HEADER MOTOR PROTEIN 07-FEB-11 2Y8I
TITLE STRUCTURAL BASIS FOR THE ALLOSTERIC INTERFERENCE OF MYOSIN FUNCTION BY
TITLE 2 MUTANTS G680A AND G680V OF DICTYOSTELIUM MYOSIN-2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYOSIN-2 HEAVY CHAIN;
COMPND 3 CHAIN: X;
COMPND 4 FRAGMENT: MOTOR DOMAIN, RESIDUES 2-759;
COMPND 5 SYNONYM: MYOSIN II HEAVY CHAIN;
COMPND 6 EC: 3.6.4.1;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DICTYOSTELIUM DISCOIDEUM;
SOURCE 3 ORGANISM_COMMON: SLIME MOLD;
SOURCE 4 ORGANISM_TAXID: 44689;
SOURCE 5 EXPRESSION_SYSTEM: DICTYOSTELIUM DISCOIDEUM;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 44689;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PDXA-3H
KEYWDS MOTOR PROTEIN, ADP COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.PRELLER,S.BAUER,N.ADAMEK,S.FUJITA-BECKER,R.FEDOROV,M.A.GEEVES,
AUTHOR 2 D.J.MANSTEIN
REVDAT 5 20-DEC-23 2Y8I 1 REMARK
REVDAT 4 31-JUL-19 2Y8I 1 REMARK LINK
REVDAT 3 20-JUN-18 2Y8I 1 REMARK
REVDAT 2 12-OCT-11 2Y8I 1 JRNL
REVDAT 1 20-JUL-11 2Y8I 0
JRNL AUTH M.PRELLER,S.BAUER,N.ADAMEK,S.FUJITA-BECKER,R.FEDOROV,
JRNL AUTH 2 M.A.GEEVES,D.J.MANSTEIN
JRNL TITL STRUCTURAL BASIS FOR THE ALLOSTERIC INTERFERENCE OF MYOSIN
JRNL TITL 2 FUNCTION BY REACTIVE THIOL REGION MUTATIONS G680A AND G680V.
JRNL REF J.BIOL.CHEM. V. 286 35051 2011
JRNL REFN ISSN 0021-9258
JRNL PMID 21841195
JRNL DOI 10.1074/JBC.M111.265298
REMARK 2
REMARK 2 RESOLUTION. 3.13 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) : 3.13
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.22
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 3 NUMBER OF REFLECTIONS : 18481
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.249
REMARK 3 R VALUE (WORKING SET) : 0.245
REMARK 3 FREE R VALUE : 0.337
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 942
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 20.2159 - 5.9481 1.00 2761 131 0.2955 0.3863
REMARK 3 2 5.9481 - 4.7413 1.00 2618 148 0.2329 0.2760
REMARK 3 3 4.7413 - 4.1478 1.00 2595 140 0.1876 0.3040
REMARK 3 4 4.1478 - 3.7713 1.00 2552 159 0.2216 0.3100
REMARK 3 5 3.7713 - 3.5025 1.00 2559 143 0.2298 0.3738
REMARK 3 6 3.5025 - 3.2969 1.00 2563 130 0.2574 0.3580
REMARK 3 7 3.2969 - 3.1324 0.83 1891 91 0.2904 0.3800
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 : 1.17
REMARK 3 K_SOL : 0.15
REMARK 3 B_SOL : 30.70
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.560
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 34.320
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) : -5.07140
REMARK 3 B22 (A**2) : -9.77290
REMARK 3 B33 (A**2) : -3.98930
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 : 0.010 6237
REMARK 3 ANGLE : 1.360 8428
REMARK 3 CHIRALITY : 0.089 918
REMARK 3 PLANARITY : 0.004 1104
REMARK 3 DIHEDRAL : 23.988 2338
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 2Y8I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-FEB-11.
