HEADER CONTRACTILE PROTEIN 26-APR-02 1LKX
TITLE MOTOR DOMAIN OF MYOE, A CLASS-I MYOSIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYOSIN IE HEAVY CHAIN;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: MOTOR DOMAIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: DICTYOSTELIUM DISCOIDEUM;
SOURCE 3 ORGANISM_TAXID: 44689;
SOURCE 4 EXPRESSION_SYSTEM: DICTYOSTELIUM DISCOIDEUM;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 44689;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PDXA-3H
KEYWDS MYOSIN MOTOR DOMAIN, LEVER ARM, CONVERTER DOMAIN, CONTRACTILE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.KOLLMAR,U.DURRWANG,W.KLICHE,D.J.MANSTEIN,F.J.KULL
REVDAT 4 14-FEB-24 1LKX 1 REMARK LINK
REVDAT 3 11-OCT-17 1LKX 1 REMARK
REVDAT 2 24-FEB-09 1LKX 1 VERSN
REVDAT 1 26-JUN-02 1LKX 0
JRNL AUTH M.KOLLMAR,U.DURRWANG,W.KLICHE,D.J.MANSTEIN,F.J.KULL
JRNL TITL CRYSTAL STRUCTURE OF THE MOTOR DOMAIN OF A CLASS-I MYOSIN.
JRNL REF EMBO J. V. 21 2517 2002
JRNL REFN ISSN 0261-4189
JRNL PMID 12032065
JRNL DOI 10.1093/EMBOJ/21.11.2517
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : -3.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 54968
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 5000
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 21069
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 132
REMARK 3 SOLVENT ATOMS : 64
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.008
REMARK 3 BOND ANGLES (DEGREES) : 1.376
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 21.22
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1LKX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUN-02.
REMARK 100 THE DEPOSITION ID IS D_1000016039.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JAN-00; NULL
REMARK 200 TEMPERATURE (KELVIN) : 80; NULL
REMARK 200 PH : 7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG; ESRF
REMARK 200 BEAMLINE : BW7B; ID13
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.8424; 0.9600
REMARK 200 MONOCHROMATOR : NULL; NULL
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; NULL
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH; NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MAR
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 54968
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CNS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.76
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 11% PEG 8K, PH 7.2, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 289K
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 71.83350
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, 3, 4
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 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 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 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 1
REMARK 465 ILE A 2
REMARK 465 PRO A 3
REMARK 465 LYS A 4
REMARK 465 THR A 5
REMARK 465 LYS A 6
REMARK 465 ALA A 7
REMARK 465 GLU A 8
REMARK 465 ARG A 288
REMARK 465 THR A 289
REMARK 465 GLY A 290
REMARK 465 THR A 291
REMARK 465 ILE A 325
REMARK 465 SER A 326
REMARK 465 THR A 327
REMARK 465 GLY A 328
REMARK 465 VAL A 329
REMARK 465 GLY A 330
REMARK 465 LYS A 331
REMARK 465 ARG A 332
REMARK 465 CYS A 333
REMARK 465 SER A 334
REMARK 465 PRO A 549
REMARK 465 THR A 550
REMARK 465 ARG A 551
REMARK 465 PRO A 552
REMARK 465 GLU A 553
REMARK 465 ASP A 554
REMARK 465 SER A 555
REMARK 465 LYS A 556
REMARK 465 LYS A 557
REMARK 465 ARG A 558
REMARK 465 PRO A 559
REMARK 465 THR A 644
REMARK 465 TRP A 645
REMARK 465 PRO A 646
REMARK 465 SER A 647
REMARK 465 PHE A 648
REMARK 465 ASN A 649
REMARK 465 GLY A 650
REMARK 465 THR A 651
REMARK 465 ALA A 652
REMARK 465 GLU A 693
REMARK 465 LEU A 694
REMARK 465 GLU A 695
REMARK 465 MET A 696
REMARK 465 PRO A 697
REMARK 465 MET B 1
REMARK 465 ILE B 2
REMARK 465 PRO B 3
REMARK 465 LYS B 4
REMARK 465 THR B 5
REMARK 465 LYS B 6
REMARK 465 ALA B 7
REMARK 465 GLU B 8
REMARK 465 ARG B 288
REMARK 465 THR B 289
REMARK 465 GLY B 290
REMARK 465 THR B 291
REMARK 465 ILE B 325
REMARK 465 SER B 326
REMARK 465 THR B 327
REMARK 465 GLY B 328
REMARK 465 VAL B 329
REMARK 465 GLY B 330
REMARK 465 LYS B 331
REMARK 465 ARG B 332
REMARK 465 CYS B 333
REMARK 465 SER B 334
REMARK 465 PRO B 549
REMARK 465 THR B 550
REMARK 465 ARG B 551
REMARK 465 PRO B 552
REMARK 465 GLU B 553
REMARK 465 ASP B 554
REMARK 465 SER B 555
REMARK 465 LYS B 556
REMARK 465 LYS B 557
REMARK 465 ARG B 558
REMARK 465 PRO B 559
REMARK 465 LYS B 643
REMARK 465 THR B 644
REMARK 465 TRP B 645
REMARK 465 PRO B 646
REMARK 465 SER B 647
REMARK 465 PHE B 648
REMARK 465 ASN B 649
REMARK 465 GLY B 650
REMARK 465 THR B 651
REMARK 465 GLU B 693
REMARK 465 LEU B 694
REMARK 465 GLU B 695
REMARK 465 MET B 696
REMARK 465 PRO B 697
REMARK 465 MET C 1
REMARK 465 ILE C 2
REMARK 465 PRO C 3
REMARK 465 LYS C 4
REMARK 465 THR C 5
REMARK 465 LYS C 6
REMARK 465 ALA C 7
REMARK 465 GLU C 8
REMARK 465 ILE C 325
REMARK 465 SER C 326
REMARK 465 THR C 327
REMARK 465 GLY C 328
REMARK 465 VAL C 329
REMARK 465 GLY C 330
REMARK 465 LYS C 331
REMARK 465 ARG C 332
REMARK 465 CYS C 333
REMARK 465 SER C 334
REMARK 465 MET D 1
REMARK 465 ILE D 2
REMARK 465 PRO D 3
REMARK 465 LYS D 4
REMARK 465 THR D 5
REMARK 465 LYS D 6
REMARK 465 ALA D 7
REMARK 465 GLU D 8
REMARK 465 ILE D 325
REMARK 465 SER D 326
REMARK 465 THR D 327
REMARK 465 GLY D 328
REMARK 465 VAL D 329
REMARK 465 GLY D 330
REMARK 465 LYS D 331
REMARK 465 ARG D 332
REMARK 465 CYS D 333
REMARK 465 SER D 334
REMARK 465 PRO D 549
REMARK 465 THR D 550
REMARK 465 ARG D 551
REMARK 465 PRO D 552
REMARK 465 GLU D 553
REMARK 465 ASP D 554
REMARK 465 SER D 555
REMARK 465 LYS D 556
REMARK 465 LYS D 557
REMARK 465 ARG D 558
REMARK 465 PRO D 559
REMARK 465 THR D 644
REMARK 465 TRP D 645
REMARK 465 PRO D 646
REMARK 465 SER D 647
REMARK 465 PHE D 648
REMARK 465 ASN D 649
REMARK 465 GLY D 650
REMARK 465 PRO D 697
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 ND2 ASN A 156 O3' ADP A 791 2.13
REMARK 500 O THR C 375 OG1 THR D 376 2.17
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 LYS A 483 N - CA - C ANGL. DEV. = -17.7 DEGREES
REMARK 500 LYS B 483 N - CA - C ANGL. DEV. = -17.3 DEGREES
REMARK 500 LYS C 483 N - CA - C ANGL. DEV. = -17.2 DEGREES
REMARK 500 PRO C 682 C - N - CA ANGL. DEV. = 11.1 DEGREES
REMARK 500 LYS D 483 N - CA - C ANGL. DEV. = -17.5 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 12 112.64 60.30
REMARK 500 ASN A 36 70.45 -110.93
