HEADER MOTOR PROTEIN 16-JAN-12 4DBR
TITLE MYOSIN VI D179Y (MD) PRE-POWERSTROKE STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYOSIN-VI;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MOTOR DOMAIN, UNP RESIDUES 5-788;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SUS SCROFA;
SOURCE 3 ORGANISM_COMMON: PIGS,SWINE,WILD BOAR;
SOURCE 4 ORGANISM_TAXID: 9823;
SOURCE 5 GENE: MYO6;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS MOTOR PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR O.PYLYPENKO,H.L.SWEENEY,A.HOUDUSSE
REVDAT 2 28-FEB-24 4DBR 1 REMARK SEQADV LINK
REVDAT 1 30-JAN-13 4DBR 0
JRNL AUTH L.SONG,O.PYLYPENKO,Z.YANG,A.HOUDUSSE,L.H.SWEENEY
JRNL TITL MUTATIONS IN MYOSIN VI THAT CAUSE A LOSS OF COORDINATION
JRNL TITL 2 BETWEEN HEADS PROVIDE INSIGHTS INTO THE STRUCTURAL CHANGES
JRNL TITL 3 UNDERLYING FORCE GENERATION AND THE IMPORTANCE OF GATING
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.2_869)
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.36
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.990
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 64845
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.216
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3242
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 29.3610 - 4.1975 1.00 6460 341 0.1643 0.1776
REMARK 3 2 4.1975 - 3.3332 1.00 6238 328 0.1537 0.1881
REMARK 3 3 3.3332 - 2.9122 1.00 6193 326 0.1764 0.2313
REMARK 3 4 2.9122 - 2.6462 1.00 6127 323 0.1798 0.2495
REMARK 3 5 2.6462 - 2.4566 1.00 6120 322 0.1779 0.2351
REMARK 3 6 2.4566 - 2.3118 1.00 6108 321 0.1832 0.2503
REMARK 3 7 2.3118 - 2.1961 1.00 6094 320 0.1812 0.2423
REMARK 3 8 2.1961 - 2.1005 1.00 6099 320 0.1979 0.2565
REMARK 3 9 2.1005 - 2.0197 1.00 6071 320 0.2070 0.2712
REMARK 3 10 2.0197 - 1.9500 1.00 6093 321 0.2337 0.2985
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.40
REMARK 3 SHRINKAGE RADIUS : 1.24
REMARK 3 K_SOL : 0.31
REMARK 3 B_SOL : 35.57
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.520
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.360
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 : 0.009 6270
REMARK 3 ANGLE : 1.257 8473
REMARK 3 CHIRALITY : 0.082 930
REMARK 3 PLANARITY : 0.005 1097
REMARK 3 DIHEDRAL : 13.419 2329
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
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 4DBR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1000070131.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-10
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98011
REMARK 200 MONOCHROMATOR : SI III
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 69466
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 29.361
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
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) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.94
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM TRISHCL PH 8, 5.5% PEG8K, 50 MM
