HEADER HYDROLASE 05-JAN-12 4AE3
TITLE CRYSTAL STRUCTURE OF AMMOSAMIDE 272:MYOSIN-2 MOTOR DOMAIN COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYOSIN-2 HEAVY CHAIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MOTOR DOMAIN, RESIDUES 2-761;
COMPND 5 SYNONYM: MYOSIN II HEAVY CHAIN;
COMPND 6 EC: 3.6.4.1;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DICTYOSTELIUM DISCOIDEUM;
SOURCE 3 ORGANISM_TAXID: 352472;
SOURCE 4 STRAIN: AX4;
SOURCE 5 EXPRESSION_SYSTEM: DICTYOSTELIUM DISCOIDEUM;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 352472;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: AX4;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PDXA-3H
KEYWDS HYDROLASE, ATPASE, CONTRACTILE PROTEIN, ACTIN BINDING, MOTOR PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.CHINTHALAPUDI,S.M.HEISSLER,W.FENICAL,D.J.MANSTEIN
REVDAT 2 20-DEC-23 4AE3 1 REMARK LINK
REVDAT 1 16-JAN-13 4AE3 0
JRNL AUTH K.CHINTHALAPUDI,S.M.HEISSLER,W.FENICAL,D.J.MANSTEIN
JRNL TITL STRUCTURAL BASIS FOR AMMOSAMIDE MEDIATED MYOSIN MOTOR
JRNL TITL 2 ACTIVITY INHIBITION
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.91
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 3 NUMBER OF REFLECTIONS : 34133
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.216
REMARK 3 R VALUE (WORKING SET) : 0.214
REMARK 3 FREE R VALUE : 0.254
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1721
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 41.9199 - 5.7191 1.00 2883 142 0.2151 0.2403
REMARK 3 2 5.7191 - 4.5412 0.99 2745 168 0.1951 0.2327
REMARK 3 3 4.5412 - 3.9677 0.98 2704 139 0.1771 0.2137
REMARK 3 4 3.9677 - 3.6051 0.98 2668 150 0.1926 0.2255
REMARK 3 5 3.6051 - 3.3468 0.98 2667 140 0.2002 0.2356
REMARK 3 6 3.3468 - 3.1496 0.98 2641 140 0.2269 0.2385
REMARK 3 7 3.1496 - 2.9919 0.98 2686 148 0.2264 0.2940
REMARK 3 8 2.9919 - 2.8617 1.00 2673 153 0.2542 0.3409
REMARK 3 9 2.8617 - 2.7515 0.99 2658 131 0.2574 0.3602
REMARK 3 10 2.7515 - 2.6566 0.99 2675 161 0.2479 0.3001
REMARK 3 11 2.6566 - 2.5736 0.99 2711 117 0.2519 0.2573
REMARK 3 12 2.5736 - 2.5000 1.00 2701 132 0.2711 0.3449
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 63.10
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.350
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.630
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 47.47
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 3.58190
REMARK 3 B22 (A**2) : 6.47470
REMARK 3 B33 (A**2) : -10.05660
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 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 : 0.012 6172
REMARK 3 ANGLE : 1.554 8340
REMARK 3 CHIRALITY : 0.103 902
REMARK 3 PLANARITY : 0.009 1076
REMARK 3 DIHEDRAL : 15.920 2334
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: LEVER ARM RESIDUES(FROM 700 TO 748) ARE
REMARK 3 HIGHLY MOBILE.
REMARK 4
REMARK 4 4AE3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-JAN-12.
REMARK 100 THE DEPOSITION ID IS D_1290050875.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-SEP-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : BRUKER X8 PROTEUM
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : PROTEUM2
REMARK 200 DATA SCALING SOFTWARE : SADABS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34133
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 41.910
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 76.61
REMARK 200 R MERGE (I) : 0.57000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.6800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 49.39
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.160
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 1YV3
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM HEPES PH 7.6, 140 MM NACL, 11%
REMARK 280 W/V PEG5K-MME, 2% (V/V) MPD
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 76.91500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 76.91500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 44.02500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 72.76000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 44.02500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 72.76000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 76.91500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 44.02500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 72.76000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 76.91500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 44.02500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 72.76000
REMARK 290 SMTRY3 8 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2301 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2305 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2367 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2377 LIES ON A SPECIAL POSITION.