REMARK 500 ILE A 41 49.92 -146.16
REMARK 500 ASP A 43 -27.54 71.99
REMARK 500 LYS A 52 158.70 176.08
REMARK 500 ASN A 55 66.55 -65.84
REMARK 500 PHE A 120 -60.91 -179.14
REMARK 500 SER A 123 -143.16 -82.41
REMARK 500 ASN A 124 -91.03 -179.06
REMARK 500 SER A 126 95.07 -26.87
REMARK 500 SER A 157 106.00 36.26
REMARK 500 LEU A 183 106.62 -6.16
REMARK 500 PRO A 221 82.13 -63.33
REMARK 500 ASN A 222 104.05 179.35
REMARK 500 CYS A 234 118.98 -172.49
REMARK 500 ALA A 285 83.80 -59.71
REMARK 500 GLU A 286 -36.37 -135.08
REMARK 500 SER A 297 -68.49 -95.45
REMARK 500 ASP A 298 64.40 -67.59
REMARK 500 ARG A 323 -147.30 -102.63
REMARK 500 THR A 376 -86.55 -51.86
REMARK 500 SER A 397 -161.81 -121.17
REMARK 500 LEU A 417 -87.77 -86.94
REMARK 500 TYR A 426 -38.93 -34.96
REMARK 500 GLU A 432 110.23 -11.15
REMARK 500 ASN A 435 102.37 -46.53
REMARK 500 PHE A 439 -116.47 -8.07
REMARK 500 LYS A 442 4.48 49.48
REMARK 500 PRO A 443 2.77 -69.87
REMARK 500 LEU A 447 -39.89 -38.22
REMARK 500 GLU A 449 50.47 -165.03
REMARK 500 LYS A 450 -71.06 -149.05
REMARK 500 PRO A 452 110.77 -31.93
REMARK 500 ILE A 453 56.33 83.93
REMARK 500 ALA A 466 -6.41 -57.19
REMARK 500 PHE A 481 -140.50 -118.29
REMARK 500 LYS A 483 -2.41 173.17
REMARK 500 PRO A 485 -176.91 -68.53
REMARK 500 HIS A 486 -15.77 72.92
REMARK 500 VAL A 491 -78.30 -49.05
REMARK 500 LYS A 494 73.34 -37.54
REMARK 500 SER A 537 1.08 -69.29
REMARK 500 THR A 561 125.14 9.02
REMARK 500 ASP A 600 77.04 -104.38
REMARK 500 GLU A 601 -68.56 -23.15
REMARK 500 GLU A 615 1.89 -68.89
REMARK 500 ARG A 621 -85.77 -69.30
REMARK 500 ALA A 622 -36.46 -35.35
REMARK 500 ALA A 625 -81.22 -50.12
REMARK 500 TYR A 630 -72.31 -69.41
REMARK 500
REMARK 500 THIS ENTRY HAS 248 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 A 790 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 108 OG1
REMARK 620 2 SER A 158 OG 74.9
REMARK 620 3 ADP A 791 O2A 107.4 151.1
REMARK 620 4 ADP A 791 O1B 79.7 134.6 72.7
REMARK 620 5 VO4 A 792 O2 124.4 76.7 120.1 87.9
REMARK 620 6 HOH A 805 O 68.9 76.1 132.4 59.8 58.3
REMARK 620 7 HOH A 808 O 125.8 90.2 64.6 134.9 100.9 156.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 VO4 A 792 V
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP A 791 O2B
REMARK 620 2 VO4 A 792 O1 95.6
REMARK 620 3 VO4 A 792 O2 96.0 125.2
REMARK 620 4 VO4 A 792 O3 98.8 115.1 115.7
REMARK 620 5 VO4 A 792 O4 173.8 80.3 82.8 87.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 793 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 108 OG1
REMARK 620 2 SER B 158 OG 67.0
REMARK 620 3 ADP B 794 O1B 77.7 124.1
REMARK 620 4 ADP B 794 O2A 102.4 143.4 84.2
REMARK 620 5 VO4 B 795 O3 116.7 74.4 85.5 136.2
REMARK 620 6 HOH B 796 O 118.7 82.5 153.4 72.2 102.8
REMARK 620 7 HOH B 797 O 60.2 62.6 62.5 144.3 57.9 142.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 VO4 B 795 V
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP B 794 O2B
REMARK 620 2 VO4 B 795 O1 88.1
REMARK 620 3 VO4 B 795 O2 100.6 123.9
REMARK 620 4 VO4 B 795 O3 101.7 116.3 115.7
REMARK 620 5 VO4 B 795 O4 171.4 83.4 83.4 83.1
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG C 890 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR C 108 OG1
REMARK 620 2 SER C 158 OG 71.4
REMARK 620 3 ADP C 891 O2B 142.2 141.3
REMARK 620 4 ADP C 891 O1B 85.7 150.1 56.7
REMARK 620 5 VO4 C 892 O2 150.0 82.2 59.6 112.9
REMARK 620 6 HOH C 897 O 109.0 89.2 92.9 117.0 84.1
REMARK 620 7 HOH C 909 O 69.6 81.3 93.5 72.6 92.9 170.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 VO4 C 892 V
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP C 891 O2B
REMARK 620 2 VO4 C 892 O1 101.2
REMARK 620 3 VO4 C 892 O2 95.0 122.9
REMARK 620 4 VO4 C 892 O3 92.6 115.3 118.2
REMARK 620 5 VO4 C 892 O4 174.3 84.5 81.9 84.7
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG D 893 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR D 108 OG1
REMARK 620 2 SER D 158 OG 70.3
REMARK 620 3 ADP D 894 O3B 130.2 141.2
REMARK 620 4 ADP D 894 O2B 79.2 142.3 53.2
REMARK 620 5 VO4 D 895 O3 136.3 81.7 61.0 107.6
REMARK 620 6 HOH D 906 O 59.9 76.2 87.6 69.5 81.6
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 VO4 D 895 V
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ADP D 894 O3B
REMARK 620 2 VO4 D 895 O1 97.0
REMARK 620 3 VO4 D 895 O2 98.1 122.4
REMARK 620 4 VO4 D 895 O3 94.2 117.2 116.7
REMARK 620 5 VO4 D 895 O4 177.0 84.0 83.7 82.8
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 MG A 790
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VO4 A 792
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 793
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VO4 B 795
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 890
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VO4 C 892
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 893
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VO4 D 895
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 791
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 794
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 891
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP D 894
REMARK 999
REMARK 999 SEQUENCE AUTHOR STATES THE PUBLISHED SEQUENCE FOR DISTY MYOE IS
REMARK 999 INCORRECT IN A NUMBER OF PLACES. THE AUTHORS BELIEVE THEIR
REMARK 999 SEQUENCE TO BE MORE ACCURATE. THEY HAVE IDENTIFIED THE FOLLOWING
REMARK 999 CHANGES IN THEIR SEQUENCE/STRUCTURE FROM THE PUBLISHED ONE. THE
REMARK 999 DERIVED SEQUENCE OF MYOE WAS DIFFERENT FROM THE PUBLISHED
REMARK 999 SEQUENCE (URRUTIA ET AL., 1993, ACC. NR. L06805) IN 25 PLACES:
REMARK 999 WHILE SOME CHANGES CONCERNED NON-CONSERVED RESIDUES, ESPECIALLY
REMARK 999 IN THE REGIONS WHERE ADDITIONAL RESIDUES OR DELETIONS WERE FOUND,
REMARK 999 THE DERIVED SEQUENCE WAS IN BETTER AGREEMENT WITH THE AMINO
REMARK 999 ACID ALIGNMENT OF THE DICTYOSTELIUM MYOSINS. IN ONE REGION, A
REMARK 999 TEN RESIDUE SURFACE LOOP WAS FOUND TO BE COMPLETELY DIFFERENT.
REMARK 999 IN DETAIL, THE SEQUENCE CONTAINED THE FOLLOWING MODIFICATIONS
REMARK 999 COMPARED TO THE PUBLISHED ONE: D26E, R48T, I77M, I137L, R138D,
REMARK 999 F139 ABSENT, 140 ABSENT, N215D, L371I, S372I, I373N, V374C,
REMARK 999 H375T, R376T, G378K, T379G, P380 INSERTED, V427 INSERTED, R428
REMARK 999 INSERTED, K429E, N440 INSERTED, N498I, D604V, I681N, R683T. THE
REMARK 999 AUTHORS STATE THEIR SEQUENCE COMPLETELY AGREES WITH THE FRAGMENT
REMARK 999 (AA270-1003) OBTAINED FROM THE DICTY GENOME SEQUENCING PROJECT.
