104 OE2 101.4 121.1 158.4 76.5
REMARK 620 6 GLU B 104 OE1 95.5 70.7 147.7 126.9 50.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B1151 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 129 OD2
REMARK 620 2 ASP B 131 OD2 73.7
REMARK 620 3 ASP B 131 OD1 116.4 44.6
REMARK 620 4 ASP B 133 OD2 88.5 86.4 99.4
REMARK 620 5 GLN B 135 O 82.0 149.7 161.0 74.9
REMARK 620 6 GLU B 140 OE2 84.8 77.4 70.6 163.6 118.6
REMARK 620 7 GLU B 140 OE1 115.2 119.2 88.8 148.3 87.3 46.9
REMARK 620 N 1 2 3 4 5 6
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 998
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEF A 999
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A1000
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B1148
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B1149
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B1150
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B1151
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2BKH RELATED DB: PDB
REMARK 900 MYOSIN VI NUCLEOTIDE-FREE (MD) CRYSTAL STRUCTURE
REMARK 900 RELATED ID: 2V26 RELATED DB: PDB
REMARK 900 MYOSIN VI (MD) PRE-POWERSTROKE STATE (MG. ADP.VO4)
REMARK 900 RELATED ID: 2BKI RELATED DB: PDB
REMARK 900 MYOSIN VI NUCLEOTIDE-FREE (LONG.S1) CRYSTAL STRUCTURE.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE AUTHORS STATE THAT THE ORIGINAL SEQUENCE (UNIPROT
REMARK 999 Q29122) OF MYOSIN VI FROM PIG WAS MOST LIKELY
REMARK 999 INCORRECT BECAUSE THE CHANGES THAT ARE IN THEIR CLONE
REMARK 999 (LYS DELETION AND THE 6 MUTATIONS) ARE CONSERVED ACROSS
REMARK 999 THE MYOSIN VI FAMILY.
DBREF 2VAS A 2 277 UNP Q29122 MYO6_PIG 2 277
DBREF 2VAS A 304 377 UNP Q29122 MYO6_PIG 304 377
DBREF 2VAS A 378 815 UNP Q29122 MYO6_PIG 379 816
DBREF 2VAS B 0 148 UNP P62152 CALM_DROME 1 149
SEQADV 2VAS VAL A 547 UNP Q29122 GLY 548 CONFLICT
SEQADV 2VAS ARG A 572 UNP Q29122 ALA 573 CONFLICT
SEQADV 2VAS ASP A 573 UNP Q29122 TYR 574 CONFLICT
SEQADV 2VAS LEU A 714 UNP Q29122 VAL 715 CONFLICT
SEQADV 2VAS TYR A 721 UNP Q29122 SER 722 CONFLICT
SEQADV 2VAS MET A 722 UNP Q29122 LEU 723 CONFLICT
SEQRES 1 A 788 GLU ASP GLY LYS PRO VAL TRP ALA PRO HIS PRO THR ASP
SEQRES 2 A 788 GLY PHE GLN VAL GLY ASN ILE VAL ASP ILE GLY PRO ASP
SEQRES 3 A 788 SER LEU THR ILE GLU PRO LEU ASN GLN LYS GLY LYS THR
SEQRES 4 A 788 PHE LEU ALA LEU ILE ASN GLN VAL PHE PRO ALA GLU GLU
SEQRES 5 A 788 ASP SER LYS LYS ASP VAL GLU ASP ASN CYS SER LEU MET
