HEADER MOTOR PROTEIN 19-MAR-12 4E7Z
TITLE MYOSIN VI (MD) PRE-POWERSTROKE STATE, P21 CRYSTAL FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYOSIN-VI;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: 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: UNIDENTIFIED BACULOVIRUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10469;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9 CELL
KEYWDS MYOSIN, MOLECULAR MOTOR, MOTOR PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR T.ISABET,H.L.SWEENEY,A.HOUDUSSE
REVDAT 3 28-FEB-24 4E7Z 1 REMARK SEQADV LINK
REVDAT 2 31-OCT-12 4E7Z 1 JRNL
REVDAT 1 19-SEP-12 4E7Z 0
JRNL AUTH J.MENETREY,T.ISABET,V.ROPARS,M.MUKHERJEA,O.PYLYPENKO,X.LIU,
JRNL AUTH 2 J.PEREZ,P.VACHETTE,H.L.SWEENEY,A.M.HOUDUSSE
JRNL TITL PROCESSIVE STEPS IN THE REVERSE DIRECTION REQUIRE UNCOUPLING
JRNL TITL 2 OF THE LEAD HEAD LEVER ARM OF MYOSIN VI.
JRNL REF MOL.CELL V. 48 75 2012
JRNL REFN ISSN 1097-2765
JRNL PMID 22940248
JRNL DOI 10.1016/J.MOLCEL.2012.07.034
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.4_486)
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.65
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 2.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 3 NUMBER OF REFLECTIONS : 80414
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.231
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 4027
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 29.6550 - 4.9483 0.99 7846 410 0.1581 0.1964
REMARK 3 2 4.9483 - 3.9305 0.98 7629 405 0.1414 0.1766
REMARK 3 3 3.9305 - 3.4345 0.98 7635 404 0.1761 0.2399
REMARK 3 4 3.4345 - 3.1209 0.98 7613 401 0.1926 0.2531
REMARK 3 5 3.1209 - 2.8974 0.99 7628 403 0.1986 0.2794
REMARK 3 6 2.8974 - 2.7267 0.98 7627 402 0.1993 0.2653
REMARK 3 7 2.7267 - 2.5902 0.99 7599 401 0.1998 0.2705
REMARK 3 8 2.5902 - 2.4775 0.98 7637 402 0.2105 0.2691
REMARK 3 9 2.4775 - 2.3822 0.98 7572 399 0.2102 0.2867
REMARK 3 10 2.3822 - 2.3000 0.98 7601 400 0.2162 0.2859
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.11
REMARK 3 K_SOL : 0.31
REMARK 3 B_SOL : 33.82
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.630
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) : 8.27910
REMARK 3 B22 (A**2) : 3.42320
REMARK 3 B33 (A**2) : -5.48560
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -6.97280
REMARK 3 B23 (A**2) : 0.00000
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 : 0.010 12228
REMARK 3 ANGLE : 1.252 16529
REMARK 3 CHIRALITY : 0.082 1823
REMARK 3 PLANARITY : 0.005 2145
REMARK 3 DIHEDRAL : 13.949 4472
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 4E7Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071283.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-MAY-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.75
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 111 CHANNEL
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 : 80429
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.35
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 3.81
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 3.5% PEG 8000, 50MM MES, 1MM TCEP,
REMARK 280 50MM SAM AND A STOCK SOLUTION OF THE PROTEIN AT 10 MG.ML-1
REMARK 280 TRAPPED IN THE PRE-POWERSTROKE STATE WITH 2MM MG.ADP AND VO4, PH
REMARK 280 6.75, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 46.65950
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 350