REMARK 280 KSCN, 5% GLYCEROL, 20 MM DTT, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
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 45.97000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.21500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.76500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.21500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.97000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.76500
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 SER A 357
REMARK 465 THR A 358
REMARK 465 SER A 359
REMARK 465 GLY A 360
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 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 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 ASP A 27 CG OD1 OD2
REMARK 470 SER A 28 OG
REMARK 470 ASN A 35 CG OD1 ND2
REMARK 470 LYS A 37 CG CD CE NZ
REMARK 470 LYS A 39 CG CD CE NZ
REMARK 470 LYS A 83 NZ
REMARK 470 LYS A 240 CG CD CE NZ
REMARK 470 GLU A 241 OE1 OE2
REMARK 470 GLU A 299 CG CD OE1 OE2
REMARK 470 LYS A 302 CD CE NZ
REMARK 470 GLU A 354 CG CD OE1 OE2
REMARK 470 ILE A 407 CG1 CG2 CD1
REMARK 470 GLU A 446 OE1 OE2
REMARK 470 LEU A 480 CD1 CD2
REMARK 470 LYS A 498 CE NZ
REMARK 470 LYS A 552 CG CD CE NZ
REMARK 470 LYS A 564 CG CD CE NZ
REMARK 470 ASN A 570 CG OD1 ND2
REMARK 470 ARG A 572 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 595 OE1 OE2
REMARK 470 ARG A 613 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 622 CG CD OE1 OE2
REMARK 470 LYS A 782 CG CD CE NZ
REMARK 470 ARG A 783 CD NE CZ NH1 NH2
REMARK 470 ILE A 789 CG1 CG2 CD1
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 35 -28.73 72.33
REMARK 500 GLN A 36 55.88 -92.81
REMARK 500 ALA A 91 -120.49 52.87
REMARK 500 LYS A 105 -13.13 75.05
REMARK 500 ASN A 244 -176.77 -68.21
REMARK 500 SER A 266 -168.35 -161.95
REMARK 500 SER A 467 -162.24 -123.47
REMARK 500 LEU A 522 -49.68 71.73
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 810 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 158 OG1
REMARK 620 2 SER A 204 OG 83.5
REMARK 620 3 ADP A 809 O1B 91.9 173.7
REMARK 620 4 VO4 A 811 O2 164.4 81.1 103.7
REMARK 620 5 HOH A1626 O 88.5 87.6 87.9 92.5
REMARK 620 6 HOH A1627 O 88.5 86.4 97.8 88.9 173.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 VO4 A 811 V
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP A 809 O2B
REMARK 620 2 VO4 A 811 O1 179.6
REMARK 620 3 VO4 A 811 O2 97.9 82.0
REMARK 620 4 VO4 A 811 O3 84.0 95.7 114.6
REMARK 620 5 VO4 A 811 O4 90.5 89.9 123.7 121.6
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 808
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 809
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 810
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VO4 A 811
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2V26 RELATED DB: PDB
REMARK 900 MYOSIN VI (MD) PRE-POWERSTROKE STATE
REMARK 900 RELATED ID: 4DBP RELATED DB: PDB
REMARK 900 RELATED ID: 4DBQ RELATED DB: PDB
DBREF 4DBR A 5 789 UNP F1RQI7 F1RQI7_PIG 5 789
SEQADV 4DBR ALA A 4 UNP F1RQI7 EXPRESSION TAG