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 ASN A 203
REMARK 465 GLN A 204
REMARK 465 ALA A 205
REMARK 465 ASN A 206
REMARK 465 GLY A 207
REMARK 465 GLN A 750
REMARK 465 LEU A 751
REMARK 465 ALA A 752
REMARK 465 ARG A 753
REMARK 465 ILE A 754
REMARK 465 GLU A 755
REMARK 465 GLU A 756
REMARK 465 ALA A 757
REMARK 465 ARG A 758
REMARK 465 GLU A 759
REMARK 465 GLN A 760
REMARK 465 ARG A 761
REMARK 465 LEU A 762
REMARK 465 GLU A 763
REMARK 465 SER A 764
REMARK 465 ASN A 765
REMARK 465 GLU A 766
REMARK 465 PRO A 767
REMARK 465 PRO A 768
REMARK 465 MET A 769
REMARK 465 ASP A 770
REMARK 465 PHE A 771
REMARK 465 ASP A 772
REMARK 465 ASP A 773
REMARK 465 ASP A 774
REMARK 465 ILE A 775
REMARK 465 PRO A 776
REMARK 465 PHE A 777
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 700 CG OD1 OD2
REMARK 470 LYS A 703 CG CD CE NZ
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 O10 27X A 1752 O HOH A 2213 1.81
REMARK 500 OD1 ASN A 541 O HOH A 2351 1.84
REMARK 500 OD2 ASP A 86 O HOH A 2082 1.85
REMARK 500 OE2 GLU A 365 O HOH A 2257 1.85
REMARK 500 O HOH A 2030 O HOH A 2079 1.87
REMARK 500 O HOH A 2260 O HOH A 2272 1.90
REMARK 500 O HOH A 2070 O HOH A 2094 1.92
REMARK 500 O HOH A 2074 O HOH A 2191 1.95
REMARK 500 O HOH A 2018 O HOH A 2110 1.96
REMARK 500 OE2 GLU A 492 O HOH A 2323 1.97
REMARK 500 O HOH A 2213 O HOH A 2387 1.99
REMARK 500 O SER A 57 O HOH A 2064 2.00
REMARK 500 O HOH A 2151 O HOH A 2352 2.04
REMARK 500 OD2 ASP A 160 OH TYR A 195 2.04
REMARK 500 NH2 ARG A 164 O HOH A 2136 2.05
REMARK 500 OD2 ASP A 10 O HOH A 2011 2.05
REMARK 500 O HOH A 2174 O HOH A 2395 2.06
REMARK 500 O1 EDO A 1754 O HOH A 2211 2.08
REMARK 500 O HOH A 2103 O HOH A 2242 2.09
REMARK 500 O HOH A 2006 O HOH A 2023 2.10
REMARK 500 OD1 ASP A 160 O HOH A 2133 2.14
REMARK 500 O HOH A 2054 O HOH A 2055 2.15
REMARK 500 O HOH A 2024 O HOH A 2061 2.15
REMARK 500 O HOH A 2337 O HOH A 2338 2.15
REMARK 500 O SER A 719 OG1 THR A 723 2.15
REMARK 500 O HOH A 2036 O HOH A 2085 2.16
REMARK 500 O HOH A 2117 O HOH A 2118 2.16
REMARK 500 NZ LYS A 670 O HOH A 2051 2.17
REMARK 500 O HOH A 2157 O HOH A 2428 2.18
REMARK 500 O HOH A 2068 O HOH A 2177 2.18
REMARK 500 OD1 ASP A 454 O HOH A 2164 2.18
REMARK 500 O PRO A 615 OG SER A 619 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 2232 O HOH A 2235 3555 1.91
REMARK 500 O HOH A 2062 O HOH A 2062 4556 1.97
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 ASN A 711 N - CA - C ANGL. DEV. = 17.6 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 ASP A 66 38.54 -82.52
REMARK 500 LEU A 262 72.24 58.07
REMARK 500 THR A 274 -8.98 75.23
REMARK 500 ASN A 277 -178.63 -66.90
REMARK 500 ALA A 299 -151.90 -124.28
REMARK 500 SER A 465 -166.20 -117.78
REMARK 500 LYS A 498 62.13 35.91
REMARK 500 LYS A 553 16.92 57.29
REMARK 500 LYS A 554 -52.68 -123.89
REMARK 500 TYR A 698 -3.57 -51.45
REMARK 500 VAL A 702 -29.03 -38.12
REMARK 500 TYR A 705 -153.63 -125.64
REMARK 500 TYR A 706 -84.37 -129.77
REMARK 500 LEU A 708 19.14 -154.32
REMARK 500 PRO A 710 61.17 -66.58
REMARK 500 ASN A 711 45.13 74.81
REMARK 500 PRO A 713 -155.71 -73.49
REMARK 500 PRO A 734 1.59 -62.79