REMARK 100 THE DEPOSITION ID IS D_1290046913.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-JAN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9175
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20093
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.130
REMARK 200 RESOLUTION RANGE LOW (A) : 20.220
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4
REMARK 200 DATA REDUNDANCY : 11.10
REMARK 200 R MERGE (I) : 0.17000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.2300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.13
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.19
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.46000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.370
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1MMD
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 13% PEG 6000, 4% GLYCEROL., PH 7.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 X,-Y,-Z
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 -X,-Y+1/2,Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.90000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 90.25000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.90000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 90.25000
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: X
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 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN X, GLY 680 TO ALA
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 ASN X 206
REMARK 475 GLY X 207
REMARK 475 SER X 208
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 HOH X 2239 O HOH X 2240 0.53
REMARK 500 O HOH X 2237 O HOH X 2238 0.60
REMARK 500 O LYS X 554 O HOH X 2183 1.32
REMARK 500 CE1 PHE X 225 CD1 ILE X 280 1.36
REMARK 500 O ASN X 376 OG1 THR X 380 1.39
REMARK 500 ND2 ASN X 203 O ALA X 205 1.41
REMARK 500 O ARG X 689 N GLY X 691 1.42
REMARK 500 O ASN X 219 OE1 GLU X 223 1.54
REMARK 500 O LEU X 222 O HOH X 2082 1.55
REMARK 500 O GLN X 593 O HOH X 2193 1.65
REMARK 500 C LEU X 222 O HOH X 2082 1.65
REMARK 500 ND2 ASN X 679 O HOH X 2214 1.78
REMARK 500 O PHE X 85 CG1 VAL X 88 1.82
REMARK 500 C PHE X 85 O HOH X 2039 1.84
REMARK 500 ND2 ASN X 172 CD2 PHE X 449 1.84
REMARK 500 C LYS X 703 O HOH X 2219 1.89
REMARK 500 O THR X 64 N GLY X 67 1.91
REMARK 500 C LEU X 121 O HOH X 2048 1.92
REMARK 500 O GLN X 213 O HOH X 2079 1.94
REMARK 500 OG SER X 257 O HOH X 2095 1.95
REMARK 500 O ALA X 748 O HOH X 2251 1.95
REMARK 500 OD1 ASN X 172 CA TYR X 448 1.96
REMARK 500 CA ASP X 58 O HOH X 2029 1.96
REMARK 500 O SER X 640 OG1 THR X 644 1.96
REMARK 500 O ILE X 514 OD1 ASP X 518 1.96