SEQADV 4DBR TYR A 179 UNP F1RQI7 ASP 179 ENGINEERED MUTATION
SEQRES 1 A 786 ALA LYS PRO VAL TRP ALA PRO HIS PRO THR ASP GLY PHE
SEQRES 2 A 786 GLN VAL GLY ASN ILE VAL ASP ILE GLY PRO ASP SER LEU
SEQRES 3 A 786 THR ILE GLU PRO LEU ASN GLN LYS GLY LYS THR PHE LEU
SEQRES 4 A 786 ALA LEU ILE ASN GLN VAL PHE PRO ALA GLU GLU ASP SER
SEQRES 5 A 786 LYS LYS ASP VAL GLU ASP ASN CYS SER LEU MET TYR LEU
SEQRES 6 A 786 ASN GLU ALA THR LEU LEU HIS ASN ILE LYS VAL ARG TYR
SEQRES 7 A 786 SER LYS ASP ARG ILE TYR THR TYR VAL ALA ASN ILE LEU
SEQRES 8 A 786 ILE ALA VAL ASN PRO TYR PHE ASP ILE PRO LYS ILE TYR
SEQRES 9 A 786 SER SER GLU THR ILE LYS SER TYR GLN GLY LYS SER LEU
SEQRES 10 A 786 GLY THR MET PRO PRO HIS VAL PHE ALA ILE ALA ASP LYS
SEQRES 11 A 786 ALA PHE ARG ASP MET LYS VAL LEU LYS LEU SER GLN SER
SEQRES 12 A 786 ILE ILE VAL SER GLY GLU SER GLY ALA GLY LYS THR GLU
SEQRES 13 A 786 ASN THR LYS PHE VAL LEU ARG TYR LEU THR GLU SER TYR
SEQRES 14 A 786 GLY THR GLY GLN ASP ILE TYR ASP ARG ILE VAL GLU ALA
SEQRES 15 A 786 ASN PRO LEU LEU GLU ALA PHE GLY ASN ALA LYS THR VAL
SEQRES 16 A 786 ARG ASN ASN ASN SER SER ARG PHE GLY LYS PHE VAL GLU
SEQRES 17 A 786 ILE HIS PHE ASN GLU LYS SER SER VAL VAL GLY GLY PHE
SEQRES 18 A 786 VAL SER HIS TYR LEU LEU GLU LYS SER ARG ILE CYS VAL
SEQRES 19 A 786 GLN GLY LYS GLU GLU ARG ASN TYR HIS ILE PHE TYR ARG
SEQRES 20 A 786 LEU CYS ALA GLY ALA SER GLU ASP ILE ARG GLU ARG LEU
SEQRES 21 A 786 HIS LEU SER SER PRO ASP ASN PHE ARG TYR LEU ASN ARG
SEQRES 22 A 786 GLY CYS THR ARG TYR PHE ALA ASN LYS GLU THR ASP LYS
SEQRES 23 A 786 GLN ILE LEU GLN ASN ARG LYS SER PRO GLU TYR LEU LYS
SEQRES 24 A 786 ALA GLY SER LEU LYS ASP PRO LEU LEU ASP ASP HIS GLY
SEQRES 25 A 786 ASP PHE ILE ARG MET CYS THR ALA MET LYS LYS ILE GLY
SEQRES 26 A 786 LEU ASP ASP GLU GLU LYS LEU ASP LEU PHE ARG VAL VAL
SEQRES 27 A 786 ALA GLY VAL LEU HIS LEU GLY ASN ILE ASP PHE GLU GLU
SEQRES 28 A 786 ALA GLY SER THR SER GLY GLY CYS ASN LEU LYS ASN LYS
SEQRES 29 A 786 SER THR GLN ALA LEU GLU TYR CYS ALA GLU LEU LEU GLY
SEQRES 30 A 786 LEU ASP GLN ASP ASP LEU ARG VAL SER LEU THR THR ARG
SEQRES 31 A 786 VAL MET LEU THR THR ALA GLY GLY ALA LYS GLY THR VAL
SEQRES 32 A 786 ILE LYS VAL PRO LEU LYS VAL GLU GLN ALA ASN ASN ALA
SEQRES 33 A 786 ARG ASP ALA LEU ALA LYS THR VAL TYR SER HIS LEU PHE
SEQRES 34 A 786 ASP HIS VAL VAL ASN ARG VAL ASN GLN CYS PHE PRO PHE
SEQRES 35 A 786 GLU THR SER SER TYR PHE ILE GLY VAL LEU ASP ILE ALA
SEQRES 36 A 786 GLY PHE GLU TYR PHE GLU HIS ASN SER PHE GLU GLN PHE
SEQRES 37 A 786 CYS ILE ASN TYR CYS ASN GLU LYS LEU GLN GLN PHE PHE
SEQRES 38 A 786 ASN GLU ARG ILE LEU LYS GLU GLU GLN GLU LEU TYR GLN
SEQRES 39 A 786 LYS GLU GLY LEU GLY VAL ASN GLU VAL HIS TYR VAL ASP
SEQRES 40 A 786 ASN GLN ASP CYS ILE ASP LEU ILE GLU ALA ARG LEU VAL
SEQRES 41 A 786 GLY ILE LEU ASP ILE LEU ASP GLU GLU ASN ARG LEU PRO
SEQRES 42 A 786 GLN PRO SER ASP GLN HIS PHE THR SER ALA VAL HIS GLN
SEQRES 43 A 786 LYS HIS LYS ASP HIS PHE ARG LEU SER ILE PRO ARG LYS
SEQRES 44 A 786 SER LYS LEU ALA ILE HIS ARG ASN ILE ARG ASP ASP GLU