SEQRES 6 A 788 TYR LEU ASN GLU ALA THR LEU LEU HIS ASN ILE LYS VAL
SEQRES 7 A 788 ARG TYR SER LYS ASP ARG ILE TYR THR TYR VAL ALA ASN
SEQRES 8 A 788 ILE LEU ILE ALA VAL ASN PRO TYR PHE ASP ILE PRO LYS
SEQRES 9 A 788 ILE TYR SER SER GLU THR ILE LYS SER TYR GLN GLY LYS
SEQRES 10 A 788 SER LEU GLY THR MET PRO PRO HIS VAL PHE ALA ILE ALA
SEQRES 11 A 788 ASP LYS ALA PHE ARG ASP MET LYS VAL LEU LYS LEU SER
SEQRES 12 A 788 GLN SER ILE ILE VAL SER GLY GLU SER GLY ALA GLY LYS
SEQRES 13 A 788 THR GLU ASN THR LYS PHE VAL LEU ARG TYR LEU THR GLU
SEQRES 14 A 788 SER TYR GLY THR GLY GLN ASP ILE ASP ASP ARG ILE VAL
SEQRES 15 A 788 GLU ALA ASN PRO LEU LEU GLU ALA PHE GLY ASN ALA LYS
SEQRES 16 A 788 THR VAL ARG ASN ASN ASN SER SER ARG PHE GLY LYS PHE
SEQRES 17 A 788 VAL GLU ILE HIS PHE ASN GLU LYS SER SER VAL VAL GLY
SEQRES 18 A 788 GLY PHE VAL SER HIS TYR LEU LEU GLU LYS SER ARG ILE
SEQRES 19 A 788 CYS VAL GLN GLY LYS GLU GLU ARG ASN TYR HIS ILE PHE
SEQRES 20 A 788 TYR ARG LEU CYS ALA GLY ALA SER GLU ASP ILE ARG GLU
SEQRES 21 A 788 ARG LEU HIS LEU SER SER PRO ASP ASN PHE ARG TYR LEU
SEQRES 22 A 788 ASN ARG GLY GLY SER LEU LYS ASP PRO LEU LEU ASP ASP
SEQRES 23 A 788 HIS GLY ASP PHE ILE ARG MET CYS THR ALA MET LYS LYS
SEQRES 24 A 788 ILE GLY LEU ASP ASP GLU GLU LYS LEU ASP LEU PHE ARG
SEQRES 25 A 788 VAL VAL ALA GLY VAL LEU HIS LEU GLY ASN ILE ASP PHE
SEQRES 26 A 788 GLU GLU ALA GLY SER THR SER GLY GLY CYS ASN LEU LYS
SEQRES 27 A 788 ASN LYS SER THR GLN ALA LEU GLU TYR CYS ALA GLU LEU
SEQRES 28 A 788 LEU GLY LEU ASP GLN ASP ASP LEU ARG VAL SER LEU THR
SEQRES 29 A 788 THR ARG VAL MET LEU THR THR ALA GLY GLY ALA LYS GLY
SEQRES 30 A 788 THR VAL ILE LYS VAL PRO LEU LYS VAL GLU GLN ALA ASN
SEQRES 31 A 788 ASN ALA ARG ASP ALA LEU ALA LYS THR VAL TYR SER HIS
SEQRES 32 A 788 LEU PHE ASP HIS VAL VAL ASN ARG VAL ASN GLN CYS PHE
SEQRES 33 A 788 PRO PHE GLU THR SER SER TYR PHE ILE GLY VAL LEU ASP
SEQRES 34 A 788 ILE ALA GLY PHE GLU TYR PHE GLU HIS ASN SER PHE GLU
SEQRES 35 A 788 GLN PHE CYS ILE ASN TYR CYS ASN GLU LYS LEU GLN GLN
SEQRES 36 A 788 PHE PHE ASN GLU ARG ILE LEU LYS GLU GLU GLN GLU LEU
SEQRES 37 A 788 TYR GLN LYS GLU GLY LEU GLY VAL ASN GLU VAL HIS TYR
SEQRES 38 A 788 VAL ASP ASN GLN ASP CYS ILE ASP LEU ILE GLU ALA ARG
SEQRES 39 A 788 LEU VAL GLY ILE LEU ASP ILE LEU ASP GLU GLU ASN ARG
SEQRES 40 A 788 LEU PRO GLN PRO SER ASP GLN HIS PHE THR SER ALA VAL
SEQRES 41 A 788 HIS GLN LYS HIS LYS ASP HIS PHE ARG LEU SER ILE PRO