REMARK 500 OG1 THR X 648 O HOH X 2207 1.97
REMARK 500 CG2 THR X 117 O HOH X 2046 1.97
REMARK 500 CB PHE X 746 O HOH X 2248 1.98
REMARK 500 CD1 PHE X 692 O HOH X 2243 1.98
REMARK 500 CG ASN X 172 O HOH X 2067 1.99
REMARK 500 CB ASP X 40 O HOH X 2022 2.00
REMARK 500 N GLY X 87 OD1 ASN X 105 2.00
REMARK 500 CD1 TRP X 432 NZ LYS X 610 2.00
REMARK 500 OD2 ASP X 141 O HOH X 2053 2.00
REMARK 500 O THR X 380 O HOH X 2132 2.01
REMARK 500 NH2 ARG X 170 O HOH X 2063 2.02
REMARK 500 C GLU X 360 O HOH X 2127 2.03
REMARK 500 C ASP X 58 O HOH X 2029 2.04
REMARK 500 O ASN X 541 OG1 THR X 545 2.04
REMARK 500 O VAL X 702 CD2 TYR X 706 2.04
REMARK 500 O HOH X 2216 O HOH X 2217 2.05
REMARK 500 CG ASN X 203 O ALA X 205 2.06
REMARK 500 CB GLN X 213 O HOH X 2078 2.06
REMARK 500 OD1 ASN X 172 N PHE X 449 2.06
REMARK 500 CG PHE X 692 O HOH X 2243 2.06
REMARK 500 O GLU X 360 O HOH X 2127 2.06
REMARK 500 N ASP X 58 O HOH X 2029 2.06
REMARK 500 C LYS X 372 O HOH X 2129 2.06
REMARK 500 C ASN X 219 OE1 GLU X 223 2.07
REMARK 500 O HOH X 2076 O HOH X 2077 2.07
REMARK 500
REMARK 500 THIS ENTRY HAS 96 CLOSE CONTACTS
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 NH1 ARG X 397 O ARG X 402 2556 1.10
REMARK 500 O GLN X 204 OE2 GLU X 273 1455 1.56
REMARK 500 CG ARG X 402 O HOH X 2255 3645 1.93
REMARK 500 O HOH X 2065 O HOH X 2149 1455 2.02
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 THR X 28 N - CA - C ANGL. DEV. = -20.9 DEGREES
REMARK 500 PRO X 39 CB - CA - C ANGL. DEV. = -14.1 DEGREES
REMARK 500 GLU X 55 N - CA - C ANGL. DEV. = -16.2 DEGREES
REMARK 500 ASP X 58 CB - CA - C ANGL. DEV. = -13.9 DEGREES
REMARK 500 ASN X 78 N - CA - C ANGL. DEV. = -17.1 DEGREES
REMARK 500 GLY X 120 N - CA - C ANGL. DEV. = -15.4 DEGREES
REMARK 500 GLY X 251 N - CA - C ANGL. DEV. = 18.1 DEGREES
REMARK 500 SER X 343 CB - CA - C ANGL. DEV. = -11.5 DEGREES
REMARK 500 GLY X 364 N - CA - C ANGL. DEV. = -18.3 DEGREES
REMARK 500 VAL X 534 CB - CA - C ANGL. DEV. = -13.9 DEGREES
REMARK 500 GLN X 594 N - CA - C ANGL. DEV. = 19.1 DEGREES
REMARK 500 ILE X 617 N - CA - C ANGL. DEV. = 19.0 DEGREES
REMARK 500 GLU X 683 CB - CA - C ANGL. DEV. = -13.5 DEGREES
REMARK 500 TYR X 698 CB - CA - C ANGL. DEV. = -12.4 DEGREES
REMARK 500 TYR X 705 CB - CA - C ANGL. DEV. = -12.3 DEGREES
REMARK 500 TYR X 705 N - CA - C ANGL. DEV. = 22.6 DEGREES
REMARK 500 TYR X 706 N - CA - CB ANGL. DEV. = -12.8 DEGREES
REMARK 500 ASN X 731 N - CA - C ANGL. DEV. = 17.2 DEGREES
REMARK 500 GLY X 749 N - CA - C ANGL. DEV. = 16.4 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 SER X 9 113.69 -35.90
REMARK 500 ASP X 10 -34.36 -36.83