REMARK 350 BIOMOLECULE: 2
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: 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 MET A -8
REMARK 465 ASP A -7
REMARK 465 TYR A -6
REMARK 465 LYS A -5
REMARK 465 ASP A -4
REMARK 465 ASP A -3
REMARK 465 ASP A -2
REMARK 465 ASP A -1
REMARK 465 LYS A 0
REMARK 465 GLY A 1
REMARK 465 GLU A 2
REMARK 465 ASP A 3
REMARK 465 GLY A 4
REMARK 465 GLN A 176
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 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 ILE A 789
REMARK 465 MET B -8
REMARK 465 ASP B -7
REMARK 465 TYR B -6
REMARK 465 LYS B -5
REMARK 465 ASP B -4
REMARK 465 ASP B -3
REMARK 465 ASP B -2
REMARK 465 ASP B -1
REMARK 465 LYS B 0
REMARK 465 GLY B 1
REMARK 465 GLU B 2
REMARK 465 ASP B 3
REMARK 465 GLY B 4
REMARK 465 ALA B 355
REMARK 465 GLY B 356
REMARK 465 SER B 357
REMARK 465 THR B 358
REMARK 465 SER B 359
REMARK 465 GLY B 360
REMARK 465 MET B 395
REMARK 465 LEU B 396
REMARK 465 THR B 397
REMARK 465 THR B 398
REMARK 465 ALA B 399
REMARK 465 GLY B 400
REMARK 465 GLY B 401
REMARK 465 ALA B 402
REMARK 465 LYS B 403
REMARK 465 GLY B 404
REMARK 465 THR B 405
REMARK 465 VAL B 406
REMARK 465 ILE B 407
REMARK 465 LYS B 408
REMARK 465 SER B 623
REMARK 465 SER B 624
REMARK 465 THR B 625
REMARK 465 ASN B 626
REMARK 465 ASN B 627
REMARK 465 ASN B 628
REMARK 465 LYS B 629
REMARK 465 ASP B 630
REMARK 465 THR B 631
REMARK 465 LYS B 632
REMARK 465 GLN B 633
REMARK 465 LYS B 634
REMARK 465 ALA B 635
REMARK 465 GLY B 636
REMARK 465 LYS B 637
REMARK 465 MET B 722
REMARK 465 PRO B 723
REMARK 465 ASP B 724
REMARK 465 LYS B 725
REMARK 465 ILE B 789
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 LYS A 5 CG CD CE NZ
REMARK 470 ASP A 27 CB CG OD1 OD2
REMARK 470 LYS A 37 CG CD CE NZ
REMARK 470 LYS A 39 CG CD CE NZ
REMARK 470 LYS A 105 CD CE NZ
REMARK 470 GLU A 110 CD OE1 OE2
REMARK 470 LYS A 139 CE NZ
REMARK 470 LYS A 142 CD CE NZ
REMARK 470 GLU A 216 CG CD OE1 OE2
REMARK 470 LYS A 217 CD CE NZ
REMARK 470 LYS A 240 CD CE NZ
REMARK 470 GLU A 261 CG CD OE1 OE2
REMARK 470 ARG A 262 CD NE CZ NH1 NH2
REMARK 470 LYS A 285 CE NZ
REMARK 470 LYS A 325 CD CE NZ
REMARK 470 LYS A 367 CD CE NZ
REMARK 470 LEU A 396 CG CD1 CD2
REMARK 470 GLU A 414 CD OE1 OE2
REMARK 470 GLU A 446 CG CD OE1
REMARK 470 GLN A 497 CD OE1 NE2
REMARK 470 LYS A 552 CG CD CE NZ
REMARK 470 LYS A 564 CD CE NZ
REMARK 470 ARG A 569 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 713 CG CD OE1 OE2
REMARK 470 LYS A 719 CE NZ
REMARK 470 LYS A 725 CD CE NZ
REMARK 470 ARG A 728 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 37 CG CD CE NZ
REMARK 470 LYS B 39 CG CD CE NZ
REMARK 470 ARG B 166 NE CZ NH1 NH2
REMARK 470 GLN B 176 CG CD OE1 NE2
REMARK 470 LYS B 217 CG CD CE NZ
REMARK 470 LYS B 285 CD CE NZ
REMARK 470 GLU B 286 CD OE1 OE2
REMARK 470 LYS B 302 CE NZ
REMARK 470 LYS B 325 CE NZ
REMARK 470 GLU B 354 CG CD OE1 OE2
REMARK 470 LYS B 367 CD CE NZ
REMARK 470 THR B 369 CB CG2
REMARK 470 GLU B 373 CG CD OE1 OE2
REMARK 470 ARG B 393 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 412 CD CE NZ
REMARK 470 GLU B 414 CD OE1 OE2
REMARK 470 GLU B 446 CG CD OE1 OE2
REMARK 470 LYS B 498 CD CE NZ
REMARK 470 ARG B 521 NE CZ NH1 NH2
REMARK 470 LEU B 522 CG CD1 CD2
REMARK 470 GLN B 537 CG CD OE1 NE2
REMARK 470 LYS B 552 CD CE NZ
REMARK 470 LYS B 562 CE NZ
REMARK 470 LYS B 564 CD CE NZ