SEQRES 45 A 786 GLY PHE ILE ILE ARG HIS PHE ALA GLY ALA VAL CYS TYR
SEQRES 46 A 786 GLU THR THR GLN PHE VAL GLU LYS ASN ASN ASP ALA LEU
SEQRES 47 A 786 HIS MET SER LEU GLU SER LEU ILE CYS GLU SER ARG ASP
SEQRES 48 A 786 LYS PHE ILE ARG GLU LEU PHE GLU SER SER THR ASN ASN
SEQRES 49 A 786 ASN LYS ASP THR LYS GLN LYS ALA GLY LYS LEU SER PHE
SEQRES 50 A 786 ILE SER VAL GLY ASN LYS PHE LYS THR GLN LEU ASN LEU
SEQRES 51 A 786 LEU LEU ASP LYS LEU ARG SER THR GLY ALA SER PHE ILE
SEQRES 52 A 786 ARG CYS ILE LYS PRO ASN LEU LYS MET THR SER HIS HIS
SEQRES 53 A 786 PHE GLU GLY ALA GLN ILE LEU SER GLN LEU GLN CYS SER
SEQRES 54 A 786 GLY MET VAL SER VAL LEU ASP LEU MET GLN GLY GLY PHE
SEQRES 55 A 786 PRO SER ARG ALA SER PHE HIS GLU LEU TYR ASN MET TYR
SEQRES 56 A 786 LYS LYS TYR MET PRO ASP LYS LEU ALA ARG LEU ASP PRO
SEQRES 57 A 786 ARG LEU PHE CYS LYS ALA LEU PHE LYS ALA LEU GLY LEU
SEQRES 58 A 786 ASN GLU ILE ASP TYR LYS PHE GLY LEU THR LYS VAL PHE
SEQRES 59 A 786 PHE ARG PRO GLY LYS PHE ALA GLU PHE ASP GLN ILE MET
SEQRES 60 A 786 LYS SER ASP PRO ASP HIS LEU ALA GLU LEU VAL LYS ARG
SEQRES 61 A 786 VAL ASN HIS TRP LEU ILE
HET EDO A 801 4
HET EDO A 802 4
HET EDO A 803 4
HET EDO A 804 4
HET EDO A 805 4
HET EDO A 806 4
HET EDO A 807 4
HET EDO A 808 4
HET ADP A 809 27
HET MG A 810 1
HET VO4 A 811 5
HETNAM EDO 1,2-ETHANEDIOL
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM VO4 VANADATE ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 EDO 8(C2 H6 O2)
FORMUL 10 ADP C10 H15 N5 O10 P2
FORMUL 11 MG MG 2+
FORMUL 12 VO4 O4 V 3-
FORMUL 13 HOH *727(H2 O)
HELIX 1 1 LEU A 44 VAL A 48 5 5
HELIX 2 2 ASP A 61 LEU A 65 5 5
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 ALA A 185 1 10
HELIX 8 8 ALA A 185 GLY A 193 1 9
HELIX 9 9 LYS A 232 CYS A 236 5 5
HELIX 10 10 TYR A 245 ALA A 255 1 11
HELIX 11 11 SER A 256 HIS A 264 1 9
HELIX 12 12 SER A 267 ASN A 270 5 4
HELIX 13 13 PHE A 271 ARG A 276 1 6
HELIX 14 14 ASN A 284 ILE A 291 1 8
HELIX 15 15 LEU A 292 LYS A 296 5 5
HELIX 16 16 SER A 297 GLY A 304 1 8
HELIX 17 17 ASP A 312 GLY A 328 1 17
HELIX 18 18 ASP A 330 ASN A 349 1 20
HELIX 19 19 SER A 368 LEU A 379 1 12
HELIX 20 20 ASP A 382 THR A 391 1 10
HELIX 21 21 LYS A 412 GLN A 441 1 30
HELIX 22 22 SER A 467 LEU A 489 1 23
HELIX 23 23 LYS A 490 GLU A 499 1 10
HELIX 24 24 ASN A 511 ALA A 520 1 10
HELIX 25 25 GLY A 524 ARG A 534 1 11
HELIX 26 26 SER A 539 HIS A 551 1 13
HELIX 27 27 ILE A 559 SER A 563 5 5
HELIX 28 28 LEU A 565 ASN A 570 1 6
HELIX 29 29 ARG A 572 ASP A 574 5 3
HELIX 30 30 GLN A 592 ASN A 597 1 6
HELIX 31 31 HIS A 602 GLU A 611 1 10
HELIX 32 32 ASP A 614 PHE A 621 1 8
HELIX 33 33 SER A 642 SER A 660 1 19
HELIX 34 34 GLU A 681 SER A 692 1 12
HELIX 35 35 GLY A 693 MET A 701 1 9
HELIX 36 36 PHE A 711 LYS A 720 1 10
HELIX 37 37 PRO A 723 LEU A 729 1 7
HELIX 38 38 ASP A 730 LEU A 742 1 13
HELIX 39 39 ASN A 745 ILE A 747 5 3
HELIX 40 40 LYS A 762 LYS A 771 1 10
HELIX 41 41 ASP A 773 LEU A 788 1 16
SHEET 1 A 5 PHE A 41 ALA A 43 0