SEQRES 42 A 788 ARG LYS SER LYS LEU ALA ILE HIS ARG ASN ILE ARG ASP
SEQRES 43 A 788 ASP GLU GLY PHE ILE ILE ARG HIS PHE ALA GLY ALA VAL
SEQRES 44 A 788 CYS TYR GLU THR THR GLN PHE VAL GLU LYS ASN ASN ASP
SEQRES 45 A 788 ALA LEU HIS MET SER LEU GLU SER LEU ILE CYS GLU SER
SEQRES 46 A 788 ARG ASP LYS PHE ILE ARG GLU LEU PHE GLU SER SER THR
SEQRES 47 A 788 ASN ASN ASN LYS ASP THR LYS GLN LYS ALA GLY LYS LEU
SEQRES 48 A 788 SER PHE ILE SER VAL GLY ASN LYS PHE LYS THR GLN LEU
SEQRES 49 A 788 ASN LEU LEU LEU ASP LYS LEU ARG SER THR GLY ALA SER
SEQRES 50 A 788 PHE ILE ARG CYS ILE LYS PRO ASN LEU LYS MET THR SER
SEQRES 51 A 788 HIS HIS PHE GLU GLY ALA GLN ILE LEU SER GLN LEU GLN
SEQRES 52 A 788 CYS SER GLY MET VAL SER VAL LEU ASP LEU MET GLN GLY
SEQRES 53 A 788 GLY PHE PRO SER ARG ALA SER PHE HIS GLU LEU TYR ASN
SEQRES 54 A 788 MET TYR LYS LYS TYR MET PRO ASP LYS LEU ALA ARG LEU
SEQRES 55 A 788 ASP PRO ARG LEU PHE CYS LYS ALA LEU PHE LYS ALA LEU
SEQRES 56 A 788 GLY LEU ASN GLU ILE ASP TYR LYS PHE GLY LEU THR LYS
SEQRES 57 A 788 VAL PHE PHE ARG PRO GLY LYS PHE ALA GLU PHE ASP GLN
SEQRES 58 A 788 ILE MET LYS SER ASP PRO ASP HIS LEU ALA GLU LEU VAL
SEQRES 59 A 788 LYS ARG VAL ASN HIS TRP LEU ILE CYS SER ARG TRP LYS
SEQRES 60 A 788 LYS VAL GLN TRP CYS SER LEU SER VAL ILE LYS LEU LYS
SEQRES 61 A 788 ASN LYS ILE LYS TYR ARG ALA GLU
SEQRES 1 B 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 B 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 B 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 B 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 B 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 B 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 B 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 B 149 VAL PHE ASP LYS ASP GLY ASN GLY PHE ILE SER ALA ALA
SEQRES 9 B 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 B 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 B 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 B 149 THR MET MET THR SER LYS
HET ADP A 998 27
HET BEF A 999 4
HET MG A1000 1
HET CA B1148 1
HET CA B1149 1
HET CA B1150 1
HET CA B1151 1
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM BEF BERYLLIUM TRIFLUORIDE ION
HETNAM MG MAGNESIUM ION
HETNAM CA CALCIUM ION
FORMUL 3 ADP C10 H15 N5 O10 P2
FORMUL 4 BEF BE F3 1-
FORMUL 5 MG MG 2+
FORMUL 6 CA 4(CA 2+)
FORMUL 10 HOH *154(H2 O)
HELIX 1 1 ASN A 46 VAL A 48 5 3
HELIX 2 2 ASN A 62 LEU A 65 5 4