REMARK 470 GLU B 595 CG CD OE1 OE2
REMARK 470 MET B 603 CG SD CE
REMARK 470 SER B 710 OG
REMARK 470 PHE B 711 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 HIS B 712 CG ND1 CD2 CE1 NE2
REMARK 470 GLU B 713 CG CD OE1 OE2
REMARK 470 TYR B 715 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 719 CG CD CE NZ
REMARK 470 LYS B 720 CG CD CE NZ
REMARK 470 LEU B 726 CG CD1 CD2
REMARK 470 ARG B 728 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 736 CG CD CE NZ
REMARK 470 LYS B 740 CG CD CE NZ
REMARK 470 GLU B 746 CG CD OE1 OE2
REMARK 470 GLN B 768 OE1 NE2
REMARK 470 LYS B 771 CG CD CE NZ
REMARK 470 ASP B 773 CG OD1 OD2
REMARK 470 ASP B 775 CG OD1 OD2
REMARK 470 GLU B 779 CG CD OE1 OE2
REMARK 470 VAL B 781 O
REMARK 470 LYS B 782 CG CD CE NZ
REMARK 470 ARG B 783 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 785 CG OD1 ND2
REMARK 470 HIS B 786 CG ND1 CD2 CE1 NE2
REMARK 470 LEU B 788 CG CD1 CD2
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 ARG B 618 O HOH B 1060 2.05
REMARK 500 O HOH A 1134 O HOH A 1137 2.08
REMARK 500 O HOH B 1047 O HOH B 1048 2.12
REMARK 500 OG SER B 119 OD2 ASP B 767 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 PRO A 26 -77.06 -33.67
REMARK 500 GLN A 36 58.10 -143.48
REMARK 500 ALA A 91 -117.59 57.69
REMARK 500 LYS A 105 -12.93 77.80
REMARK 500 ASP A 180 -47.10 83.65
REMARK 500 LEU A 229 73.19 48.28
REMARK 500 SER A 266 -168.98 -161.09
REMARK 500 THR A 358 -81.54 -91.91
REMARK 500 ILE A 407 -72.26 -111.36
REMARK 500 LYS A 408 96.35 113.12
REMARK 500 PHE A 443 57.29 -144.39
REMARK 500 SER A 467 -155.21 -121.76
REMARK 500 LYS A 490 -66.92 -91.86
REMARK 500 LEU A 522 -47.39 65.86
REMARK 500 GLN A 592 -4.84 76.68
REMARK 500 SER B 28 131.63 -170.88
REMARK 500 GLN B 36 62.61 -152.41
REMARK 500 ALA B 91 -115.59 56.63
REMARK 500 LYS B 105 -17.08 77.91
REMARK 500 VAL B 140 -72.32 -56.04
REMARK 500 ASN B 202 51.09 -119.95
REMARK 500 LEU B 229 78.17 44.10
REMARK 500 PHE B 443 44.94 -140.25
REMARK 500 LEU B 522 -48.71 70.33
REMARK 500 PHE B 621 62.55 -115.64
REMARK 500 GLN B 702 -36.17 -37.49
REMARK 500 HIS B 712 4.32 -163.02
REMARK 500 TYR B 718 -126.57 -92.80
REMARK 500 LYS B 719 -69.35 63.66
REMARK 500 LYS B 720 -8.61 -49.59
REMARK 500 ALA B 727 41.73 -108.53
REMARK 500 LEU B 729 -138.39 62.65
REMARK 500 LYS B 750 135.87 -170.77
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 803 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 158 OG1
REMARK 620 2 SER A 204 OG 85.8
REMARK 620 3 ADP A 801 O1B 107.5 162.6
REMARK 620 4 VO4 A 802 O2 171.5 92.1 73.1
REMARK 620 5 HOH A 933 O 98.5 95.2 93.9 89.9
REMARK 620 6 HOH A1035 O 94.2 85.3 82.6 77.4 167.3
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 VO4 A 802 V
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP A 801 O2B
REMARK 620 2 VO4 A 802 O1 176.5
REMARK 620 3 VO4 A 802 O2 85.2 98.1
REMARK 620 4 VO4 A 802 O3 79.6 98.1 113.2
REMARK 620 5 VO4 A 802 O4 84.1 94.7 124.9 117.6
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 803 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 158 OG1
REMARK 620 2 SER B 204 OG 80.6
REMARK 620 3 ADP B 801 O1B 91.6 155.8
REMARK 620 4 VO4 B 802 O2 147.4 87.3 87.3
REMARK 620 5 HOH B 971 O 78.8 83.4 72.6 69.7
REMARK 620 6 HOH B 983 O 97.6 96.5 107.3 113.8 176.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 VO4 B 802 V
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP B 801 O2B