REMARK 500 VAL X 17 3.45 -67.34
REMARK 500 LYS X 18 66.46 68.41
REMARK 500 LEU X 27 -102.58 -150.44
REMARK 500 PRO X 41 7.79 -61.47
REMARK 500 LYS X 42 -90.42 -118.93
REMARK 500 SER X 46 76.64 108.81
REMARK 500 SER X 54 114.47 -166.61
REMARK 500 LYS X 63 71.17 -166.97
REMARK 500 ASP X 86 131.24 -32.10
REMARK 500 ALA X 101 -6.43 -59.89
REMARK 500 ASP X 113 11.27 82.79
REMARK 500 PHE X 129 -12.52 81.79
REMARK 500 PHE X 143 5.48 -61.52
REMARK 500 ALA X 183 -12.89 -47.83
REMARK 500 VAL X 210 -59.28 -138.61
REMARK 500 ASN X 235 52.87 -118.69
REMARK 500 PHE X 239 -159.81 -130.79
REMARK 500 SER X 254 -86.09 -116.84
REMARK 500 GLN X 283 -52.72 -132.48
REMARK 500 LEU X 296 70.33 -154.25
REMARK 500 HIS X 297 113.68 9.81
REMARK 500 PRO X 301 69.52 -67.15
REMARK 500 GLU X 302 -20.65 -168.05
REMARK 500 VAL X 313 -68.26 -139.62
REMARK 500 ASN X 376 -7.27 -52.31
REMARK 500 VAL X 411 -16.02 -45.82
REMARK 500 LEU X 421 -9.43 -57.57
REMARK 500 TYR X 448 167.26 31.04
REMARK 500 ILE X 450 78.41 -119.99
REMARK 500 SER X 465 171.30 -57.71
REMARK 500 GLU X 467 -33.22 -39.36
REMARK 500 LYS X 498 10.34 80.85
REMARK 500 TRP X 501 173.51 -56.82
REMARK 500 PHE X 503 122.05 -31.21
REMARK 500 PHE X 506 -62.99 -142.29
REMARK 500 LEU X 508 104.96 69.61
REMARK 500 ASP X 530 0.38 -69.28
REMARK 500 ASP X 540 -73.43 -4.75
REMARK 500 LEU X 547 1.93 -65.55
REMARK 500 GLU X 559 96.70 -160.12
REMARK 500 PHE X 563 -63.12 -126.48
REMARK 500 TYR X 573 -0.78 -56.33
REMARK 500 LEU X 592 133.81 -173.97
REMARK 500 PRO X 615 -8.34 -48.83
REMARK 500 ARG X 620 -162.72 -115.60
REMARK 500 LYS X 623 -84.07 -179.28
REMARK 500 ALA X 625 -6.26 170.01
REMARK 500 GLU X 646 9.63 -66.33
REMARK 500
REMARK 500 THIS ENTRY HAS 63 RAMACHANDRAN OUTLIERS.
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 X1002 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR X 186 OG1
REMARK 620 2 SER X 237 OG 134.3
REMARK 620 3 ASP X 454 OD2 99.4 126.0
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP X 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 1002
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: 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: 1W9I RELATED DB: PDB
REMARK 900 MYOSIN II DICTYOSTELIUM DISCOIDEUM MOTOR DOMAIN S456Y BOUND WITH
REMARK 900 MGADP-BEFX
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: 1MND RELATED DB: PDB
REMARK 900 TRUNCATED HEAD OF MYOSIN FROM DICTYOSTELIUM DISCOIDEUM COMPLEXED
REMARK 900 WITH MGADP-ALF4
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: 2XEL RELATED DB: PDB
REMARK 900 MOLECULAR MECHANISM OF PENTACHLOROPSEUDILIN MEDIATED INHIBITION OF
REMARK 900 MYOSIN MOTOR ACTIVITY