DBREF 1LKX A 1 697 UNP Q03479 MYOE_DICDI 1 697
DBREF 1LKX B 1 697 UNP Q03479 MYOE_DICDI 1 697
DBREF 1LKX C 1 697 UNP Q03479 MYOE_DICDI 1 697
DBREF 1LKX D 1 697 UNP Q03479 MYOE_DICDI 1 697
SEQADV 1LKX GLU A 26 UNP Q03479 ASP 26 SEE REMARK 999
SEQADV 1LKX THR A 48 UNP Q03479 ARG 48 SEE REMARK 999
SEQADV 1LKX MET A 77 UNP Q03479 ILE 77 SEE REMARK 999
SEQADV 1LKX A UNP Q03479 ILE 137 SEE REMARK 999
SEQADV 1LKX A UNP Q03479 ARG 138 SEE REMARK 999
SEQADV 1LKX LEU A 137 UNP Q03479 PHE 139 SEE REMARK 999
SEQADV 1LKX ASP A 138 UNP Q03479 GLN 140 SEE REMARK 999
SEQADV 1LKX ASP A 215 UNP Q03479 ASN 217 SEE REMARK 999
SEQADV 1LKX ILE A 371 UNP Q03479 LEU 373 SEE REMARK 999
SEQADV 1LKX ILE A 372 UNP Q03479 SER 374 SEE REMARK 999
SEQADV 1LKX ASN A 373 UNP Q03479 ILE 375 SEE REMARK 999
SEQADV 1LKX CYS A 374 UNP Q03479 VAL 376 SEE REMARK 999
SEQADV 1LKX THR A 375 UNP Q03479 HIS 377 SEE REMARK 999
SEQADV 1LKX THR A 376 UNP Q03479 ARG 378 SEE REMARK 999
SEQADV 1LKX LYS A 378 UNP Q03479 SEE REMARK 999
SEQADV 1LKX PRO A 380 UNP Q03479 THR 381 SEE REMARK 999
SEQADV 1LKX VAL A 427 UNP Q03479 SEE REMARK 999
SEQADV 1LKX ARG A 428 UNP Q03479 SEE REMARK 999
SEQADV 1LKX GLU A 429 UNP Q03479 LYS 428 SEE REMARK 999
SEQADV 1LKX ASN A 440 UNP Q03479 SEE REMARK 999
SEQADV 1LKX ILE A 498 UNP Q03479 ASN 496 SEE REMARK 999
SEQADV 1LKX VAL A 604 UNP Q03479 ASP 602 SEE REMARK 999
SEQADV 1LKX ASN A 681 UNP Q03479 ILE 679 SEE REMARK 999
SEQADV 1LKX THR A 683 UNP Q03479 ARG 681 SEE REMARK 999
SEQADV 1LKX GLU B 26 UNP Q03479 ASP 26 SEE REMARK 999
SEQADV 1LKX THR B 48 UNP Q03479 ARG 48 SEE REMARK 999
SEQADV 1LKX MET B 77 UNP Q03479 ILE 77 SEE REMARK 999
SEQADV 1LKX B UNP Q03479 ILE 137 SEE REMARK 999
SEQADV 1LKX B UNP Q03479 ARG 138 SEE REMARK 999
SEQADV 1LKX LEU B 137 UNP Q03479 PHE 139 SEE REMARK 999
SEQADV 1LKX ASP B 138 UNP Q03479 GLN 140 SEE REMARK 999
SEQADV 1LKX ASP B 215 UNP Q03479 ASN 217 SEE REMARK 999
SEQADV 1LKX ILE B 371 UNP Q03479 LEU 373 SEE REMARK 999
SEQADV 1LKX ILE B 372 UNP Q03479 SER 374 SEE REMARK 999
SEQADV 1LKX ASN B 373 UNP Q03479 ILE 375 SEE REMARK 999
SEQADV 1LKX CYS B 374 UNP Q03479 VAL 376 SEE REMARK 999
SEQADV 1LKX THR B 375 UNP Q03479 HIS 377 SEE REMARK 999
SEQADV 1LKX THR B 376 UNP Q03479 ARG 378 SEE REMARK 999
SEQADV 1LKX LYS B 378 UNP Q03479 SEE REMARK 999
SEQADV 1LKX PRO B 380 UNP Q03479 THR 381 SEE REMARK 999
SEQADV 1LKX VAL B 427 UNP Q03479 SEE REMARK 999
SEQADV 1LKX ARG B 428 UNP Q03479 SEE REMARK 999
SEQADV 1LKX GLU B 429 UNP Q03479 LYS 428 SEE REMARK 999
SEQADV 1LKX ASN B 440 UNP Q03479 SEE REMARK 999
SEQADV 1LKX ILE B 498 UNP Q03479 ASN 496 SEE REMARK 999
SEQADV 1LKX VAL B 604 UNP Q03479 ASP 602 SEE REMARK 999
SEQADV 1LKX ASN B 681 UNP Q03479 ILE 679 SEE REMARK 999
SEQADV 1LKX THR B 683 UNP Q03479 ARG 681 SEE REMARK 999
SEQADV 1LKX GLU C 26 UNP Q03479 ASP 26 SEE REMARK 999
SEQADV 1LKX THR C 48 UNP Q03479 ARG 48 SEE REMARK 999
SEQADV 1LKX MET C 77 UNP Q03479 ILE 77 SEE REMARK 999
SEQADV 1LKX C UNP Q03479 ILE 137 SEE REMARK 999
SEQADV 1LKX C UNP Q03479 ARG 138 SEE REMARK 999
SEQADV 1LKX LEU C 137 UNP Q03479 PHE 139 SEE REMARK 999
SEQADV 1LKX ASP C 138 UNP Q03479 GLN 140 SEE REMARK 999
SEQADV 1LKX ASP C 215 UNP Q03479 ASN 217 SEE REMARK 999
SEQADV 1LKX ILE C 371 UNP Q03479 LEU 373 SEE REMARK 999
SEQADV 1LKX ILE C 372 UNP Q03479 SER 374 SEE REMARK 999
SEQADV 1LKX ASN C 373 UNP Q03479 ILE 375 SEE REMARK 999
SEQADV 1LKX CYS C 374 UNP Q03479 VAL 376 SEE REMARK 999
SEQADV 1LKX THR C 375 UNP Q03479 HIS 377 SEE REMARK 999
SEQADV 1LKX THR C 376 UNP Q03479 ARG 378 SEE REMARK 999
SEQADV 1LKX LYS C 378 UNP Q03479 SEE REMARK 999
SEQADV 1LKX PRO C 380 UNP Q03479 THR 381 SEE REMARK 999
SEQADV 1LKX VAL C 427 UNP Q03479 SEE REMARK 999
SEQADV 1LKX ARG C 428 UNP Q03479 SEE REMARK 999
SEQADV 1LKX GLU C 429 UNP Q03479 LYS 428 SEE REMARK 999
SEQADV 1LKX ASN C 440 UNP Q03479 SEE REMARK 999
SEQADV 1LKX ILE C 498 UNP Q03479 ASN 496 SEE REMARK 999
SEQADV 1LKX VAL C 604 UNP Q03479 ASP 602 SEE REMARK 999
SEQADV 1LKX ASN C 681 UNP Q03479 ILE 679 SEE REMARK 999
SEQADV 1LKX THR C 683 UNP Q03479 ARG 681 SEE REMARK 999
SEQADV 1LKX GLU D 26 UNP Q03479 ASP 26 SEE REMARK 999
SEQADV 1LKX THR D 48 UNP Q03479 ARG 48 SEE REMARK 999
SEQADV 1LKX MET D 77 UNP Q03479 ILE 77 SEE REMARK 999
SEQADV 1LKX D UNP Q03479 ILE 137 SEE REMARK 999
SEQADV 1LKX D UNP Q03479 ARG 138 SEE REMARK 999
SEQADV 1LKX LEU D 137 UNP Q03479 PHE 139 SEE REMARK 999
SEQADV 1LKX ASP D 138 UNP Q03479 GLN 140 SEE REMARK 999
SEQADV 1LKX ASP D 215 UNP Q03479 ASN 217 SEE REMARK 999
SEQADV 1LKX ILE D 371 UNP Q03479 LEU 373 SEE REMARK 999
SEQADV 1LKX ILE D 372 UNP Q03479 SER 374 SEE REMARK 999
SEQADV 1LKX ASN D 373 UNP Q03479 ILE 375 SEE REMARK 999
SEQADV 1LKX CYS D 374 UNP Q03479 VAL 376 SEE REMARK 999
SEQADV 1LKX THR D 375 UNP Q03479 HIS 377 SEE REMARK 999
SEQADV 1LKX THR D 376 UNP Q03479 ARG 378 SEE REMARK 999
SEQADV 1LKX LYS D 378 UNP Q03479 SEE REMARK 999
SEQADV 1LKX PRO D 380 UNP Q03479 THR 381 SEE REMARK 999