REMARK 620 2 VO4 B 802 O1 177.8
REMARK 620 3 VO4 B 802 O2 82.0 97.5
REMARK 620 4 VO4 B 802 O3 81.8 96.4 108.2
REMARK 620 5 VO4 B 802 O4 83.9 98.1 125.4 121.4
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 ADP A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VO4 A 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 805
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 806
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 807
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VO4 B 802
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 803
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 804
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 805
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4E7S RELATED DB: PDB
DBREF 4E7Z A 2 789 UNP F1RQI7 F1RQI7_PIG 2 789
DBREF 4E7Z B 2 789 UNP F1RQI7 F1RQI7_PIG 2 789
SEQADV 4E7Z MET A -8 UNP F1RQI7 EXPRESSION TAG
SEQADV 4E7Z ASP A -7 UNP F1RQI7 EXPRESSION TAG
SEQADV 4E7Z TYR A -6 UNP F1RQI7 EXPRESSION TAG
SEQADV 4E7Z LYS A -5 UNP F1RQI7 EXPRESSION TAG
SEQADV 4E7Z ASP A -4 UNP F1RQI7 EXPRESSION TAG
SEQADV 4E7Z ASP A -3 UNP F1RQI7 EXPRESSION TAG
SEQADV 4E7Z ASP A -2 UNP F1RQI7 EXPRESSION TAG
SEQADV 4E7Z ASP A -1 UNP F1RQI7 EXPRESSION TAG
SEQADV 4E7Z LYS A 0 UNP F1RQI7 EXPRESSION TAG
SEQADV 4E7Z GLY A 1 UNP F1RQI7 EXPRESSION TAG
SEQADV 4E7Z MET B -8 UNP F1RQI7 EXPRESSION TAG
SEQADV 4E7Z ASP B -7 UNP F1RQI7 EXPRESSION TAG
SEQADV 4E7Z TYR B -6 UNP F1RQI7 EXPRESSION TAG
SEQADV 4E7Z LYS B -5 UNP F1RQI7 EXPRESSION TAG
SEQADV 4E7Z ASP B -4 UNP F1RQI7 EXPRESSION TAG
SEQADV 4E7Z ASP B -3 UNP F1RQI7 EXPRESSION TAG
SEQADV 4E7Z ASP B -2 UNP F1RQI7 EXPRESSION TAG
SEQADV 4E7Z ASP B -1 UNP F1RQI7 EXPRESSION TAG
SEQADV 4E7Z LYS B 0 UNP F1RQI7 EXPRESSION TAG
SEQADV 4E7Z GLY B 1 UNP F1RQI7 EXPRESSION TAG
SEQRES 1 A 798 MET ASP TYR LYS ASP ASP ASP ASP LYS GLY GLU ASP GLY
SEQRES 2 A 798 LYS PRO VAL TRP ALA PRO HIS PRO THR ASP GLY PHE GLN
SEQRES 3 A 798 VAL GLY ASN ILE VAL ASP ILE GLY PRO ASP SER LEU THR
SEQRES 4 A 798 ILE GLU PRO LEU ASN GLN LYS GLY LYS THR PHE LEU ALA
SEQRES 5 A 798 LEU ILE ASN GLN VAL PHE PRO ALA GLU GLU ASP SER LYS
SEQRES 6 A 798 LYS ASP VAL GLU ASP ASN CYS SER LEU MET TYR LEU ASN
SEQRES 7 A 798 GLU ALA THR LEU LEU HIS ASN ILE LYS VAL ARG TYR SER
SEQRES 8 A 798 LYS ASP ARG ILE TYR THR TYR VAL ALA ASN ILE LEU ILE
SEQRES 9 A 798 ALA VAL ASN PRO TYR PHE ASP ILE PRO LYS ILE TYR SER
SEQRES 10 A 798 SER GLU THR ILE LYS SER TYR GLN GLY LYS SER LEU GLY
SEQRES 11 A 798 THR MET PRO PRO HIS VAL PHE ALA ILE ALA ASP LYS ALA
SEQRES 12 A 798 PHE ARG ASP MET LYS VAL LEU LYS LEU SER GLN SER ILE
SEQRES 13 A 798 ILE VAL SER GLY GLU SER GLY ALA GLY LYS THR GLU ASN
SEQRES 14 A 798 THR LYS PHE VAL LEU ARG TYR LEU THR GLU SER TYR GLY
SEQRES 15 A 798 THR GLY GLN ASP ILE ASP ASP ARG ILE VAL GLU ALA ASN
SEQRES 16 A 798 PRO LEU LEU GLU ALA PHE GLY ASN ALA LYS THR VAL ARG
SEQRES 17 A 798 ASN ASN ASN SER SER ARG PHE GLY LYS PHE VAL GLU ILE
SEQRES 18 A 798 HIS PHE ASN GLU LYS SER SER VAL VAL GLY GLY PHE VAL
SEQRES 19 A 798 SER HIS TYR LEU LEU GLU LYS SER ARG ILE CYS VAL GLN
SEQRES 20 A 798 GLY LYS GLU GLU ARG ASN TYR HIS ILE PHE TYR ARG LEU
SEQRES 21 A 798 CYS ALA GLY ALA SER GLU ASP ILE ARG GLU ARG LEU HIS
SEQRES 22 A 798 LEU SER SER PRO ASP ASN PHE ARG TYR LEU ASN ARG GLY
SEQRES 23 A 798 CYS THR ARG TYR PHE ALA ASN LYS GLU THR ASP LYS GLN