REMARK 900 RELATED ID: 2JJ9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF MYOSIN-2 IN COMPLEX WITH ADP- METAVANADATE
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: 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: 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: 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: 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: 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: 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
DBREF 2Y8I X 2 759 UNP P08799 MYS2_DICDI 2 759
SEQADV 2Y8I ALA X 680 UNP P08799 GLY 680 ENGINEERED MUTATION
SEQRES 1 X 758 ASN PRO ILE HIS ASP ARG THR SER ASP TYR HIS LYS TYR
SEQRES 2 X 758 LEU LYS VAL LYS GLN GLY ASP SER ASP LEU PHE LYS LEU
SEQRES 3 X 758 THR VAL SER ASP LYS ARG TYR ILE TRP TYR ASN PRO ASP
SEQRES 4 X 758 PRO LYS GLU ARG ASP SER TYR GLU CYS GLY GLU ILE VAL
SEQRES 5 X 758 SER GLU THR SER ASP SER PHE THR PHE LYS THR VAL ASP
SEQRES 6 X 758 GLY GLN ASP ARG GLN VAL LYS LYS ASP ASP ALA ASN GLN
SEQRES 7 X 758 ARG ASN PRO ILE LYS PHE ASP GLY VAL GLU ASP MET SER
SEQRES 8 X 758 GLU LEU SER TYR LEU ASN GLU PRO ALA VAL PHE HIS ASN
SEQRES 9 X 758 LEU ARG VAL ARG TYR ASN GLN ASP LEU ILE TYR THR TYR
SEQRES 10 X 758 SER GLY LEU PHE LEU VAL ALA VAL ASN PRO PHE LYS ARG
SEQRES 11 X 758 ILE PRO ILE TYR THR GLN GLU MET VAL ASP ILE PHE LYS
SEQRES 12 X 758 GLY ARG ARG ARG ASN GLU VAL ALA PRO HIS ILE PHE ALA
SEQRES 13 X 758 ILE SER ASP VAL ALA TYR ARG SER MET LEU ASP ASP ARG
SEQRES 14 X 758 GLN ASN GLN SER LEU LEU ILE THR GLY GLU SER GLY ALA
SEQRES 15 X 758 GLY LYS THR GLU ASN THR LYS LYS VAL ILE GLN TYR LEU
SEQRES 16 X 758 ALA SER VAL ALA GLY ARG ASN GLN ALA ASN GLY SER GLY
SEQRES 17 X 758 VAL LEU GLU GLN GLN ILE LEU GLN ALA ASN PRO ILE LEU
SEQRES 18 X 758 GLU ALA PHE GLY ASN ALA LYS THR THR ARG ASN ASN ASN
SEQRES 19 X 758 SER SER ARG PHE GLY LYS PHE ILE GLU ILE GLN PHE ASN
SEQRES 20 X 758 SER ALA GLY PHE ILE SER GLY ALA SER ILE GLN SER TYR
SEQRES 21 X 758 LEU LEU GLU LYS SER ARG VAL VAL PHE GLN SER GLU THR
SEQRES 22 X 758 GLU ARG ASN TYR HIS ILE PHE TYR GLN LEU LEU ALA GLY
SEQRES 23 X 758 ALA THR ALA GLU GLU LYS LYS ALA LEU HIS LEU ALA GLY
SEQRES 24 X 758 PRO GLU SER PHE ASN TYR LEU ASN GLN SER GLY CYS VAL
SEQRES 25 X 758 ASP ILE LYS GLY VAL SER ASP SER GLU GLU PHE LYS ILE
SEQRES 26 X 758 THR ARG GLN ALA MET ASP ILE VAL GLY PHE SER GLN GLU
SEQRES 27 X 758 GLU GLN MET SER ILE PHE LYS ILE ILE ALA GLY ILE LEU
SEQRES 28 X 758 HIS LEU GLY ASN ILE LYS PHE GLU LYS GLY ALA GLY GLU
SEQRES 29 X 758 GLY ALA VAL LEU LYS ASP LYS THR ALA LEU ASN ALA ALA