SEQADV 1LKX VAL D 427 UNP Q03479 SEE REMARK 999
SEQADV 1LKX ARG D 428 UNP Q03479 SEE REMARK 999
SEQADV 1LKX GLU D 429 UNP Q03479 LYS 428 SEE REMARK 999
SEQADV 1LKX ASN D 440 UNP Q03479 SEE REMARK 999
SEQADV 1LKX ILE D 498 UNP Q03479 ASN 496 SEE REMARK 999
SEQADV 1LKX VAL D 604 UNP Q03479 ASP 602 SEE REMARK 999
SEQADV 1LKX ASN D 681 UNP Q03479 ILE 679 SEE REMARK 999
SEQADV 1LKX THR D 683 UNP Q03479 ARG 681 SEE REMARK 999
SEQRES 1 A 697 MET ILE PRO LYS THR LYS ALA GLU GLY VAL PRO ASP PHE
SEQRES 2 A 697 VAL LEU LEU ASN GLN ILE THR GLU ASN ALA PHE ILE GLU
SEQRES 3 A 697 ASN LEU THR MET ARG HIS LYS SER ASP ASN ILE TYR THR
SEQRES 4 A 697 TYR ILE GLY ASP VAL VAL ILE SER THR ASN PRO PHE LYS
SEQRES 5 A 697 ASN LEU ASN ILE TYR LYS GLU SER ASP ILE LYS ALA TYR
SEQRES 6 A 697 ASN GLY ARG TYR LYS TYR GLU MET PRO PRO HIS MET TYR
SEQRES 7 A 697 ALA LEU ALA ASN ASP ALA TYR ARG SER MET ARG GLN SER
SEQRES 8 A 697 GLN GLU ASN GLN CYS VAL ILE ILE SER GLY GLU SER GLY
SEQRES 9 A 697 ALA GLY LYS THR GLU ALA SER LYS LYS ILE MET GLN PHE
SEQRES 10 A 697 LEU THR PHE VAL SER SER ASN GLN SER PRO ASN GLY GLU
SEQRES 11 A 697 ARG ILE SER LYS MET LEU LEU ASP SER ASN PRO LEU LEU
SEQRES 12 A 697 GLU ALA PHE GLY ASN ALA LYS THR LEU ARG ASN ASP ASN
SEQRES 13 A 697 SER SER ARG PHE GLY LYS TYR MET GLU MET GLN PHE ASN
SEQRES 14 A 697 ALA VAL GLY SER PRO ILE GLY GLY LYS ILE THR ASN TYR
SEQRES 15 A 697 LEU LEU GLU LYS SER ARG VAL VAL GLY ARG THR GLN GLY
SEQRES 16 A 697 GLU ARG SER PHE HIS ILE PHE TYR GLN MET LEU LYS GLY
SEQRES 17 A 697 LEU SER GLN SER LYS LEU ASP GLU LEU GLY LEU THR PRO
SEQRES 18 A 697 ASN ALA PRO ALA TYR GLU TYR LEU LYS LYS SER GLY CYS
SEQRES 19 A 697 PHE ASP VAL SER THR ILE ASP ASP SER GLY GLU PHE LYS
SEQRES 20 A 697 ILE ILE VAL LYS ALA MET GLU THR LEU GLY LEU LYS GLU
SEQRES 21 A 697 SER ASP GLN ASN SER ILE TRP ARG ILE LEU ALA ALA ILE
SEQRES 22 A 697 LEU HIS ILE GLY ASN ILE THR PHE ALA GLU ALA ALA GLU
SEQRES 23 A 697 GLN ARG THR GLY THR THR THR VAL LYS VAL SER ASP THR
SEQRES 24 A 697 LYS SER LEU ALA ALA ALA ALA SER CYS LEU LYS THR ASP
SEQRES 25 A 697 GLN GLN SER LEU SER ILE ALA LEU CYS TYR ARG SER ILE
SEQRES 26 A 697 SER THR GLY VAL GLY LYS ARG CYS SER VAL ILE SER VAL
SEQRES 27 A 697 PRO MET ASP CYS ASN GLN ALA ALA TYR SER ARG ASP ALA
SEQRES 28 A 697 LEU ALA LYS ALA LEU TYR GLU ARG LEU PHE ASN TRP LEU
SEQRES 29 A 697 VAL SER LYS ILE ASN THR ILE ILE ASN CYS THR THR GLU
SEQRES 30 A 697 LYS GLY PRO VAL ILE GLY ILE LEU ASP ILE TYR GLY PHE
SEQRES 31 A 697 GLU VAL PHE GLN ASN ASN SER PHE GLU GLN LEU ASN ILE
SEQRES 32 A 697 ASN PHE CYS ASN GLU LYS LEU GLN GLN LEU PHE ILE GLU
SEQRES 33 A 697 LEU THR LEU LYS SER GLU GLN GLU GLU TYR VAL ARG GLU
SEQRES 34 A 697 GLY ILE GLU TRP LYS ASN ILE GLU TYR PHE ASN ASN LYS
SEQRES 35 A 697 PRO ILE CYS GLU LEU ILE GLU LYS LYS PRO ILE GLY LEU
SEQRES 36 A 697 ILE SER LEU LEU ASP GLU ALA CYS LEU ILE ALA LYS SER
SEQRES 37 A 697 THR ASP GLN THR PHE LEU ASP SER ILE CYS LYS GLN PHE
SEQRES 38 A 697 GLU LYS ASN PRO HIS LEU GLN SER TYR VAL VAL SER LYS
SEQRES 39 A 697 ASP ARG SER ILE GLY ASP THR CYS PHE ARG LEU LYS HIS
SEQRES 40 A 697 TYR ALA GLY ASP VAL THR TYR ASP VAL ARG GLY PHE LEU
SEQRES 41 A 697 ASP LYS ASN LYS ASP THR LEU PHE GLY ASP LEU ILE SER
SEQRES 42 A 697 SER MET GLN SER SER SER ASP PRO LEU VAL GLN GLY LEU
SEQRES 43 A 697 PHE PRO PRO THR ARG PRO GLU ASP SER LYS LYS ARG PRO
SEQRES 44 A 697 GLU THR ALA GLY SER GLN PHE ARG ASN ALA MET ASN ALA
SEQRES 45 A 697 LEU ILE THR THR LEU LEU ALA CYS SER PRO HIS TYR VAL
SEQRES 46 A 697 ARG CYS ILE LYS SER ASN ASP ASN LYS GLN ALA GLY VAL
SEQRES 47 A 697 ILE ASP GLU ASP ARG VAL ARG HIS GLN VAL ARG TYR LEU
SEQRES 48 A 697 GLY LEU LEU GLU ASN VAL ARG VAL ARG ARG ALA GLY PHE
SEQRES 49 A 697 ALA GLY ARG ILE GLU TYR THR ARG PHE TYR ASN ARG TYR
SEQRES 50 A 697 LYS MET LEU CYS LYS LYS THR TRP PRO SER PHE ASN GLY
SEQRES 51 A 697 THR ALA LYS GLN ALA THR GLU LEU ILE LEU GLN GLN HIS
SEQRES 52 A 697 ASN ILE ASP LYS GLU GLU ILE ARG MET GLY LYS THR LYS
SEQRES 53 A 697 VAL PHE ILE ARG ASN PRO THR THR LEU PHE TYR PHE GLU
SEQRES 54 A 697 GLU LYS ARG GLU LEU GLU MET PRO
SEQRES 1 B 697 MET ILE PRO LYS THR LYS ALA GLU GLY VAL PRO ASP PHE
SEQRES 2 B 697 VAL LEU LEU ASN GLN ILE THR GLU ASN ALA PHE ILE GLU
SEQRES 3 B 697 ASN LEU THR MET ARG HIS LYS SER ASP ASN ILE TYR THR
SEQRES 4 B 697 TYR ILE GLY ASP VAL VAL ILE SER THR ASN PRO PHE LYS
SEQRES 5 B 697 ASN LEU ASN ILE TYR LYS GLU SER ASP ILE LYS ALA TYR
SEQRES 6 B 697 ASN GLY ARG TYR LYS TYR GLU MET PRO PRO HIS MET TYR
SEQRES 7 B 697 ALA LEU ALA ASN ASP ALA TYR ARG SER MET ARG GLN SER
SEQRES 8 B 697 GLN GLU ASN GLN CYS VAL ILE ILE SER GLY GLU SER GLY
SEQRES 9 B 697 ALA GLY LYS THR GLU ALA SER LYS LYS ILE MET GLN PHE
SEQRES 10 B 697 LEU THR PHE VAL SER SER ASN GLN SER PRO ASN GLY GLU
SEQRES 11 B 697 ARG ILE SER LYS MET LEU LEU ASP SER ASN PRO LEU LEU
SEQRES 12 B 697 GLU ALA PHE GLY ASN ALA LYS THR LEU ARG ASN ASP ASN