SEQRES 24 A 798 ILE LEU GLN ASN ARG LYS SER PRO GLU TYR LEU LYS ALA
SEQRES 25 A 798 GLY SER LEU LYS ASP PRO LEU LEU ASP ASP HIS GLY ASP
SEQRES 26 A 798 PHE ILE ARG MET CYS THR ALA MET LYS LYS ILE GLY LEU
SEQRES 27 A 798 ASP ASP GLU GLU LYS LEU ASP LEU PHE ARG VAL VAL ALA
SEQRES 28 A 798 GLY VAL LEU HIS LEU GLY ASN ILE ASP PHE GLU GLU ALA
SEQRES 29 A 798 GLY SER THR SER GLY GLY CYS ASN LEU LYS ASN LYS SER
SEQRES 30 A 798 THR GLN ALA LEU GLU TYR CYS ALA GLU LEU LEU GLY LEU
SEQRES 31 A 798 ASP GLN ASP ASP LEU ARG VAL SER LEU THR THR ARG VAL
SEQRES 32 A 798 MET LEU THR THR ALA GLY GLY ALA LYS GLY THR VAL ILE
SEQRES 33 A 798 LYS VAL PRO LEU LYS VAL GLU GLN ALA ASN ASN ALA ARG
SEQRES 34 A 798 ASP ALA LEU ALA LYS THR VAL TYR SER HIS LEU PHE ASP
SEQRES 35 A 798 HIS VAL VAL ASN ARG VAL ASN GLN CYS PHE PRO PHE GLU
SEQRES 36 A 798 THR SER SER TYR PHE ILE GLY VAL LEU ASP ILE ALA GLY
SEQRES 37 A 798 PHE GLU TYR PHE GLU HIS ASN SER PHE GLU GLN PHE CYS
SEQRES 38 A 798 ILE ASN TYR CYS ASN GLU LYS LEU GLN GLN PHE PHE ASN
SEQRES 39 A 798 GLU ARG ILE LEU LYS GLU GLU GLN GLU LEU TYR GLN LYS
SEQRES 40 A 798 GLU GLY LEU GLY VAL ASN GLU VAL HIS TYR VAL ASP ASN
SEQRES 41 A 798 GLN ASP CYS ILE ASP LEU ILE GLU ALA ARG LEU VAL GLY
SEQRES 42 A 798 ILE LEU ASP ILE LEU ASP GLU GLU ASN ARG LEU PRO GLN
SEQRES 43 A 798 PRO SER ASP GLN HIS PHE THR SER ALA VAL HIS GLN LYS
SEQRES 44 A 798 HIS LYS ASP HIS PHE ARG LEU SER ILE PRO ARG LYS SER
SEQRES 45 A 798 LYS LEU ALA ILE HIS ARG ASN ILE ARG ASP ASP GLU GLY
SEQRES 46 A 798 PHE ILE ILE ARG HIS PHE ALA GLY ALA VAL CYS TYR GLU
SEQRES 47 A 798 THR THR GLN PHE VAL GLU LYS ASN ASN ASP ALA LEU HIS
SEQRES 48 A 798 MET SER LEU GLU SER LEU ILE CYS GLU SER ARG ASP LYS
SEQRES 49 A 798 PHE ILE ARG GLU LEU PHE GLU SER SER THR ASN ASN ASN
SEQRES 50 A 798 LYS ASP THR LYS GLN LYS ALA GLY LYS LEU SER PHE ILE
SEQRES 51 A 798 SER VAL GLY ASN LYS PHE LYS THR GLN LEU ASN LEU LEU
SEQRES 52 A 798 LEU ASP LYS LEU ARG SER THR GLY ALA SER PHE ILE ARG
SEQRES 53 A 798 CYS ILE LYS PRO ASN LEU LYS MET THR SER HIS HIS PHE
SEQRES 54 A 798 GLU GLY ALA GLN ILE LEU SER GLN LEU GLN CYS SER GLY
SEQRES 55 A 798 MET VAL SER VAL LEU ASP LEU MET GLN GLY GLY PHE PRO
SEQRES 56 A 798 SER ARG ALA SER PHE HIS GLU LEU TYR ASN MET TYR LYS
SEQRES 57 A 798 LYS TYR MET PRO ASP LYS LEU ALA ARG LEU ASP PRO ARG
SEQRES 58 A 798 LEU PHE CYS LYS ALA LEU PHE LYS ALA LEU GLY LEU ASN
SEQRES 59 A 798 GLU ILE ASP TYR LYS PHE GLY LEU THR LYS VAL PHE PHE
SEQRES 60 A 798 ARG PRO GLY LYS PHE ALA GLU PHE ASP GLN ILE MET LYS
SEQRES 61 A 798 SER ASP PRO ASP HIS LEU ALA GLU LEU VAL LYS ARG VAL
SEQRES 62 A 798 ASN HIS TRP LEU ILE
SEQRES 1 B 798 MET ASP TYR LYS ASP ASP ASP ASP LYS GLY GLU ASP GLY
SEQRES 2 B 798 LYS PRO VAL TRP ALA PRO HIS PRO THR ASP GLY PHE GLN
SEQRES 3 B 798 VAL GLY ASN ILE VAL ASP ILE GLY PRO ASP SER LEU THR
SEQRES 4 B 798 ILE GLU PRO LEU ASN GLN LYS GLY LYS THR PHE LEU ALA
SEQRES 5 B 798 LEU ILE ASN GLN VAL PHE PRO ALA GLU GLU ASP SER LYS
SEQRES 6 B 798 LYS ASP VAL GLU ASP ASN CYS SER LEU MET TYR LEU ASN
SEQRES 7 B 798 GLU ALA THR LEU LEU HIS ASN ILE LYS VAL ARG TYR SER
SEQRES 8 B 798 LYS ASP ARG ILE TYR THR TYR VAL ALA ASN ILE LEU ILE
SEQRES 9 B 798 ALA VAL ASN PRO TYR PHE ASP ILE PRO LYS ILE TYR SER
SEQRES 10 B 798 SER GLU THR ILE LYS SER TYR GLN GLY LYS SER LEU GLY
SEQRES 11 B 798 THR MET PRO PRO HIS VAL PHE ALA ILE ALA ASP LYS ALA