REMARK 500 ALA A 748 46.27 -152.23
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A2069 DISTANCE = 6.23 ANGSTROMS
REMARK 525 HOH A2167 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH A2434 DISTANCE = 8.75 ANGSTROMS
REMARK 525 HOH A2435 DISTANCE = 5.99 ANGSTROMS
REMARK 525 HOH A2436 DISTANCE = 6.16 ANGSTROMS
REMARK 525 HOH A2437 DISTANCE = 7.01 ANGSTROMS
REMARK 525 HOH A2438 DISTANCE = 8.81 ANGSTROMS
REMARK 600
REMARK 600 HETEROGEN
REMARK 600
REMARK 600 AMMOSAMIDE 272 (27X): AMMOSAMIDE 272
REMARK 600 ADP ORTHOVANADATE (AOV) (AOV): ADP LINKED TO VO4
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 A1751 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 186 OG1
REMARK 620 2 SER A 237 OG 75.8
REMARK 620 3 AOV A1750 O1B 79.2 153.0
REMARK 620 4 AOV A1750 O1G 156.6 92.7 106.7
REMARK 620 5 HOH A2163 O 68.0 76.8 84.5 89.7
REMARK 620 6 HOH A2164 O 68.7 86.9 93.6 131.9 136.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AOV A 1750
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1751
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 27X A 1752
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 27X A 1753
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1754
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1755
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1756
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1757
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1MNE RELATED DB: PDB
REMARK 900 TRUNCATED HEAD OF MYOSIN FROM DICTYOSTELIUM DISCOIDEUM COMPLEXED
REMARK 900 WITH MG-PYROPHOSPHATE
REMARK 900 RELATED ID: 1D1C RELATED DB: PDB
REMARK 900 DICTYOSTELIUM MYOSIN S1DC (MOTOR DOMAIN FRAGMENT) COMPLEXED WITH N-
REMARK 900 METHYL-O-NITROPHENYL AMINOETHYLDIPHOSPHATE BERYLLIUM TRIFLUORIDE.
REMARK 900 RELATED ID: 1W9L RELATED DB: PDB
REMARK 900 MYOSIN II DICTYOSTELIUM DISCOIDEUM MOTOR DOMAIN S456E BOUND WITH
REMARK 900 MGADP-ALF4
REMARK 900 RELATED ID: 1VOM RELATED DB: PDB
REMARK 900 COMPLEX BETWEEN DICTYOSTELIUM MYOSIN AND MGADP AND VANADATE AT 1.9A
REMARK 900 RESOLUTION
REMARK 900 RELATED ID: 1MMN RELATED DB: PDB
REMARK 900 X-RAY STRUCTURES OF THE MGADP, MGATPGAMMAS, AND MGAMPPNP COMPLEXES
REMARK 900 OF THE DICTYOSTELIUM DISCOIDEUM MYOSIN MOTOR DOMAIN
REMARK 900 RELATED ID: 2AKA RELATED DB: PDB
REMARK 900 STRUCTURE OF THE NUCLEOTIDE-FREE MYOSIN II MOTOR DOMAINFROM
REMARK 900 DICTYOSTELIUM DISCOIDEUM FUSED TO THE GTPASE DOMAINOF DYNAMIN 1
REMARK 900 FROM RATTUS NORVEGICUS
REMARK 900 RELATED ID: 2JHR RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MYOSIN-2 MOTOR DOMAIN IN COMPLEX WITH ADP-
REMARK 900 METAVANADATE AND PENTABROMOPSEUDILIN
REMARK 900 RELATED ID: 2Y8I RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR THE ALLOSTERIC INTERFERENCE OF MYOSIN FUNCTION
REMARK 900 BY MUTANTS G680A AND G680V OF DICTYOSTELIUM MYOSIN-2
REMARK 900 RELATED ID: 1W9J RELATED DB: PDB
REMARK 900 MYOSIN II DICTYOSTELIUM DISCOIDEUM MOTOR DOMAIN S456Y BOUND WITH
REMARK 900 MGADP-ALF4
REMARK 900 RELATED ID: 2X9H RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MYOSIN-2 MOTOR DOMAIN IN COMPLEX WITH ADP-
REMARK 900 METAVANADATE AND PENTACHLOROCARBAZOLE