SEQRES 13 B 697 SER SER ARG PHE GLY LYS TYR MET GLU MET GLN PHE ASN
SEQRES 14 B 697 ALA VAL GLY SER PRO ILE GLY GLY LYS ILE THR ASN TYR
SEQRES 15 B 697 LEU LEU GLU LYS SER ARG VAL VAL GLY ARG THR GLN GLY
SEQRES 16 B 697 GLU ARG SER PHE HIS ILE PHE TYR GLN MET LEU LYS GLY
SEQRES 17 B 697 LEU SER GLN SER LYS LEU ASP GLU LEU GLY LEU THR PRO
SEQRES 18 B 697 ASN ALA PRO ALA TYR GLU TYR LEU LYS LYS SER GLY CYS
SEQRES 19 B 697 PHE ASP VAL SER THR ILE ASP ASP SER GLY GLU PHE LYS
SEQRES 20 B 697 ILE ILE VAL LYS ALA MET GLU THR LEU GLY LEU LYS GLU
SEQRES 21 B 697 SER ASP GLN ASN SER ILE TRP ARG ILE LEU ALA ALA ILE
SEQRES 22 B 697 LEU HIS ILE GLY ASN ILE THR PHE ALA GLU ALA ALA GLU
SEQRES 23 B 697 GLN ARG THR GLY THR THR THR VAL LYS VAL SER ASP THR
SEQRES 24 B 697 LYS SER LEU ALA ALA ALA ALA SER CYS LEU LYS THR ASP
SEQRES 25 B 697 GLN GLN SER LEU SER ILE ALA LEU CYS TYR ARG SER ILE
SEQRES 26 B 697 SER THR GLY VAL GLY LYS ARG CYS SER VAL ILE SER VAL
SEQRES 27 B 697 PRO MET ASP CYS ASN GLN ALA ALA TYR SER ARG ASP ALA
SEQRES 28 B 697 LEU ALA LYS ALA LEU TYR GLU ARG LEU PHE ASN TRP LEU
SEQRES 29 B 697 VAL SER LYS ILE ASN THR ILE ILE ASN CYS THR THR GLU
SEQRES 30 B 697 LYS GLY PRO VAL ILE GLY ILE LEU ASP ILE TYR GLY PHE
SEQRES 31 B 697 GLU VAL PHE GLN ASN ASN SER PHE GLU GLN LEU ASN ILE
SEQRES 32 B 697 ASN PHE CYS ASN GLU LYS LEU GLN GLN LEU PHE ILE GLU
SEQRES 33 B 697 LEU THR LEU LYS SER GLU GLN GLU GLU TYR VAL ARG GLU
SEQRES 34 B 697 GLY ILE GLU TRP LYS ASN ILE GLU TYR PHE ASN ASN LYS
SEQRES 35 B 697 PRO ILE CYS GLU LEU ILE GLU LYS LYS PRO ILE GLY LEU
SEQRES 36 B 697 ILE SER LEU LEU ASP GLU ALA CYS LEU ILE ALA LYS SER
SEQRES 37 B 697 THR ASP GLN THR PHE LEU ASP SER ILE CYS LYS GLN PHE
SEQRES 38 B 697 GLU LYS ASN PRO HIS LEU GLN SER TYR VAL VAL SER LYS
SEQRES 39 B 697 ASP ARG SER ILE GLY ASP THR CYS PHE ARG LEU LYS HIS
SEQRES 40 B 697 TYR ALA GLY ASP VAL THR TYR ASP VAL ARG GLY PHE LEU
SEQRES 41 B 697 ASP LYS ASN LYS ASP THR LEU PHE GLY ASP LEU ILE SER
SEQRES 42 B 697 SER MET GLN SER SER SER ASP PRO LEU VAL GLN GLY LEU
SEQRES 43 B 697 PHE PRO PRO THR ARG PRO GLU ASP SER LYS LYS ARG PRO
SEQRES 44 B 697 GLU THR ALA GLY SER GLN PHE ARG ASN ALA MET ASN ALA
SEQRES 45 B 697 LEU ILE THR THR LEU LEU ALA CYS SER PRO HIS TYR VAL
SEQRES 46 B 697 ARG CYS ILE LYS SER ASN ASP ASN LYS GLN ALA GLY VAL
SEQRES 47 B 697 ILE ASP GLU ASP ARG VAL ARG HIS GLN VAL ARG TYR LEU
SEQRES 48 B 697 GLY LEU LEU GLU ASN VAL ARG VAL ARG ARG ALA GLY PHE
SEQRES 49 B 697 ALA GLY ARG ILE GLU TYR THR ARG PHE TYR ASN ARG TYR
SEQRES 50 B 697 LYS MET LEU CYS LYS LYS THR TRP PRO SER PHE ASN GLY
SEQRES 51 B 697 THR ALA LYS GLN ALA THR GLU LEU ILE LEU GLN GLN HIS
SEQRES 52 B 697 ASN ILE ASP LYS GLU GLU ILE ARG MET GLY LYS THR LYS
SEQRES 53 B 697 VAL PHE ILE ARG ASN PRO THR THR LEU PHE TYR PHE GLU
SEQRES 54 B 697 GLU LYS ARG GLU LEU GLU MET PRO
SEQRES 1 C 697 MET ILE PRO LYS THR LYS ALA GLU GLY VAL PRO ASP PHE
SEQRES 2 C 697 VAL LEU LEU ASN GLN ILE THR GLU ASN ALA PHE ILE GLU
SEQRES 3 C 697 ASN LEU THR MET ARG HIS LYS SER ASP ASN ILE TYR THR
SEQRES 4 C 697 TYR ILE GLY ASP VAL VAL ILE SER THR ASN PRO PHE LYS
SEQRES 5 C 697 ASN LEU ASN ILE TYR LYS GLU SER ASP ILE LYS ALA TYR
SEQRES 6 C 697 ASN GLY ARG TYR LYS TYR GLU MET PRO PRO HIS MET TYR
SEQRES 7 C 697 ALA LEU ALA ASN ASP ALA TYR ARG SER MET ARG GLN SER
SEQRES 8 C 697 GLN GLU ASN GLN CYS VAL ILE ILE SER GLY GLU SER GLY
SEQRES 9 C 697 ALA GLY LYS THR GLU ALA SER LYS LYS ILE MET GLN PHE
SEQRES 10 C 697 LEU THR PHE VAL SER SER ASN GLN SER PRO ASN GLY GLU
SEQRES 11 C 697 ARG ILE SER LYS MET LEU LEU ASP SER ASN PRO LEU LEU
SEQRES 12 C 697 GLU ALA PHE GLY ASN ALA LYS THR LEU ARG ASN ASP ASN
SEQRES 13 C 697 SER SER ARG PHE GLY LYS TYR MET GLU MET GLN PHE ASN
SEQRES 14 C 697 ALA VAL GLY SER PRO ILE GLY GLY LYS ILE THR ASN TYR
SEQRES 15 C 697 LEU LEU GLU LYS SER ARG VAL VAL GLY ARG THR GLN GLY
SEQRES 16 C 697 GLU ARG SER PHE HIS ILE PHE TYR GLN MET LEU LYS GLY
SEQRES 17 C 697 LEU SER GLN SER LYS LEU ASP GLU LEU GLY LEU THR PRO
SEQRES 18 C 697 ASN ALA PRO ALA TYR GLU TYR LEU LYS LYS SER GLY CYS
SEQRES 19 C 697 PHE ASP VAL SER THR ILE ASP ASP SER GLY GLU PHE LYS
SEQRES 20 C 697 ILE ILE VAL LYS ALA MET GLU THR LEU GLY LEU LYS GLU
SEQRES 21 C 697 SER ASP GLN ASN SER ILE TRP ARG ILE LEU ALA ALA ILE
SEQRES 22 C 697 LEU HIS ILE GLY ASN ILE THR PHE ALA GLU ALA ALA GLU
SEQRES 23 C 697 GLN ARG THR GLY THR THR THR VAL LYS VAL SER ASP THR
SEQRES 24 C 697 LYS SER LEU ALA ALA ALA ALA SER CYS LEU LYS THR ASP
SEQRES 25 C 697 GLN GLN SER LEU SER ILE ALA LEU CYS TYR ARG SER ILE
SEQRES 26 C 697 SER THR GLY VAL GLY LYS ARG CYS SER VAL ILE SER VAL
SEQRES 27 C 697 PRO MET ASP CYS ASN GLN ALA ALA TYR SER ARG ASP ALA
SEQRES 28 C 697 LEU ALA LYS ALA LEU TYR GLU ARG LEU PHE ASN TRP LEU
SEQRES 29 C 697 VAL SER LYS ILE ASN THR ILE ILE ASN CYS THR THR GLU
SEQRES 30 C 697 LYS GLY PRO VAL ILE GLY ILE LEU ASP ILE TYR GLY PHE
SEQRES 31 C 697 GLU VAL PHE GLN ASN ASN SER PHE GLU GLN LEU ASN ILE