SEQRES 12 B 798 PHE ARG ASP MET LYS VAL LEU LYS LEU SER GLN SER ILE
SEQRES 13 B 798 ILE VAL SER GLY GLU SER GLY ALA GLY LYS THR GLU ASN
SEQRES 14 B 798 THR LYS PHE VAL LEU ARG TYR LEU THR GLU SER TYR GLY
SEQRES 15 B 798 THR GLY GLN ASP ILE ASP ASP ARG ILE VAL GLU ALA ASN
SEQRES 16 B 798 PRO LEU LEU GLU ALA PHE GLY ASN ALA LYS THR VAL ARG
SEQRES 17 B 798 ASN ASN ASN SER SER ARG PHE GLY LYS PHE VAL GLU ILE
SEQRES 18 B 798 HIS PHE ASN GLU LYS SER SER VAL VAL GLY GLY PHE VAL
SEQRES 19 B 798 SER HIS TYR LEU LEU GLU LYS SER ARG ILE CYS VAL GLN
SEQRES 20 B 798 GLY LYS GLU GLU ARG ASN TYR HIS ILE PHE TYR ARG LEU
SEQRES 21 B 798 CYS ALA GLY ALA SER GLU ASP ILE ARG GLU ARG LEU HIS
SEQRES 22 B 798 LEU SER SER PRO ASP ASN PHE ARG TYR LEU ASN ARG GLY
SEQRES 23 B 798 CYS THR ARG TYR PHE ALA ASN LYS GLU THR ASP LYS GLN
SEQRES 24 B 798 ILE LEU GLN ASN ARG LYS SER PRO GLU TYR LEU LYS ALA
SEQRES 25 B 798 GLY SER LEU LYS ASP PRO LEU LEU ASP ASP HIS GLY ASP
SEQRES 26 B 798 PHE ILE ARG MET CYS THR ALA MET LYS LYS ILE GLY LEU
SEQRES 27 B 798 ASP ASP GLU GLU LYS LEU ASP LEU PHE ARG VAL VAL ALA
SEQRES 28 B 798 GLY VAL LEU HIS LEU GLY ASN ILE ASP PHE GLU GLU ALA
SEQRES 29 B 798 GLY SER THR SER GLY GLY CYS ASN LEU LYS ASN LYS SER
SEQRES 30 B 798 THR GLN ALA LEU GLU TYR CYS ALA GLU LEU LEU GLY LEU
SEQRES 31 B 798 ASP GLN ASP ASP LEU ARG VAL SER LEU THR THR ARG VAL
SEQRES 32 B 798 MET LEU THR THR ALA GLY GLY ALA LYS GLY THR VAL ILE
SEQRES 33 B 798 LYS VAL PRO LEU LYS VAL GLU GLN ALA ASN ASN ALA ARG
SEQRES 34 B 798 ASP ALA LEU ALA LYS THR VAL TYR SER HIS LEU PHE ASP
SEQRES 35 B 798 HIS VAL VAL ASN ARG VAL ASN GLN CYS PHE PRO PHE GLU
SEQRES 36 B 798 THR SER SER TYR PHE ILE GLY VAL LEU ASP ILE ALA GLY
SEQRES 37 B 798 PHE GLU TYR PHE GLU HIS ASN SER PHE GLU GLN PHE CYS
SEQRES 38 B 798 ILE ASN TYR CYS ASN GLU LYS LEU GLN GLN PHE PHE ASN
SEQRES 39 B 798 GLU ARG ILE LEU LYS GLU GLU GLN GLU LEU TYR GLN LYS
SEQRES 40 B 798 GLU GLY LEU GLY VAL ASN GLU VAL HIS TYR VAL ASP ASN
SEQRES 41 B 798 GLN ASP CYS ILE ASP LEU ILE GLU ALA ARG LEU VAL GLY
SEQRES 42 B 798 ILE LEU ASP ILE LEU ASP GLU GLU ASN ARG LEU PRO GLN
SEQRES 43 B 798 PRO SER ASP GLN HIS PHE THR SER ALA VAL HIS GLN LYS
SEQRES 44 B 798 HIS LYS ASP HIS PHE ARG LEU SER ILE PRO ARG LYS SER
SEQRES 45 B 798 LYS LEU ALA ILE HIS ARG ASN ILE ARG ASP ASP GLU GLY
SEQRES 46 B 798 PHE ILE ILE ARG HIS PHE ALA GLY ALA VAL CYS TYR GLU
SEQRES 47 B 798 THR THR GLN PHE VAL GLU LYS ASN ASN ASP ALA LEU HIS
SEQRES 48 B 798 MET SER LEU GLU SER LEU ILE CYS GLU SER ARG ASP LYS
SEQRES 49 B 798 PHE ILE ARG GLU LEU PHE GLU SER SER THR ASN ASN ASN
SEQRES 50 B 798 LYS ASP THR LYS GLN LYS ALA GLY LYS LEU SER PHE ILE
SEQRES 51 B 798 SER VAL GLY ASN LYS PHE LYS THR GLN LEU ASN LEU LEU
SEQRES 52 B 798 LEU ASP LYS LEU ARG SER THR GLY ALA SER PHE ILE ARG
SEQRES 53 B 798 CYS ILE LYS PRO ASN LEU LYS MET THR SER HIS HIS PHE
SEQRES 54 B 798 GLU GLY ALA GLN ILE LEU SER GLN LEU GLN CYS SER GLY
SEQRES 55 B 798 MET VAL SER VAL LEU ASP LEU MET GLN GLY GLY PHE PRO
SEQRES 56 B 798 SER ARG ALA SER PHE HIS GLU LEU TYR ASN MET TYR LYS
SEQRES 57 B 798 LYS TYR MET PRO ASP LYS LEU ALA ARG LEU ASP PRO ARG
SEQRES 58 B 798 LEU PHE CYS LYS ALA LEU PHE LYS ALA LEU GLY LEU ASN
SEQRES 59 B 798 GLU ILE ASP TYR LYS PHE GLY LEU THR LYS VAL PHE PHE
SEQRES 60 B 798 ARG PRO GLY LYS PHE ALA GLU PHE ASP GLN ILE MET LYS
SEQRES 61 B 798 SER ASP PRO ASP HIS LEU ALA GLU LEU VAL LYS ARG VAL