REMARK 900 RELATED ID: 1FMV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE APO MOTOR DOMAIN OF DICTYOSTELLIUMMYOSIN II
REMARK 900 RELATED ID: 1MMA RELATED DB: PDB
REMARK 900 X-RAY STRUCTURES OF THE MGADP, MGATPGAMMAS, AND MGAMPPNP COMPLEXES
REMARK 900 OF THE DICTYOSTELIUM DISCOIDEUM MYOSIN MOTOR DOMAIN
REMARK 900 RELATED ID: 2XO8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MYOSIN-2 IN COMPLEX WITH
REMARK 900 TRIBROMODICHLOROPSEUDILIN
REMARK 900 RELATED ID: 1MMG RELATED DB: PDB
REMARK 900 X-RAY STRUCTURES OF THE MGADP, MGATPGAMMAS, AND MGAMPPNP COMPLEXES
REMARK 900 OF THE DICTYOSTELIUM DISCOIDEUM MYOSIN MOTOR DOMAIN
REMARK 900 RELATED ID: 2Y0R RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR THE ALLOSTERIC INTERFERENCE OF MYOSIN FUNCTION
REMARK 900 BY MUTANTS G680A AND G680V OF DICTYOSTELIUM MYOSIN-2
REMARK 900 RELATED ID: 1W9I RELATED DB: PDB
REMARK 900 MYOSIN II DICTYOSTELIUM DISCOIDEUM MOTOR DOMAIN S456Y BOUND WITH
REMARK 900 MGADP-BEFX
REMARK 900 RELATED ID: 1MND RELATED DB: PDB
REMARK 900 TRUNCATED HEAD OF MYOSIN FROM DICTYOSTELIUM DISCOIDEUM COMPLEXED
REMARK 900 WITH MGADP-ALF4
REMARK 900 RELATED ID: 1W9K RELATED DB: PDB
REMARK 900 DICTYOSTELIUM DISCOIDEUM MYOSIN II MOTOR DOMAIN S456E WITH BOUND
REMARK 900 MGADP-BEFX
REMARK 900 RELATED ID: 1JX2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE NUCLEOTIDE-FREE DYNAMIN A GTPASEDOMAIN,
REMARK 900 DETERMINED AS MYOSIN FUSION
REMARK 900 RELATED ID: 1Q5G RELATED DB: PDB
REMARK 900 STRUCTURE OF THE NUCLEOTIDE-FREE MYOSIN II MOTOR DOMAINFROM
REMARK 900 DICTYOSTELIUM DISCOIDEUM
REMARK 900 RELATED ID: 1D0Y RELATED DB: PDB
REMARK 900 DICTYOSTELIUM MYOSIN S1DC (MOTOR DOMAIN FRAGMENT) COMPLEXED WITH O-
REMARK 900 NITROPHENYL AMINOETHYLDIPHOSPHATE BERYLLIUM FLUORIDE.
REMARK 900 RELATED ID: 1LVK RELATED DB: PDB
REMARK 900 X-RAY CRYSTAL STRUCTURE OF THE MG (DOT) 2'(3')-O -(N-
REMARK 900 METHYLANTHRANILOYL) NUCLEOTIDE BOUND TO DICTYOSTELIUM DISCOIDEUM
REMARK 900 MYOSIN MOTOR DOMAIN
REMARK 900 RELATED ID: 2JJ9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MYOSIN-2 IN COMPLEX WITH ADP- METAVANADATE
REMARK 900 RELATED ID: 2XEL RELATED DB: PDB
REMARK 900 MOLECULAR MECHANISM OF PENTACHLOROPSEUDILIN MEDIATED INHIBITION OF
REMARK 900 MYOSIN MOTOR ACTIVITY
REMARK 900 RELATED ID: 1JWY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE DYNAMIN A GTPASE DOMAIN COMPLEXEDWITH GDP,
REMARK 900 DETERMINED AS MYOSIN FUSION
REMARK 900 RELATED ID: 1YV3 RELATED DB: PDB
REMARK 900 THE STRUCTURAL BASIS OF BLEBBISTATIN INHIBITION ANDSPECIFICITY FOR
REMARK 900 MYOSIN II
REMARK 900 RELATED ID: 1D0X RELATED DB: PDB
REMARK 900 DICTYOSTELIUM MYOSIN S1DC (MOTOR DOMAIN FRAGMENT) COMPLEXED WITH M-
REMARK 900 NITROPHENYL AMINOETHYLDIPHOSPHATE BERYLLIUM TRIFLUORIDE.
REMARK 900 RELATED ID: 1FMW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE MGATP COMPLEX FOR THE MOTOR DOMAINOF
REMARK 900 DICTYOSTELIUM MYOSIN II
REMARK 900 RELATED ID: 1D1B RELATED DB: PDB
REMARK 900 DICTYOSTELIUM MYOSIN S1DC (MOTOR DOMAIN FRAGMENT) COMPLEXED WITH O,
REMARK 900 P-DINITROPHENYL AMINOPROPYLDIPHOSPHATE BERYLLIUM TRIFLUORIDE.