SHEET 2 A 5 LEU A 29 PRO A 33 -1 N ILE A 31 O PHE A 41
SHEET 3 A 5 GLY A 15 ILE A 24 -1 N VAL A 22 O THR A 30
SHEET 4 A 5 VAL A 7 HIS A 11 -1 N VAL A 7 O GLY A 19
SHEET 5 A 5 PHE A 49 PRO A 50 -1 O PHE A 49 N TRP A 8
SHEET 1 B 7 TYR A 87 VAL A 90 0
SHEET 2 B 7 ILE A 93 VAL A 97 -1 O ILE A 95 N THR A 88
SHEET 3 B 7 GLY A 662 ILE A 669 1 O ARG A 667 N LEU A 94
SHEET 4 B 7 GLN A 145 SER A 150 1 N ILE A 148 O SER A 664
SHEET 5 B 7 TYR A 450 ASP A 456 1 O GLY A 453 N GLN A 145
SHEET 6 B 7 GLY A 207 PHE A 214 -1 N LYS A 208 O ASP A 456
SHEET 7 B 7 VAL A 220 TYR A 228 -1 O PHE A 224 N GLU A 211
SHEET 1 C 2 ASN A 194 ALA A 195 0
SHEET 2 C 2 SER A 203 SER A 204 -1 O SER A 203 N ALA A 195
SHEET 1 D 2 PHE A 352 GLU A 354 0
SHEET 2 D 2 CYS A 362 LEU A 364 -1 O ASN A 363 N GLU A 353
SHEET 1 E 2 THR A 392 ARG A 393 0
SHEET 2 E 2 VAL A 409 PRO A 410 -1 O VAL A 409 N ARG A 393
SHEET 1 F 3 LEU A 557 SER A 558 0
SHEET 2 F 3 GLY A 576 HIS A 581 -1 O ILE A 578 N SER A 558
SHEET 3 F 3 GLY A 584 GLU A 589 -1 O TYR A 588 N PHE A 577
SHEET 1 G 3 SER A 707 SER A 710 0
SHEET 2 G 3 LYS A 755 PHE A 758 -1 O PHE A 758 N SER A 707
SHEET 3 G 3 TYR A 749 PHE A 751 -1 N LYS A 750 O PHE A 757
LINK OG1 THR A 158 MG MG A 810 1555 1555 2.29
LINK OG SER A 204 MG MG A 810 1555 1555 2.33
LINK O1B ADP A 809 MG MG A 810 1555 1555 2.23
LINK O2B ADP A 809 V VO4 A 811 1555 1555 2.16
LINK MG MG A 810 O2 VO4 A 811 1555 1555 2.12
LINK MG MG A 810 O HOH A1626 1555 1555 2.18
LINK MG MG A 810 O HOH A1627 1555 1555 2.18
SITE 1 AC1 7 PHE A 206 GLY A 207 ALA A 458 ILE A 473
SITE 2 AC1 7 CYS A 476 ASN A 477 EDO A 803
SITE 1 AC2 7 ASP A 84 ARG A 85 ILE A 86 TYR A 87
SITE 2 AC2 7 ILE A 106 HOH A1027 HOH A1284
SITE 1 AC3 9 ARG A 205 PHE A 206 TYR A 228 LEU A 229
SITE 2 AC3 9 LEU A 230 GLU A 231 ILE A 473 EDO A 801
SITE 3 AC3 9 HOH A1283
SITE 1 AC4 7 ASN A 92 ILE A 93 GLU A 492 MET A 701
SITE 2 AC4 7 PRO A 706 HOH A1144 HOH A1254
SITE 1 AC5 7 GLU A 152 ARG A 199 TYR A 462 LYS A 670
SITE 2 AC5 7 LEU A 673 HOH A1044 HOH A1557
SITE 1 AC6 4 ASN A 284 ASP A 288 GLY A 304 SER A 305
SITE 1 AC7 4 SER A 226 HIS A 227 GLN A 650 HOH A 960
SITE 1 AC8 5 HIS A 507 TYR A 508 ASP A 510 HOH A 990
SITE 2 AC8 5 HOH A1531
SITE 1 AC9 24 ILE A 86 ASN A 98 PRO A 99 TYR A 100
SITE 2 AC9 24 PHE A 101 ASP A 102 TYR A 107 GLY A 154
SITE 3 AC9 24 ALA A 155 GLY A 156 LYS A 157 THR A 158
SITE 4 AC9 24 GLU A 159 PHE A 163 ASN A 200 LEU A 310
SITE 5 AC9 24 MG A 810 VO4 A 811 HOH A 901 HOH A 934
SITE 6 AC9 24 HOH A1009 HOH A1029 HOH A1045 HOH A1626
SITE 1 BC1 6 THR A 158 SER A 204 ADP A 809 VO4 A 811
SITE 2 BC1 6 HOH A1626 HOH A1627
SITE 1 BC2 12 SER A 153 GLY A 154 LYS A 157 ASN A 200
SITE 2 BC2 12 SER A 203 SER A 204 ALA A 458 GLY A 459
SITE 3 BC2 12 ADP A 809 MG A 810 HOH A 913 HOH A1627
CRYST1 91.940 93.530 102.430 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 0.010877 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010692 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009763 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