SEQRES 62 B 798 ASN HIS TRP LEU ILE
HET ADP A 801 27
HET VO4 A 802 5
HET MG A 803 1
HET GOL A 804 6
HET GOL A 805 6
HET GOL A 806 6
HET GOL A 807 6
HET ADP B 801 27
HET VO4 B 802 5
HET MG B 803 1
HET GOL B 804 6
HET GOL B 805 6
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM VO4 VANADATE ION
HETNAM MG MAGNESIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 ADP 2(C10 H15 N5 O10 P2)
FORMUL 4 VO4 2(O4 V 3-)
FORMUL 5 MG 2(MG 2+)
FORMUL 6 GOL 6(C3 H8 O3)
FORMUL 15 HOH *456(H2 O)
HELIX 1 1 ASN A 46 VAL A 48 5 3
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 ILE A 178 GLY A 193 1 16
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 ASN A 270 5 4
HELIX 12 12 PHE A 271 ARG A 276 1 6
HELIX 13 13 ASN A 284 LYS A 289 1 6
HELIX 14 14 GLN A 290 ILE A 291 5 2
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 GLY A 348 1 19
HELIX 19 19 SER A 368 GLY A 380 1 13
HELIX 20 20 ASP A 382 THR A 391 1 10
HELIX 21 21 LYS A 412 CYS A 442 1 31
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 LEU A 535 1 12
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 ARG A 569 5 5
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 GLY A 703 1 11
HELIX 36 36 PHE A 711 LYS A 719 1 9
HELIX 37 37 LYS A 720 MET A 722 5 3
HELIX 38 38 PRO A 723 ARG A 728 1 6
HELIX 39 39 ASP A 730 LEU A 742 1 13
HELIX 40 40 LYS A 762 LYS A 771 1 10
HELIX 41 41 ASP A 773 LEU A 788 1 16
HELIX 42 42 LEU B 44 VAL B 48 5 5
HELIX 43 43 ASP B 61 LEU B 65 5 5
HELIX 44 44 ASN B 69 LYS B 83 1 15
HELIX 45 45 SER B 108 TYR B 115 1 8
HELIX 46 46 HIS B 126 LYS B 142 1 17
HELIX 47 47 GLY B 156 GLY B 173 1 18
HELIX 48 48 GLN B 176 GLY B 193 1 18
HELIX 49 49 LYS B 232 CYS B 236 5 5
HELIX 50 50 TYR B 245 ALA B 255 1 11
HELIX 51 51 SER B 256 HIS B 264 1 9
HELIX 52 52 SER B 267 ASN B 270 5 4
HELIX 53 53 PHE B 271 ARG B 276 1 6
HELIX 54 54 ASN B 284 LYS B 289 1 6
HELIX 55 55 GLN B 290 ILE B 291 5 2
HELIX 56 56 LEU B 292 LYS B 296 5 5
HELIX 57 57 SER B 297 GLY B 304 1 8
HELIX 58 58 ASP B 312 ILE B 327 1 16
HELIX 59 59 ASP B 330 GLY B 348 1 19
HELIX 60 60 SER B 368 LEU B 379 1 12
HELIX 61 61 ASP B 382 THR B 392 1 11
HELIX 62 62 LYS B 412 GLN B 441 1 30
HELIX 63 63 SER B 467 LEU B 489 1 23
HELIX 64 64 LYS B 490 GLU B 499 1 10
HELIX 65 65 ASN B 511 ALA B 520 1 10
HELIX 66 66 GLY B 524 LEU B 535 1 12
HELIX 67 67 SER B 539 HIS B 551 1 13
HELIX 68 68 ILE B 559 SER B 563 5 5
HELIX 69 69 LEU B 565 ARG B 569 5 5
HELIX 70 70 ARG B 572 ASP B 574 5 3
HELIX 71 71 GLN B 592 ASN B 597 1 6
HELIX 72 72 HIS B 602 GLU B 611 1 10
HELIX 73 73 ASP B 614 LEU B 620 1 7
HELIX 74 74 SER B 642 SER B 660 1 19
HELIX 75 75 GLU B 681 SER B 692 1 12
HELIX 76 76 GLY B 693 LEU B 700 1 8
HELIX 77 77 ASP B 730 LEU B 742 1 13
HELIX 78 78 LYS B 762 LYS B 771 1 10
HELIX 79 79 ASP B 773 VAL B 781 1 9
HELIX 80 80 VAL B 784 LEU B 788 5 5
SHEET 1 A 5 PHE A 41 LEU A 44 0
SHEET 2 A 5 SER A 28 PRO A 33 -1 N ILE A 31 O PHE A 41
SHEET 3 A 5 GLY A 15 GLY A 25 -1 N ASN A 20 O GLU A 32
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
SHEET 1 H 5 PHE B 41 ALA B 43 0
SHEET 2 H 5 SER B 28 PRO B 33 -1 N ILE B 31 O PHE B 41
SHEET 3 H 5 GLY B 15 GLY B 25 -1 N GLY B 25 O SER B 28
SHEET 4 H 5 VAL B 7 HIS B 11 -1 N VAL B 7 O GLY B 19
SHEET 5 H 5 PHE B 49 PRO B 50 -1 O PHE B 49 N TRP B 8
SHEET 1 I 7 TYR B 87 VAL B 90 0
SHEET 2 I 7 ILE B 93 VAL B 97 -1 O ILE B 95 N THR B 88