REMARK 900 RELATED ID: 1G8X RELATED DB: PDB
REMARK 900 STRUCTURE OF A GENETICALLY ENGINEERED MOLECULAR MOTOR
REMARK 900 RELATED ID: 1D1A RELATED DB: PDB
REMARK 900 DICTYOSTELIUM MYOSIN S1DC (MOTOR DOMAIN FRAGMENT) COMPLEXED WITH O,
REMARK 900 P-DINITROPHENYL AMINOETHYLDIPHOSPHATE BERYLLIUM TRIFLUORIDE.
REMARK 900 RELATED ID: 1D0Z RELATED DB: PDB
REMARK 900 DICTYOSTELIUM MYOSIN S1DC (MOTOR DOMAIN FRAGMENT) COMPLEXED WITH P-
REMARK 900 NITROPHENYL AMINOETHYLDIPHOSPHATE BERYLLIUM TRIFLUORIDE.
REMARK 900 RELATED ID: 1MMD RELATED DB: PDB
REMARK 900 TRUNCATED HEAD OF MYOSIN FROM DICTYOSTELIUM DISCOIDEUM COMPLEXED
REMARK 900 WITH MGADP-BEF3
REMARK 900 RELATED ID: 2Y9E RELATED DB: PDB
REMARK 900 STRUCTURAL BASIS FOR THE ALLOSTERIC INTERFERENCE OF MYOSIN FUNCTION
REMARK 900 BY MUTANTS G680A AND G680V OF DICTYOSTELIUM MYOSIN-2
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES FROM 750 ARE NOT RESOLVED IN THE MOTOR DOMAIN.
DBREF 4AE3 A 2 761 UNP P08799 MYS2_DICDI 2 761
SEQADV 4AE3 LEU A 762 UNP P08799 EXPRESSION TAG
SEQADV 4AE3 GLU A 763 UNP P08799 EXPRESSION TAG
SEQADV 4AE3 SER A 764 UNP P08799 EXPRESSION TAG
SEQADV 4AE3 ASN A 765 UNP P08799 EXPRESSION TAG
SEQADV 4AE3 GLU A 766 UNP P08799 EXPRESSION TAG
SEQADV 4AE3 PRO A 767 UNP P08799 EXPRESSION TAG
SEQADV 4AE3 PRO A 768 UNP P08799 EXPRESSION TAG
SEQADV 4AE3 MET A 769 UNP P08799 EXPRESSION TAG
SEQADV 4AE3 ASP A 770 UNP P08799 EXPRESSION TAG
SEQADV 4AE3 PHE A 771 UNP P08799 EXPRESSION TAG
SEQADV 4AE3 ASP A 772 UNP P08799 EXPRESSION TAG
SEQADV 4AE3 ASP A 773 UNP P08799 EXPRESSION TAG
SEQADV 4AE3 ASP A 774 UNP P08799 EXPRESSION TAG
SEQADV 4AE3 ILE A 775 UNP P08799 EXPRESSION TAG
SEQADV 4AE3 PRO A 776 UNP P08799 EXPRESSION TAG
SEQADV 4AE3 PHE A 777 UNP P08799 EXPRESSION TAG
SEQRES 1 A 776 ASN PRO ILE HIS ASP ARG THR SER ASP TYR HIS LYS TYR
SEQRES 2 A 776 LEU LYS VAL LYS GLN GLY ASP SER ASP LEU PHE LYS LEU
SEQRES 3 A 776 THR VAL SER ASP LYS ARG TYR ILE TRP TYR ASN PRO ASP
SEQRES 4 A 776 PRO LYS GLU ARG ASP SER TYR GLU CYS GLY GLU ILE VAL
SEQRES 5 A 776 SER GLU THR SER ASP SER PHE THR PHE LYS THR VAL ASP
SEQRES 6 A 776 GLY GLN ASP ARG GLN VAL LYS LYS ASP ASP ALA ASN GLN
SEQRES 7 A 776 ARG ASN PRO ILE LYS PHE ASP GLY VAL GLU ASP MET SER
SEQRES 8 A 776 GLU LEU SER TYR LEU ASN GLU PRO ALA VAL PHE HIS ASN
SEQRES 9 A 776 LEU ARG VAL ARG TYR ASN GLN ASP LEU ILE TYR THR TYR
SEQRES 10 A 776 SER GLY LEU PHE LEU VAL ALA VAL ASN PRO PHE LYS ARG
SEQRES 11 A 776 ILE PRO ILE TYR THR GLN GLU MET VAL ASP ILE PHE LYS
SEQRES 12 A 776 GLY ARG ARG ARG ASN GLU VAL ALA PRO HIS ILE PHE ALA
SEQRES 13 A 776 ILE SER ASP VAL ALA TYR ARG SER MET LEU ASP ASP ARG