HELIX 3 3 ASN A 69 LYS A 83 1 15
HELIX 4 4 SER A 108 GLN A 116 1 9
HELIX 5 5 HIS A 126 LYS A 142 1 17
HELIX 6 6 GLY A 156 GLY A 173 1 18
HELIX 7 7 GLN A 176 GLY A 193 1 18
HELIX 8 8 LYS A 232 CYS A 236 5 5
HELIX 9 9 TYR A 245 ALA A 255 1 11
HELIX 10 10 SER A 256 HIS A 264 1 9
HELIX 11 11 SER A 267 PHE A 271 5 5
HELIX 12 12 ASP A 312 LYS A 325 1 14
HELIX 13 13 ASP A 330 ASN A 349 1 20
HELIX 14 14 SER A 368 LEU A 379 1 12
HELIX 15 15 ASP A 382 LEU A 390 1 9
HELIX 16 16 LYS A 412 GLN A 441 1 30
HELIX 17 17 SER A 467 GLY A 500 1 34
HELIX 18 18 ASN A 511 ALA A 520 1 10
HELIX 19 19 GLY A 524 ARG A 534 1 11
HELIX 20 20 SER A 539 HIS A 551 1 13
HELIX 21 21 ILE A 559 SER A 563 5 5
HELIX 22 22 LEU A 565 ASN A 570 1 6
HELIX 23 23 ARG A 572 ASP A 574 5 3
HELIX 24 24 GLN A 592 ASN A 597 1 6
HELIX 25 25 HIS A 602 GLU A 611 1 10
HELIX 26 26 ASP A 614 LEU A 620 1 7
HELIX 27 27 SER A 642 SER A 660 1 19
HELIX 28 28 GLU A 681 SER A 692 1 12
HELIX 29 29 GLY A 693 LEU A 700 1 8
HELIX 30 30 PHE A 711 LYS A 719 1 9
HELIX 31 31 LYS A 720 MET A 722 5 3
HELIX 32 32 PRO A 723 ARG A 728 1 6
HELIX 33 33 ASP A 730 LEU A 742 1 13
HELIX 34 34 GLY A 761 LYS A 771 1 11
HELIX 35 35 ASP A 773 ARG A 783 1 11
HELIX 36 36 VAL A 784 GLU A 815 1 32
HELIX 37 37 THR B 5 ASP B 20 1 16
HELIX 38 38 THR B 28 SER B 38 1 11
HELIX 39 39 THR B 44 ASN B 53 1 10
HELIX 40 40 GLU B 54 ASP B 56 5 3
HELIX 41 41 ASP B 64 MET B 71 1 8
HELIX 42 42 THR B 79 ASP B 93 1 15
HELIX 43 43 SER B 101 LEU B 112 1 12
HELIX 44 44 THR B 117 ASP B 129 1 13
HELIX 45 45 ASN B 137 THR B 146 1 10
SHEET 1 AA 5 PHE A 41 LEU A 44 0
SHEET 2 AA 5 SER A 28 PRO A 33 -1 O LEU A 29 N ALA A 43
SHEET 3 AA 5 GLY A 15 ILE A 24 -1 O ASN A 20 N GLU A 32
SHEET 4 AA 5 VAL A 7 HIS A 11 -1 O VAL A 7 N GLY A 19
SHEET 5 AA 5 PHE A 49 PRO A 50 -1 O PHE A 49 N TRP A 8
SHEET 1 AB 7 TYR A 87 VAL A 90 0
SHEET 2 AB 7 ILE A 93 VAL A 97 -1 O ILE A 93 N VAL A 90
SHEET 3 AB 7 GLY A 662 ILE A 669 1 O PHE A 665 N LEU A 94
SHEET 4 AB 7 GLN A 145 SER A 150 1 O SER A 146 N SER A 664
SHEET 5 AB 7 TYR A 450 ASP A 456 1 O PHE A 451 N GLN A 145
SHEET 6 AB 7 GLY A 207 PHE A 214 -1 O LYS A 208 N ASP A 456
SHEET 7 AB 7 VAL A 220 TYR A 228 -1 N VAL A 221 O HIS A 213
SHEET 1 AC 2 ASN A 194 ALA A 195 0
SHEET 2 AC 2 SER A 203 SER A 204 -1 O SER A 203 N ALA A 195
SHEET 1 AD 3 LEU A 557 SER A 558 0
SHEET 2 AD 3 GLY A 576 HIS A 581 -1 O ILE A 578 N SER A 558
SHEET 3 AD 3 GLY A 584 GLU A 589 -1 O GLY A 584 N HIS A 581