SEQRES 32 C 697 ASN PHE CYS ASN GLU LYS LEU GLN GLN LEU PHE ILE GLU
SEQRES 33 C 697 LEU THR LEU LYS SER GLU GLN GLU GLU TYR VAL ARG GLU
SEQRES 34 C 697 GLY ILE GLU TRP LYS ASN ILE GLU TYR PHE ASN ASN LYS
SEQRES 35 C 697 PRO ILE CYS GLU LEU ILE GLU LYS LYS PRO ILE GLY LEU
SEQRES 36 C 697 ILE SER LEU LEU ASP GLU ALA CYS LEU ILE ALA LYS SER
SEQRES 37 C 697 THR ASP GLN THR PHE LEU ASP SER ILE CYS LYS GLN PHE
SEQRES 38 C 697 GLU LYS ASN PRO HIS LEU GLN SER TYR VAL VAL SER LYS
SEQRES 39 C 697 ASP ARG SER ILE GLY ASP THR CYS PHE ARG LEU LYS HIS
SEQRES 40 C 697 TYR ALA GLY ASP VAL THR TYR ASP VAL ARG GLY PHE LEU
SEQRES 41 C 697 ASP LYS ASN LYS ASP THR LEU PHE GLY ASP LEU ILE SER
SEQRES 42 C 697 SER MET GLN SER SER SER ASP PRO LEU VAL GLN GLY LEU
SEQRES 43 C 697 PHE PRO PRO THR ARG PRO GLU ASP SER LYS LYS ARG PRO
SEQRES 44 C 697 GLU THR ALA GLY SER GLN PHE ARG ASN ALA MET ASN ALA
SEQRES 45 C 697 LEU ILE THR THR LEU LEU ALA CYS SER PRO HIS TYR VAL
SEQRES 46 C 697 ARG CYS ILE LYS SER ASN ASP ASN LYS GLN ALA GLY VAL
SEQRES 47 C 697 ILE ASP GLU ASP ARG VAL ARG HIS GLN VAL ARG TYR LEU
SEQRES 48 C 697 GLY LEU LEU GLU ASN VAL ARG VAL ARG ARG ALA GLY PHE
SEQRES 49 C 697 ALA GLY ARG ILE GLU TYR THR ARG PHE TYR ASN ARG TYR
SEQRES 50 C 697 LYS MET LEU CYS LYS LYS THR TRP PRO SER PHE ASN GLY
SEQRES 51 C 697 THR ALA LYS GLN ALA THR GLU LEU ILE LEU GLN GLN HIS
SEQRES 52 C 697 ASN ILE ASP LYS GLU GLU ILE ARG MET GLY LYS THR LYS
SEQRES 53 C 697 VAL PHE ILE ARG ASN PRO THR THR LEU PHE TYR PHE GLU
SEQRES 54 C 697 GLU LYS ARG GLU LEU GLU MET PRO
SEQRES 1 D 697 MET ILE PRO LYS THR LYS ALA GLU GLY VAL PRO ASP PHE
SEQRES 2 D 697 VAL LEU LEU ASN GLN ILE THR GLU ASN ALA PHE ILE GLU
SEQRES 3 D 697 ASN LEU THR MET ARG HIS LYS SER ASP ASN ILE TYR THR
SEQRES 4 D 697 TYR ILE GLY ASP VAL VAL ILE SER THR ASN PRO PHE LYS
SEQRES 5 D 697 ASN LEU ASN ILE TYR LYS GLU SER ASP ILE LYS ALA TYR
SEQRES 6 D 697 ASN GLY ARG TYR LYS TYR GLU MET PRO PRO HIS MET TYR
SEQRES 7 D 697 ALA LEU ALA ASN ASP ALA TYR ARG SER MET ARG GLN SER
SEQRES 8 D 697 GLN GLU ASN GLN CYS VAL ILE ILE SER GLY GLU SER GLY
SEQRES 9 D 697 ALA GLY LYS THR GLU ALA SER LYS LYS ILE MET GLN PHE
SEQRES 10 D 697 LEU THR PHE VAL SER SER ASN GLN SER PRO ASN GLY GLU
SEQRES 11 D 697 ARG ILE SER LYS MET LEU LEU ASP SER ASN PRO LEU LEU
SEQRES 12 D 697 GLU ALA PHE GLY ASN ALA LYS THR LEU ARG ASN ASP ASN
SEQRES 13 D 697 SER SER ARG PHE GLY LYS TYR MET GLU MET GLN PHE ASN
SEQRES 14 D 697 ALA VAL GLY SER PRO ILE GLY GLY LYS ILE THR ASN TYR
SEQRES 15 D 697 LEU LEU GLU LYS SER ARG VAL VAL GLY ARG THR GLN GLY
SEQRES 16 D 697 GLU ARG SER PHE HIS ILE PHE TYR GLN MET LEU LYS GLY
SEQRES 17 D 697 LEU SER GLN SER LYS LEU ASP GLU LEU GLY LEU THR PRO
SEQRES 18 D 697 ASN ALA PRO ALA TYR GLU TYR LEU LYS LYS SER GLY CYS
SEQRES 19 D 697 PHE ASP VAL SER THR ILE ASP ASP SER GLY GLU PHE LYS
SEQRES 20 D 697 ILE ILE VAL LYS ALA MET GLU THR LEU GLY LEU LYS GLU
SEQRES 21 D 697 SER ASP GLN ASN SER ILE TRP ARG ILE LEU ALA ALA ILE
SEQRES 22 D 697 LEU HIS ILE GLY ASN ILE THR PHE ALA GLU ALA ALA GLU
SEQRES 23 D 697 GLN ARG THR GLY THR THR THR VAL LYS VAL SER ASP THR
SEQRES 24 D 697 LYS SER LEU ALA ALA ALA ALA SER CYS LEU LYS THR ASP
SEQRES 25 D 697 GLN GLN SER LEU SER ILE ALA LEU CYS TYR ARG SER ILE
SEQRES 26 D 697 SER THR GLY VAL GLY LYS ARG CYS SER VAL ILE SER VAL
SEQRES 27 D 697 PRO MET ASP CYS ASN GLN ALA ALA TYR SER ARG ASP ALA
SEQRES 28 D 697 LEU ALA LYS ALA LEU TYR GLU ARG LEU PHE ASN TRP LEU
SEQRES 29 D 697 VAL SER LYS ILE ASN THR ILE ILE ASN CYS THR THR GLU
SEQRES 30 D 697 LYS GLY PRO VAL ILE GLY ILE LEU ASP ILE TYR GLY PHE
SEQRES 31 D 697 GLU VAL PHE GLN ASN ASN SER PHE GLU GLN LEU ASN ILE
SEQRES 32 D 697 ASN PHE CYS ASN GLU LYS LEU GLN GLN LEU PHE ILE GLU
SEQRES 33 D 697 LEU THR LEU LYS SER GLU GLN GLU GLU TYR VAL ARG GLU
SEQRES 34 D 697 GLY ILE GLU TRP LYS ASN ILE GLU TYR PHE ASN ASN LYS
SEQRES 35 D 697 PRO ILE CYS GLU LEU ILE GLU LYS LYS PRO ILE GLY LEU
SEQRES 36 D 697 ILE SER LEU LEU ASP GLU ALA CYS LEU ILE ALA LYS SER
SEQRES 37 D 697 THR ASP GLN THR PHE LEU ASP SER ILE CYS LYS GLN PHE
SEQRES 38 D 697 GLU LYS ASN PRO HIS LEU GLN SER TYR VAL VAL SER LYS
SEQRES 39 D 697 ASP ARG SER ILE GLY ASP THR CYS PHE ARG LEU LYS HIS
SEQRES 40 D 697 TYR ALA GLY ASP VAL THR TYR ASP VAL ARG GLY PHE LEU
SEQRES 41 D 697 ASP LYS ASN LYS ASP THR LEU PHE GLY ASP LEU ILE SER
SEQRES 42 D 697 SER MET GLN SER SER SER ASP PRO LEU VAL GLN GLY LEU
SEQRES 43 D 697 PHE PRO PRO THR ARG PRO GLU ASP SER LYS LYS ARG PRO
SEQRES 44 D 697 GLU THR ALA GLY SER GLN PHE ARG ASN ALA MET ASN ALA
SEQRES 45 D 697 LEU ILE THR THR LEU LEU ALA CYS SER PRO HIS TYR VAL
SEQRES 46 D 697 ARG CYS ILE LYS SER ASN ASP ASN LYS GLN ALA GLY VAL
SEQRES 47 D 697 ILE ASP GLU ASP ARG VAL ARG HIS GLN VAL ARG TYR LEU
SEQRES 48 D 697 GLY LEU LEU GLU ASN VAL ARG VAL ARG ARG ALA GLY PHE
SEQRES 49 D 697 ALA GLY ARG ILE GLU TYR THR ARG PHE TYR ASN ARG TYR