SEQRES 14 A 776 GLN ASN GLN SER LEU LEU ILE THR GLY GLU SER GLY ALA
SEQRES 15 A 776 GLY LYS THR GLU ASN THR LYS LYS VAL ILE GLN TYR LEU
SEQRES 16 A 776 ALA SER VAL ALA GLY ARG ASN GLN ALA ASN GLY SER GLY
SEQRES 17 A 776 VAL LEU GLU GLN GLN ILE LEU GLN ALA ASN PRO ILE LEU
SEQRES 18 A 776 GLU ALA PHE GLY ASN ALA LYS THR THR ARG ASN ASN ASN
SEQRES 19 A 776 SER SER ARG PHE GLY LYS PHE ILE GLU ILE GLN PHE ASN
SEQRES 20 A 776 SER ALA GLY PHE ILE SER GLY ALA SER ILE GLN SER TYR
SEQRES 21 A 776 LEU LEU GLU LYS SER ARG VAL VAL PHE GLN SER GLU THR
SEQRES 22 A 776 GLU ARG ASN TYR HIS ILE PHE TYR GLN LEU LEU ALA GLY
SEQRES 23 A 776 ALA THR ALA GLU GLU LYS LYS ALA LEU HIS LEU ALA GLY
SEQRES 24 A 776 PRO GLU SER PHE ASN TYR LEU ASN GLN SER GLY CYS VAL
SEQRES 25 A 776 ASP ILE LYS GLY VAL SER ASP SER GLU GLU PHE LYS ILE
SEQRES 26 A 776 THR ARG GLN ALA MET ASP ILE VAL GLY PHE SER GLN GLU
SEQRES 27 A 776 GLU GLN MET SER ILE PHE LYS ILE ILE ALA GLY ILE LEU
SEQRES 28 A 776 HIS LEU GLY ASN ILE LYS PHE GLU LYS GLY ALA GLY GLU
SEQRES 29 A 776 GLY ALA VAL LEU LYS ASP LYS THR ALA LEU ASN ALA ALA
SEQRES 30 A 776 SER THR VAL PHE GLY VAL ASN PRO SER VAL LEU GLU LYS
SEQRES 31 A 776 ALA LEU MET GLU PRO ARG ILE LEU ALA GLY ARG ASP LEU
SEQRES 32 A 776 VAL ALA GLN HIS LEU ASN VAL GLU LYS SER SER SER SER
SEQRES 33 A 776 ARG ASP ALA LEU VAL LYS ALA LEU TYR GLY ARG LEU PHE
SEQRES 34 A 776 LEU TRP LEU VAL LYS LYS ILE ASN ASN VAL LEU CYS GLN
SEQRES 35 A 776 GLU ARG LYS ALA TYR PHE ILE GLY VAL LEU ASP ILE SER
SEQRES 36 A 776 GLY PHE GLU ILE PHE LYS VAL ASN SER PHE GLU GLN LEU
SEQRES 37 A 776 CYS ILE ASN TYR THR ASN GLU LYS LEU GLN GLN PHE PHE
SEQRES 38 A 776 ASN HIS HIS MET PHE LYS LEU GLU GLN GLU GLU TYR LEU
SEQRES 39 A 776 LYS GLU LYS ILE ASN TRP THR PHE ILE ASP PHE GLY LEU
SEQRES 40 A 776 ASP SER GLN ALA THR ILE ASP LEU ILE ASP GLY ARG GLN
SEQRES 41 A 776 PRO PRO GLY ILE LEU ALA LEU LEU ASP GLU GLN SER VAL
SEQRES 42 A 776 PHE PRO ASN ALA THR ASP ASN THR LEU ILE THR LYS LEU
SEQRES 43 A 776 HIS SER HIS PHE SER LYS LYS ASN ALA LYS TYR GLU GLU
SEQRES 44 A 776 PRO ARG PHE SER LYS THR GLU PHE GLY VAL THR HIS TYR
SEQRES 45 A 776 ALA GLY GLN VAL MET TYR GLU ILE GLN ASP TRP LEU GLU
SEQRES 46 A 776 LYS ASN LYS ASP PRO LEU GLN GLN ASP LEU GLU LEU CYS
SEQRES 47 A 776 PHE LYS ASP SER SER ASP ASN VAL VAL THR LYS LEU PHE
SEQRES 48 A 776 ASN ASP PRO ASN ILE ALA SER ARG ALA LYS LYS GLY ALA
SEQRES 49 A 776 ASN PHE ILE THR VAL ALA ALA GLN TYR LYS GLU GLN LEU
SEQRES 50 A 776 ALA SER LEU MET ALA THR LEU GLU THR THR ASN PRO HIS
SEQRES 51 A 776 PHE VAL ARG CYS ILE ILE PRO ASN ASN LYS GLN LEU PRO