SHEET 1 AE 3 SER A 707 SER A 710 0
SHEET 2 AE 3 LYS A 755 PHE A 758 -1 O VAL A 756 N ALA A 709
SHEET 3 AE 3 TYR A 749 PHE A 751 -1 O LYS A 750 N PHE A 757
LINK OG1 THR A 158 MG MG A1000 1555 1555 2.00
LINK OG SER A 204 MG MG A1000 1555 1555 2.10
LINK O2B ADP A 998 BE BEF A 999 1555 1555 1.77
LINK O1B ADP A 998 MG MG A1000 1555 1555 2.14
LINK F2 BEF A 999 MG MG A1000 1555 1555 1.84
LINK MG MG A1000 O HOH A1001 1555 1555 2.23
LINK MG MG A1000 O HOH A1002 1555 1555 2.06
LINK OD1 ASP B 20 CA CA B1148 1555 1555 2.44
LINK OD2 ASP B 22 CA CA B1148 1555 1555 2.60
LINK OD2 ASP B 24 CA CA B1148 1555 1555 2.61
LINK O THR B 26 CA CA B1148 1555 1555 2.33
LINK OD2 ASP B 56 CA CA B1149 1555 1555 2.42
LINK OD1 ASP B 58 CA CA B1149 1555 1555 2.94
LINK O THR B 62 CA CA B1149 1555 1555 2.78
LINK OD1 ASP B 93 CA CA B1150 1555 1555 2.26
LINK OD1 ASP B 95 CA CA B1150 1555 1555 2.47
LINK OD1 ASN B 97 CA CA B1150 1555 1555 2.44
LINK O PHE B 99 CA CA B1150 1555 1555 2.34
LINK OE2 GLU B 104 CA CA B1150 1555 1555 2.62
LINK OE1 GLU B 104 CA CA B1150 1555 1555 2.48
LINK OD2 ASP B 129 CA CA B1151 1555 1555 2.32
LINK OD2 ASP B 131 CA CA B1151 1555 1555 2.33
LINK OD1 ASP B 131 CA CA B1151 1555 1555 3.11
LINK OD2 ASP B 133 CA CA B1151 1555 1555 2.60
LINK O GLN B 135 CA CA B1151 1555 1555 2.29
LINK OE2 GLU B 140 CA CA B1151 1555 1555 2.76
LINK OE1 GLU B 140 CA CA B1151 1555 1555 2.77
CISPEP 1 GLY A 175 GLN A 176 0 -28.58
SITE 1 AC1 20 ASN A 98 TYR A 100 PHE A 101 TYR A 107
SITE 2 AC1 20 GLU A 152 GLY A 154 ALA A 155 GLY A 156
SITE 3 AC1 20 LYS A 157 THR A 158 GLU A 159 PHE A 163
SITE 4 AC1 20 ASN A 200 BEF A 999 MG A1000 HOH A1001
SITE 5 AC1 20 HOH A1002 HOH A2047 HOH A2048 HOH A2145
SITE 1 AC2 10 SER A 153 GLY A 154 LYS A 157 ASN A 200
SITE 2 AC2 10 SER A 203 SER A 204 ADP A 998 MG A1000
SITE 3 AC2 10 HOH A1001 HOH A1002
SITE 1 AC3 6 THR A 158 SER A 204 ADP A 998 BEF A 999
SITE 2 AC3 6 HOH A1001 HOH A1002
SITE 1 AC4 4 ASP B 20 ASP B 22 ASP B 24 THR B 26
SITE 1 AC5 4 ASP B 56 ASP B 58 ASN B 60 THR B 62
SITE 1 AC6 5 ASP B 93 ASP B 95 ASN B 97 PHE B 99
SITE 2 AC6 5 GLU B 104
SITE 1 AC7 5 ASP B 129 ASP B 131 ASP B 133 GLN B 135
SITE 2 AC7 5 GLU B 140
CRYST1 73.420 100.470 174.070 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013620 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009953 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005745 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