SEQRES 50 D 697 LYS MET LEU CYS LYS LYS THR TRP PRO SER PHE ASN GLY
SEQRES 51 D 697 THR ALA LYS GLN ALA THR GLU LEU ILE LEU GLN GLN HIS
SEQRES 52 D 697 ASN ILE ASP LYS GLU GLU ILE ARG MET GLY LYS THR LYS
SEQRES 53 D 697 VAL PHE ILE ARG ASN PRO THR THR LEU PHE TYR PHE GLU
SEQRES 54 D 697 GLU LYS ARG GLU LEU GLU MET PRO
HET MG A 790 1
HET VO4 A 792 5
HET ADP A 791 27
HET MG B 793 1
HET VO4 B 795 5
HET ADP B 794 27
HET MG C 890 1
HET VO4 C 892 5
HET ADP C 891 27
HET MG D 893 1
HET VO4 D 895 5
HET ADP D 894 27
HETNAM MG MAGNESIUM ION
HETNAM VO4 VANADATE ION
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
FORMUL 5 MG 4(MG 2+)
FORMUL 6 VO4 4(O4 V 3-)
FORMUL 7 ADP 4(C10 H15 N5 O10 P2)
FORMUL 17 HOH *64(H2 O)
HELIX 1 1 ASP A 12 LEU A 16 5 5
HELIX 2 2 THR A 20 SER A 34 1 15
HELIX 3 3 LYS A 58 ASN A 66 1 9
HELIX 4 4 TYR A 69 MET A 73 5 5
HELIX 5 5 HIS A 76 GLN A 92 1 17
HELIX 6 6 GLY A 106 SER A 122 1 17
HELIX 7 7 SER A 126 ASN A 148 1 23
HELIX 8 8 GLU A 185 VAL A 190 5 6
HELIX 9 9 PHE A 199 LYS A 207 1 9
HELIX 10 10 SER A 210 GLY A 218 1 9
HELIX 11 11 ASN A 222 ALA A 225 5 4
HELIX 12 12 TYR A 226 LYS A 231 1 6
HELIX 13 13 ASP A 241 LEU A 256 1 16
HELIX 14 14 LYS A 259 GLY A 277 1 19
HELIX 15 15 ASP A 298 LYS A 310 1 13
HELIX 16 16 ASP A 312 TYR A 322 1 11
HELIX 17 17 ASP A 341 ASN A 373 1 33
HELIX 18 18 SER A 397 LEU A 419 1 23
HELIX 19 19 LEU A 419 GLU A 429 1 11
HELIX 20 20 LYS A 442 ILE A 448 1 7
HELIX 21 21 GLY A 454 ILE A 465 1 12
HELIX 22 22 THR A 469 PHE A 481 1 13
HELIX 23 23 GLY A 518 ASP A 525 1 8
HELIX 24 24 PHE A 528 SER A 537 1 10
HELIX 25 25 ASP A 540 PHE A 547 1 8
HELIX 26 26 THR A 561 LEU A 578 1 18
HELIX 27 27 ASP A 600 LEU A 611 1 12
HELIX 28 28 LEU A 613 GLY A 623 1 11
HELIX 29 29 TYR A 630 ASN A 635 1 6
HELIX 30 30 LYS A 653 GLN A 662 1 10
HELIX 31 31 ASP A 666 GLU A 668 5 3
HELIX 32 32 PRO A 682 GLU A 690 1 9
HELIX 33 33 ASP B 12 LEU B 16 5 5
HELIX 34 34 THR B 20 SER B 34 1 15
HELIX 35 35 LYS B 58 ASN B 66 1 9
HELIX 36 36 TYR B 69 MET B 73 5 5
HELIX 37 37 HIS B 76 GLN B 92 1 17
HELIX 38 38 GLY B 106 SER B 122 1 17
HELIX 39 39 SER B 126 ASN B 148 1 23
HELIX 40 40 GLU B 185 VAL B 190 5 6
HELIX 41 41 PHE B 199 LYS B 207 1 9
HELIX 42 42 SER B 210 GLY B 218 1 9
HELIX 43 43 ASN B 222 ALA B 225 5 4
HELIX 44 44 TYR B 226 LYS B 231 1 6
HELIX 45 45 ASP B 241 LEU B 256 1 16
HELIX 46 46 LYS B 259 GLY B 277 1 19
HELIX 47 47 ASP B 298 LYS B 310 1 13
HELIX 48 48 ASP B 312 TYR B 322 1 11
HELIX 49 49 ASP B 341 ASN B 373 1 33
HELIX 50 50 SER B 397 LEU B 419 1 23
HELIX 51 51 LEU B 419 ARG B 428 1 10
HELIX 52 52 LYS B 442 ILE B 448 1 7
HELIX 53 53 GLY B 454 ILE B 465 1 12
HELIX 54 54 THR B 469 PHE B 481 1 13
HELIX 55 55 GLY B 518 ASP B 525 1 8
HELIX 56 56 PHE B 528 SER B 537 1 10
HELIX 57 57 ASP B 540 PHE B 547 1 8
HELIX 58 58 THR B 561 LEU B 578 1 18
HELIX 59 59 ASP B 600 LEU B 611 1 12
HELIX 60 60 GLY B 612 GLY B 623 1 12
HELIX 61 61 LYS B 653 GLN B 662 1 10
HELIX 62 62 ASN B 681 GLU B 689 1 9
HELIX 63 63 ASP C 12 LEU C 16 5 5
HELIX 64 64 THR C 20 SER C 34 1 15
HELIX 65 65 LYS C 58 ASN C 66 1 9
HELIX 66 66 TYR C 69 MET C 73 5 5
HELIX 67 67 HIS C 76 GLN C 92 1 17
HELIX 68 68 GLY C 106 SER C 122 1 17
HELIX 69 69 SER C 126 ASN C 148 1 23
HELIX 70 70 GLU C 185 VAL C 190 5 6
HELIX 71 71 PHE C 199 LYS C 207 1 9
HELIX 72 72 SER C 210 GLY C 218 1 9
HELIX 73 73 ASN C 222 ALA C 225 5 4
HELIX 74 74 TYR C 226 LYS C 231 1 6
HELIX 75 75 ASP C 241 LEU C 256 1 16
HELIX 76 76 LYS C 259 GLY C 277 1 19
HELIX 77 77 ASP C 298 LYS C 310 1 13
HELIX 78 78 ASP C 312 TYR C 322 1 11
HELIX 79 79 ASP C 341 ASN C 373 1 33
HELIX 80 80 SER C 397 LEU C 419 1 23
HELIX 81 81 LEU C 419 GLU C 429 1 11
HELIX 82 82 LYS C 442 ILE C 448 1 7
HELIX 83 83 GLY C 454 ILE C 465 1 12
HELIX 84 84 THR C 469 PHE C 481 1 13
HELIX 85 85 GLY C 518 ASP C 525 1 8
HELIX 86 86 PHE C 528 SER C 537 1 10
HELIX 87 87 ASP C 540 PHE C 547 1 8
HELIX 88 88 THR C 561 LEU C 578 1 18
HELIX 89 89 ASP C 600 GLY C 612 1 13
HELIX 90 90 GLY C 612 GLY C 623 1 12
HELIX 91 91 TYR C 630 ASN C 635 1 6
HELIX 92 92 TYR C 637 CYS C 641 5 5
HELIX 93 93 THR C 651 GLN C 662 1 12
HELIX 94 94 THR C 683 LEU C 694 1 12
HELIX 95 95 ASP D 12 LEU D 16 5 5
HELIX 96 96 THR D 20 SER D 34 1 15
HELIX 97 97 LYS D 58 ASN D 66 1 9
HELIX 98 98 TYR D 69 MET D 73 5 5
HELIX 99 99 HIS D 76 GLN D 92 1 17
HELIX 100 100 GLY D 106 SER D 122 1 17
HELIX 101 101 SER D 126 ASN D 148 1 23
HELIX 102 102 GLU D 185 VAL D 190 5 6
HELIX 103 103 PHE D 199 LYS D 207 1 9
HELIX 104 104 SER D 210 GLY D 218 1 9
HELIX 105 105 ASN D 222 ALA D 225 5 4
HELIX 106 106 TYR D 226 LYS D 231 1 6
HELIX 107 107 ASP D 241 LEU D 256 1 16
HELIX 108 108 LYS D 259 GLY D 277 1 19
HELIX 109 109 ASP D 298 LYS D 310 1 13
HELIX 110 110 ASP D 312 TYR D 322 1 11
HELIX 111 111 ASP D 341 ASN D 373 1 33
HELIX 112 112 SER D 397 LEU D 419 1 23
HELIX 113 113 LEU D 419 GLY D 430 1 12
HELIX 114 114 LYS D 442 ILE D 448 1 7
HELIX 115 115 GLY D 454 ILE D 465 1 12
HELIX 116 116 THR D 469 PHE D 481 1 13