SEQRES 52 A 776 ALA LYS LEU GLU ASP LYS VAL VAL LEU ASP GLN LEU ARG
SEQRES 53 A 776 CYS ASN GLY VAL LEU GLU GLY ILE ARG ILE THR ARG LYS
SEQRES 54 A 776 GLY PHE PRO ASN ARG ILE ILE TYR ALA ASP PHE VAL LYS
SEQRES 55 A 776 ARG TYR TYR LEU LEU ALA PRO ASN VAL PRO ARG ASP ALA
SEQRES 56 A 776 GLU ASP SER GLN LYS ALA THR ASP ALA VAL LEU LYS HIS
SEQRES 57 A 776 LEU ASN ILE ASP PRO GLU GLN TYR ARG PHE GLY ILE THR
SEQRES 58 A 776 LYS ILE PHE PHE ARG ALA GLY GLN LEU ALA ARG ILE GLU
SEQRES 59 A 776 GLU ALA ARG GLU GLN ARG LEU GLU SER ASN GLU PRO PRO
SEQRES 60 A 776 MET ASP PHE ASP ASP ASP ILE PRO PHE
HET AOV A1750 32
HET MG A1751 1
HET 27X A1752 20
HET 27X A1753 20
HET EDO A1754 4
HET EDO A1755 4
HET EDO A1756 4
HET EDO A1757 4
HETNAM AOV ADP ORTHOVANADATE
HETNAM MG MAGNESIUM ION
HETNAM 27X AMMOSAMIDE 272
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 2 AOV C10 H17 N5 O14 P2 V
FORMUL 3 MG MG 2+
FORMUL 4 27X 2(C13 H12 N4 O3)
FORMUL 6 EDO 4(C2 H6 O2)
FORMUL 10 HOH *439(H2 O)
HELIX 1 1 ASN A 2 ASP A 6 5 5
HELIX 2 2 SER A 9 LYS A 16 1 8
HELIX 3 3 ASP A 21 SER A 30 1 10
HELIX 4 4 ASP A 75 ALA A 77 5 3
HELIX 5 5 PRO A 82 ASP A 86 5 5
HELIX 6 6 MET A 91 LEU A 94 5 4
HELIX 7 7 ASN A 98 GLN A 112 1 15
HELIX 8 8 THR A 136 LYS A 144 1 9
HELIX 9 9 ARG A 147 VAL A 151 5 5
HELIX 10 10 HIS A 154 ARG A 170 1 17
HELIX 11 11 GLY A 184 ALA A 200 1 17
HELIX 12 12 GLY A 209 GLY A 226 1 18
HELIX 13 13 LYS A 265 PHE A 270 1 6
HELIX 14 14 TYR A 278 ALA A 288 1 11
HELIX 15 15 THR A 289 LEU A 296 1 8
HELIX 16 16 GLY A 300 PHE A 304 5 5
HELIX 17 17 SER A 319 GLY A 335 1 17
HELIX 18 18 SER A 337 ILE A 357 1 21
HELIX 19 19 LYS A 372 GLY A 383 1 12
HELIX 20 20 ASN A 385 GLU A 395 1 11
HELIX 21 21 ASN A 410 CYS A 442 1 33
HELIX 22 22 SER A 465 PHE A 487 1 23
HELIX 23 23 PHE A 487 GLU A 497 1 11
HELIX 24 24 SER A 510 GLY A 519 1 10
HELIX 25 25 GLY A 524 VAL A 534 1 11
HELIX 26 26 THR A 539 SER A 552 1 14
HELIX 27 27 ASP A 583 ASP A 590 1 8
HELIX 28 28 GLN A 593 ASP A 602 1 10
HELIX 29 29 ASP A 605 ASP A 614 1 10
HELIX 30 30 ASP A 614 SER A 619 1 6
HELIX 31 31 THR A 629 THR A 647 1 19
HELIX 32 32 GLU A 668 GLY A 680 1 13
HELIX 33 33 GLY A 680 GLY A 691 1 12
HELIX 34 34 GLN A 720 HIS A 729 1 10
HELIX 35 35 ASP A 733 GLU A 735 5 3
SHEET 1 AA 5 ASP A 69 LYS A 73 0
SHEET 2 AA 5 SER A 59 LYS A 63 -1 O PHE A 60 N VAL A 72
SHEET 3 AA 5 GLU A 48 GLU A 55 -1 O GLU A 51 N LYS A 63
SHEET 4 AA 5 TYR A 34 TYR A 37 -1 O ILE A 35 N GLY A 50
SHEET 5 AA 5 ASN A 78 GLN A 79 -1 O ASN A 78 N TRP A 36
SHEET 1 AB 7 TYR A 116 SER A 119 0
SHEET 2 AB 7 PHE A 122 VAL A 126 -1 O PHE A 122 N SER A 119