SHEET 3 I 7 GLY B 662 ILE B 669 1 O ARG B 667 N LEU B 94
SHEET 4 I 7 GLN B 145 SER B 150 1 N ILE B 148 O SER B 664
SHEET 5 I 7 TYR B 450 ASP B 456 1 O GLY B 453 N GLN B 145
SHEET 6 I 7 GLY B 207 PHE B 214 -1 N PHE B 214 O TYR B 450
SHEET 7 I 7 VAL B 220 TYR B 228 -1 O GLY B 222 N HIS B 213
SHEET 1 J 2 ASN B 194 ALA B 195 0
SHEET 2 J 2 SER B 203 SER B 204 -1 O SER B 203 N ALA B 195
SHEET 1 K 2 PHE B 352 GLU B 353 0
SHEET 2 K 2 ASN B 363 LEU B 364 -1 O ASN B 363 N GLU B 353
SHEET 1 L 3 LEU B 557 SER B 558 0
SHEET 2 L 3 GLY B 576 HIS B 581 -1 O ILE B 578 N SER B 558
SHEET 3 L 3 GLY B 584 GLU B 589 -1 O TYR B 588 N PHE B 577
SHEET 1 M 3 SER B 707 SER B 710 0
SHEET 2 M 3 LYS B 755 PHE B 758 -1 O VAL B 756 N ALA B 709
SHEET 3 M 3 TYR B 749 PHE B 751 -1 N LYS B 750 O PHE B 757
LINK OG1 THR A 158 MG MG A 803 1555 1555 2.41
LINK OG SER A 204 MG MG A 803 1555 1555 2.47
LINK O2B ADP A 801 V VO4 A 802 1555 1555 2.26
LINK O1B ADP A 801 MG MG A 803 1555 1555 2.36
LINK O2 VO4 A 802 MG MG A 803 1555 1555 2.22
LINK MG MG A 803 O HOH A 933 1555 1555 2.47
LINK MG MG A 803 O HOH A1035 1555 1555 2.50
LINK OG1 THR B 158 MG MG B 803 1555 1555 2.40
LINK OG SER B 204 MG MG B 803 1555 1555 2.55
LINK O2B ADP B 801 V VO4 B 802 1555 1555 2.15
LINK O1B ADP B 801 MG MG B 803 1555 1555 2.39
LINK O2 VO4 B 802 MG MG B 803 1555 1555 2.28
LINK MG MG B 803 O HOH B 971 1555 1555 2.50
LINK MG MG B 803 O HOH B 983 1555 1555 2.40
SITE 1 AC1 25 ASN A 98 PRO A 99 TYR A 100 PHE A 101
SITE 2 AC1 25 ASP A 102 TYR A 107 SER A 153 GLY A 154
SITE 3 AC1 25 ALA A 155 GLY A 156 LYS A 157 THR A 158
SITE 4 AC1 25 GLU A 159 PHE A 163 ASN A 200 LEU A 310
SITE 5 AC1 25 VO4 A 802 MG A 803 HOH A 954 HOH A 973
SITE 6 AC1 25 HOH A 977 HOH A 982 HOH A 996 HOH A1014
SITE 7 AC1 25 HOH A1035
SITE 1 AC2 12 SER A 153 GLY A 154 LYS A 157 ASN A 200
SITE 2 AC2 12 SER A 203 SER A 204 ALA A 458 GLY A 459
SITE 3 AC2 12 ADP A 801 MG A 803 HOH A 979 HOH A1035
SITE 1 AC3 6 THR A 158 SER A 204 ADP A 801 VO4 A 802
SITE 2 AC3 6 HOH A 933 HOH A1035
SITE 1 AC4 8 LYS A 162 PRO A 187 GLU A 190 ASN A 202
SITE 2 AC4 8 ARG A 250 LEU A 310 ASP A 316 HOH A1086
SITE 1 AC5 9 GLY A 151 PHE A 582 CYS A 668 GLN A 688
SITE 2 AC5 9 CYS A 691 SER A 692 HOH A 965 HOH A 992
SITE 3 AC5 9 HOH A1064
SITE 1 AC6 5 ASP A 288 GLY A 304 SER A 305 LYS A 307
SITE 2 AC6 5 HOH A1113
SITE 1 AC7 6 ALA A 253 GLY A 254 ALA A 255 GLN A 290
SITE 2 AC7 6 LEU A 292 ARG A 295
SITE 1 AC8 24 ASN B 98 PRO B 99 TYR B 100 PHE B 101
SITE 2 AC8 24 TYR B 107 GLY B 154 ALA B 155 GLY B 156
SITE 3 AC8 24 LYS B 157 THR B 158 GLU B 159 PHE B 163
SITE 4 AC8 24 ASN B 200 ASN B 202 LEU B 310 VO4 B 802
SITE 5 AC8 24 MG B 803 HOH B 902 HOH B 917 HOH B 963
SITE 6 AC8 24 HOH B 971 HOH B1002 HOH B1026 HOH B1082
SITE 1 AC9 12 SER B 153 GLY B 154 LYS B 157 ASN B 200
SITE 2 AC9 12 SER B 203 SER B 204 ALA B 458 GLY B 459
SITE 3 AC9 12 ADP B 801 MG B 803 HOH B 958 HOH B 971
SITE 1 BC1 6 THR B 158 SER B 204 ADP B 801 VO4 B 802
SITE 2 BC1 6 HOH B 971 HOH B 983
SITE 1 BC2 6 ASN B 284 LYS B 285 ASP B 288 GLY B 304
SITE 2 BC2 6 SER B 305 LYS B 307
SITE 1 BC3 2 PRO A 12 ARG B 618
CRYST1 98.148 93.319 101.875 90.00 90.60 90.00 P 1 21 1 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 0.010189 0.000000 0.000107 0.00000
SCALE2 0.000000 0.010716 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009816 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