SEQRES 30 X 758 SER THR VAL PHE GLY VAL ASN PRO SER VAL LEU GLU LYS
SEQRES 31 X 758 ALA LEU MET GLU PRO ARG ILE LEU ALA GLY ARG ASP LEU
SEQRES 32 X 758 VAL ALA GLN HIS LEU ASN VAL GLU LYS SER SER SER SER
SEQRES 33 X 758 ARG ASP ALA LEU VAL LYS ALA LEU TYR GLY ARG LEU PHE
SEQRES 34 X 758 LEU TRP LEU VAL LYS LYS ILE ASN ASN VAL LEU CYS GLN
SEQRES 35 X 758 GLU ARG LYS ALA TYR PHE ILE GLY VAL LEU ASP ILE SER
SEQRES 36 X 758 GLY PHE GLU ILE PHE LYS VAL ASN SER PHE GLU GLN LEU
SEQRES 37 X 758 CYS ILE ASN TYR THR ASN GLU LYS LEU GLN GLN PHE PHE
SEQRES 38 X 758 ASN HIS HIS MET PHE LYS LEU GLU GLN GLU GLU TYR LEU
SEQRES 39 X 758 LYS GLU LYS ILE ASN TRP THR PHE ILE ASP PHE GLY LEU
SEQRES 40 X 758 ASP SER GLN ALA THR ILE ASP LEU ILE ASP GLY ARG GLN
SEQRES 41 X 758 PRO PRO GLY ILE LEU ALA LEU LEU ASP GLU GLN SER VAL
SEQRES 42 X 758 PHE PRO ASN ALA THR ASP ASN THR LEU ILE THR LYS LEU
SEQRES 43 X 758 HIS SER HIS PHE SER LYS LYS ASN ALA LYS TYR GLU GLU
SEQRES 44 X 758 PRO ARG PHE SER LYS THR GLU PHE GLY VAL THR HIS TYR
SEQRES 45 X 758 ALA GLY GLN VAL MET TYR GLU ILE GLN ASP TRP LEU GLU
SEQRES 46 X 758 LYS ASN LYS ASP PRO LEU GLN GLN ASP LEU GLU LEU CYS
SEQRES 47 X 758 PHE LYS ASP SER SER ASP ASN VAL VAL THR LYS LEU PHE
SEQRES 48 X 758 ASN ASP PRO ASN ILE ALA SER ARG ALA LYS LYS GLY ALA
SEQRES 49 X 758 ASN PHE ILE THR VAL ALA ALA GLN TYR LYS GLU GLN LEU
SEQRES 50 X 758 ALA SER LEU MET ALA THR LEU GLU THR THR ASN PRO HIS
SEQRES 51 X 758 PHE VAL ARG CYS ILE ILE PRO ASN ASN LYS GLN LEU PRO
SEQRES 52 X 758 ALA LYS LEU GLU ASP LYS VAL VAL LEU ASP GLN LEU ARG
SEQRES 53 X 758 CYS ASN ALA VAL LEU GLU GLY ILE ARG ILE THR ARG LYS
SEQRES 54 X 758 GLY PHE PRO ASN ARG ILE ILE TYR ALA ASP PHE VAL LYS
SEQRES 55 X 758 ARG TYR TYR LEU LEU ALA PRO ASN VAL PRO ARG ASP ALA
SEQRES 56 X 758 GLU ASP SER GLN LYS ALA THR ASP ALA VAL LEU LYS HIS
SEQRES 57 X 758 LEU ASN ILE ASP PRO GLU GLN TYR ARG PHE GLY ILE THR
SEQRES 58 X 758 LYS ILE PHE PHE ARG ALA GLY GLN LEU ALA ARG ILE GLU
SEQRES 59 X 758 GLU ALA ARG GLU
HET ADP X1001 27
HET MG X1002 1
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
FORMUL 2 ADP C10 H15 N5 O10 P2
FORMUL 3 MG MG 2+
FORMUL 4 HOH *258(H2 O)
HELIX 1 1 ASP X 10 LYS X 16 1 7
HELIX 2 2 ASP X 90 LEU X 94 5 5
HELIX 3 3 ASN X 98 GLN X 112 1 15
HELIX 4 4 THR X 136 LYS X 144 1 9
HELIX 5 5 HIS X 154 ARG X 170 1 17
HELIX 6 6 LYS X 185 LEU X 196 1 12
HELIX 7 7 VAL X 210 GLN X 217 1 8
HELIX 8 8 ALA X 218 PHE X 225 1 8
HELIX 9 9 SER X 266 PHE X 270 5 5
HELIX 10 10 TYR X 278 GLN X 283 5 6
HELIX 11 11 SER X 319 VAL X 334 1 16
HELIX 12 12 SER X 337 ILE X 357 1 21
HELIX 13 13 ALA X 374 GLY X 383 1 10