SHEET 3 AB 7 ASN A 649 ILE A 656 1 O PHE A 652 N LEU A 123
SHEET 4 AB 7 GLN A 173 THR A 178 1 O SER A 174 N HIS A 651
SHEET 5 AB 7 TYR A 448 ASP A 454 1 O PHE A 449 N GLN A 173
SHEET 6 AB 7 GLY A 240 PHE A 247 -1 O LYS A 241 N ASP A 454
SHEET 7 AB 7 ILE A 253 TYR A 261 -1 N SER A 254 O GLN A 246
SHEET 1 AC 2 ASN A 227 ALA A 228 0
SHEET 2 AC 2 SER A 236 SER A 237 -1 O SER A 236 N ALA A 228
SHEET 1 AD 2 GLU A 360 LYS A 361 0
SHEET 2 AD 2 ALA A 367 VAL A 368 -1 O VAL A 368 N GLU A 360
SHEET 1 AE 2 ARG A 397 ALA A 400 0
SHEET 2 AE 2 ASP A 403 ALA A 406 -1 O ASP A 403 N ALA A 400
SHEET 1 AF 3 TYR A 558 GLU A 559 0
SHEET 2 AF 3 GLU A 567 HIS A 572 -1 O GLY A 569 N GLU A 559
SHEET 3 AF 3 GLY A 575 GLU A 580 -1 O GLY A 575 N HIS A 572
SHEET 1 AG 2 LYS A 622 LYS A 623 0
SHEET 2 AG 2 ASN A 626 PHE A 627 -1 O ASN A 626 N LYS A 623
SHEET 1 AH 3 ASN A 694 ILE A 697 0
SHEET 2 AH 3 LYS A 743 PHE A 746 -1 O ILE A 744 N ILE A 696
SHEET 3 AH 3 TYR A 737 PHE A 739 -1 O ARG A 738 N PHE A 745
LINK OG1 THR A 186 MG MG A1751 1555 1555 2.56
LINK OG SER A 237 MG MG A1751 1555 1555 2.53
LINK O1B AOV A1750 MG MG A1751 1555 1555 2.42
LINK O1G AOV A1750 MG MG A1751 1555 1555 2.34
LINK MG MG A1751 O HOH A2163 1555 1555 2.41
LINK MG MG A1751 O HOH A2164 1555 1555 2.49
CISPEP 1 GLN A 521 PRO A 522 0 -5.83
SITE 1 AC1 25 ASN A 127 PRO A 128 PHE A 129 LYS A 130
SITE 2 AC1 25 ARG A 131 TYR A 135 GLU A 180 SER A 181
SITE 3 AC1 25 GLY A 182 ALA A 183 GLY A 184 LYS A 185
SITE 4 AC1 25 THR A 186 GLU A 187 ASN A 233 ASN A 235
SITE 5 AC1 25 SER A 236 SER A 237 SER A 456 GLY A 457
SITE 6 AC1 25 MG A1751 HOH A2124 HOH A2163 HOH A2166
SITE 7 AC1 25 HOH A2197
SITE 1 AC2 5 THR A 186 SER A 237 AOV A1750 HOH A2163
SITE 2 AC2 5 HOH A2164
SITE 1 AC3 12 LYS A 265 ALA A 424 GLY A 427 ARG A 428
SITE 2 AC3 12 LEU A 431 ASP A 590 PRO A 591 LEU A 592
SITE 3 AC3 12 ILE A 617 ALA A 618 SER A 619 HOH A2213
SITE 1 AC4 9 ASP A 515 ARG A 520 GLN A 521 PRO A 522
SITE 2 AC4 9 PRO A 523 GLY A 524 PHE A 551 ASN A 555
SITE 3 AC4 9 HOH A2336
SITE 1 AC5 6 GLU A 264 SER A 266 ARG A 267 PHE A 270
SITE 2 AC5 6 HOH A2211 HOH A2214
SITE 1 AC6 6 GLY A 240 LEU A 262 SER A 456 ILE A 471
SITE 2 AC6 6 THR A 474 TYR A 634
SITE 1 AC7 4 GLU A 180 ARG A 232 GLU A 459 ILE A 460
SITE 1 AC8 5 LYS A 477 ASP A 518 LEU A 638 ALA A 639
SITE 2 AC8 5 HOH A2318
CRYST1 88.050 145.520 153.830 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011357 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006872 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006501 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