HELIX 14 14 ASN X 385 GLU X 395 1 11
HELIX 15 15 GLU X 412 CYS X 442 1 31
HELIX 16 16 SER X 465 GLU X 490 1 26
HELIX 17 17 SER X 510 GLY X 519 1 10
HELIX 18 18 GLY X 524 SER X 533 1 10
HELIX 19 19 THR X 539 HIS X 550 1 12
HELIX 20 20 ASP X 583 LYS X 589 1 7
HELIX 21 21 ASP X 595 LYS X 601 1 7
HELIX 22 22 VAL X 608 ASP X 614 1 7
HELIX 23 23 THR X 629 ALA X 643 1 15
HELIX 24 24 VAL X 671 ARG X 677 1 7
HELIX 25 25 ASN X 679 GLY X 684 1 6
HELIX 26 26 ILE X 685 LYS X 690 1 6
HELIX 27 27 ASP X 700 TYR X 705 1 6
HELIX 28 28 ASP X 718 THR X 723 1 6
HELIX 29 29 ASP X 724 LEU X 727 5 4
HELIX 30 30 ASP X 733 TYR X 737 5 5
HELIX 31 31 LEU X 751 GLU X 756 1 6
SHEET 1 XA 3 GLU X 48 GLU X 51 0
SHEET 2 XA 3 TYR X 34 TYR X 37 -1 O ILE X 35 N GLY X 50
SHEET 3 XA 3 ASN X 78 GLN X 79 -1 O ASN X 78 N TRP X 36
SHEET 1 XB 7 TYR X 116 TYR X 118 0
SHEET 2 XB 7 LEU X 123 VAL X 126 -1 O VAL X 124 N THR X 117
SHEET 3 XB 7 ASN X 649 ILE X 656 1 O PHE X 652 N LEU X 123
SHEET 4 XB 7 GLN X 173 GLY X 179 1 O SER X 174 N HIS X 651
SHEET 5 XB 7 ALA X 447 ASP X 454 1 O PHE X 449 N GLN X 173
SHEET 6 XB 7 ILE X 245 PHE X 247 -1 O ILE X 245 N ILE X 450
SHEET 7 XB 7 ILE X 253 ALA X 256 -1 N SER X 254 O GLN X 246
SHEET 1 XC 6 TYR X 116 TYR X 118 0
SHEET 2 XC 6 LEU X 123 VAL X 126 -1 O VAL X 124 N THR X 117
SHEET 3 XC 6 ASN X 649 ILE X 656 1 O PHE X 652 N LEU X 123
SHEET 4 XC 6 GLN X 173 GLY X 179 1 O SER X 174 N HIS X 651
SHEET 5 XC 6 ALA X 447 ASP X 454 1 O PHE X 449 N GLN X 173
SHEET 6 XC 6 LYS X 241 ILE X 243 -1 O LYS X 241 N ASP X 454
SHEET 1 XD 2 ASN X 227 THR X 230 0
SHEET 2 XD 2 ASN X 233 SER X 237 -1 O ASN X 233 N THR X 230
SHEET 1 XE 2 GLU X 360 LYS X 361 0
SHEET 2 XE 2 ALA X 367 VAL X 368 -1 O VAL X 368 N GLU X 360
SHEET 1 XF 2 ARG X 397 ALA X 400 0
SHEET 2 XF 2 ASP X 403 ALA X 406 -1 O ASP X 403 N ALA X 400
SHEET 1 XG 2 PHE X 568 HIS X 572 0
SHEET 2 XG 2 GLY X 575 TYR X 579 -1 O GLY X 575 N HIS X 572
LINK OG1 THR X 186 MG MG X1002 1555 1555 1.83
LINK OG SER X 237 MG MG X1002 1555 1555 2.72
LINK OD2 ASP X 454 MG MG X1002 1555 1555 2.78
CISPEP 1 GLN X 521 PRO X 522 0 0.07
SITE 1 AC1 15 ASN X 127 PRO X 128 LYS X 130 TYR X 135
SITE 2 AC1 15 GLY X 182 GLY X 184 LYS X 185 THR X 186
SITE 3 AC1 15 GLU X 187 ASN X 233 MG X1002 HOH X2068
SITE 4 AC1 15 HOH X2256 HOH X2257 HOH X2258
SITE 1 AC2 4 THR X 186 SER X 237 ASP X 454 ADP X1001
CRYST1 55.000 105.800 180.500 90.00 90.00 90.00 P 2 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 0.018182 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009452 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005540 0.00000
(ATOM LINES ARE NOT SHOWN.)
END