HELIX 117 117 GLY D 518 ASP D 525 1 8
HELIX 118 118 PHE D 528 SER D 537 1 10
HELIX 119 119 ASP D 540 PHE D 547 1 8
HELIX 120 120 THR D 561 LEU D 578 1 18
HELIX 121 121 ASP D 600 LEU D 611 1 12
HELIX 122 122 GLY D 612 GLY D 623 1 12
HELIX 123 123 GLU D 629 LYS D 638 1 10
HELIX 124 124 MET D 639 CYS D 641 5 3
HELIX 125 125 THR D 651 GLN D 662 1 12
HELIX 126 126 ASP D 666 GLU D 668 5 3
HELIX 127 127 PRO D 682 GLU D 695 1 14
SHEET 1 A 7 TYR A 38 TYR A 40 0
SHEET 2 A 7 VAL A 45 THR A 48 -1 O ILE A 46 N THR A 39
SHEET 3 A 7 SER A 581 ILE A 588 1 O ARG A 586 N VAL A 45
SHEET 4 A 7 GLN A 95 SER A 100 1 N SER A 100 O CYS A 587
SHEET 5 A 7 VAL A 381 ASP A 386 1 O GLY A 383 N GLN A 95
SHEET 6 A 7 GLY A 161 PHE A 168 -1 N LYS A 162 O ASP A 386
SHEET 7 A 7 PRO A 174 TYR A 182 -1 O ILE A 175 N GLN A 167
SHEET 1 B 2 PHE A 281 ALA A 284 0
SHEET 2 B 2 THR A 293 VAL A 296 -1 O LYS A 295 N ALA A 282
SHEET 1 C 3 LEU A 487 GLN A 488 0
SHEET 2 C 3 CYS A 502 HIS A 507 -1 O ARG A 504 N GLN A 488
SHEET 3 C 3 GLY A 510 ASP A 515 -1 O VAL A 512 N LEU A 505
SHEET 1 D 2 ILE A 670 MET A 672 0
SHEET 2 D 2 VAL A 677 ILE A 679 -1 O PHE A 678 N ARG A 671
SHEET 1 E 7 TYR B 38 TYR B 40 0
SHEET 2 E 7 VAL B 45 THR B 48 -1 O ILE B 46 N THR B 39
SHEET 3 E 7 SER B 581 ILE B 588 1 O ARG B 586 N VAL B 45
SHEET 4 E 7 GLN B 95 SER B 100 1 N SER B 100 O CYS B 587
SHEET 5 E 7 VAL B 381 ASP B 386 1 O GLY B 383 N GLN B 95
SHEET 6 E 7 GLY B 161 PHE B 168 -1 N LYS B 162 O ASP B 386
SHEET 7 E 7 PRO B 174 TYR B 182 -1 O ILE B 175 N GLN B 167
SHEET 1 F 2 PHE B 281 ALA B 284 0
SHEET 2 F 2 THR B 293 VAL B 296 -1 O LYS B 295 N ALA B 282
SHEET 1 G 3 LEU B 487 GLN B 488 0
SHEET 2 G 3 CYS B 502 HIS B 507 -1 O ARG B 504 N GLN B 488
SHEET 3 G 3 GLY B 510 ASP B 515 -1 O VAL B 512 N LEU B 505
SHEET 1 H 2 ARG B 627 ILE B 628 0
SHEET 2 H 2 VAL B 677 PHE B 678 -1 O VAL B 677 N ILE B 628
SHEET 1 I 7 TYR C 38 TYR C 40 0
SHEET 2 I 7 VAL C 45 THR C 48 -1 O ILE C 46 N THR C 39
SHEET 3 I 7 SER C 581 ILE C 588 1 O ILE C 588 N SER C 47
SHEET 4 I 7 GLN C 95 SER C 100 1 N ILE C 98 O HIS C 583
SHEET 5 I 7 VAL C 381 ASP C 386 1 O GLY C 383 N VAL C 97
SHEET 6 I 7 GLY C 161 PHE C 168 -1 N LYS C 162 O ASP C 386
SHEET 7 I 7 PRO C 174 TYR C 182 -1 O TYR C 182 N GLY C 161
SHEET 1 J 2 PHE C 281 ALA C 284 0
SHEET 2 J 2 THR C 293 VAL C 296 -1 O LYS C 295 N ALA C 282
SHEET 1 K 3 LEU C 487 GLN C 488 0
SHEET 2 K 3 CYS C 502 HIS C 507 -1 O ARG C 504 N GLN C 488
SHEET 3 K 3 GLY C 510 ASP C 515 -1 O VAL C 512 N LEU C 505
SHEET 1 L 3 GLY C 626 GLU C 629 0
SHEET 2 L 3 LYS C 676 ILE C 679 -1 O VAL C 677 N ILE C 628
SHEET 3 L 3 ILE C 670 MET C 672 -1 N ARG C 671 O PHE C 678
SHEET 1 M 7 TYR D 38 TYR D 40 0
SHEET 2 M 7 VAL D 45 THR D 48 -1 O ILE D 46 N THR D 39
SHEET 3 M 7 SER D 581 ILE D 588 1 O TYR D 584 N VAL D 45
SHEET 4 M 7 GLN D 95 SER D 100 1 N SER D 100 O CYS D 587
SHEET 5 M 7 VAL D 381 ASP D 386 1 O VAL D 381 N GLN D 95
SHEET 6 M 7 GLY D 161 PHE D 168 -1 N LYS D 162 O ASP D 386
SHEET 7 M 7 PRO D 174 TYR D 182 -1 O ILE D 175 N GLN D 167
SHEET 1 N 2 PHE D 281 ALA D 284 0
SHEET 2 N 2 THR D 293 VAL D 296 -1 O LYS D 295 N ALA D 282
SHEET 1 O 3 LEU D 487 GLN D 488 0
SHEET 2 O 3 CYS D 502 HIS D 507 -1 O ARG D 504 N GLN D 488
SHEET 3 O 3 GLY D 510 ASP D 515 -1 O VAL D 512 N LEU D 505
SHEET 1 P 3 GLY D 626 ILE D 628 0
SHEET 2 P 3 VAL D 677 ILE D 679 -1 O VAL D 677 N ILE D 628
SHEET 3 P 3 ILE D 670 MET D 672 -1 N ARG D 671 O PHE D 678
LINK OG1 THR A 108 MG MG A 790 1555 1555 2.13
LINK OG SER A 158 MG MG A 790 1555 1555 2.36
LINK MG MG A 790 O2A ADP A 791 1555 1555 3.12
LINK MG MG A 790 O1B ADP A 791 1555 1555 2.39
LINK MG MG A 790 O2 VO4 A 792 1555 1555 2.42
LINK MG MG A 790 O HOH A 805 1555 1555 2.57
LINK MG MG A 790 O HOH A 808 1555 1555 3.07
LINK O2B ADP A 791 V VO4 A 792 1555 1555 2.00
LINK OG1 THR B 108 MG MG B 793 1555 1555 2.31
LINK OG SER B 158 MG MG B 793 1555 1555 2.61
LINK MG MG B 793 O1B ADP B 794 1555 1555 2.48
LINK MG MG B 793 O2A ADP B 794 1555 1555 2.87
LINK MG MG B 793 O3 VO4 B 795 1555 1555 2.36
LINK MG MG B 793 O HOH B 796 1555 1555 2.78
LINK MG MG B 793 O HOH B 797 1555 1555 2.63
LINK O2B ADP B 794 V VO4 B 795 1555 1555 1.86
LINK OG1 THR C 108 MG MG C 890 1555 1555 2.13
LINK OG SER C 158 MG MG C 890 1555 1555 2.51
LINK MG MG C 890 O2B ADP C 891 1555 1555 2.65
LINK MG MG C 890 O1B ADP C 891 1555 1555 2.58
LINK MG MG C 890 O2 VO4 C 892 1555 1555 2.53
LINK MG MG C 890 O HOH C 897 1555 1555 2.86
LINK MG MG C 890 O HOH C 909 1555 1555 2.24
LINK O2B ADP C 891 V VO4 C 892 1555 1555 1.79
LINK OG1 THR D 108 MG MG D 893 1555 1555 2.32
LINK OG SER D 158 MG MG D 893 1555 1555 2.43
LINK MG MG D 893 O3B ADP D 894 1555 1555 2.58
LINK MG MG D 893 O2B ADP D 894 1555 1555 2.89
LINK MG MG D 893 O3 VO4 D 895 1555 1555 2.37
LINK MG MG D 893 O HOH D 906 1555 1555 2.29
LINK O3B ADP D 894 V VO4 D 895 1555 1555 1.69
CISPEP 1 MET C 696 PRO C 697 0 0.08
SITE 1 AC1 6 THR A 108 SER A 158 ADP A 791 VO4 A 792
SITE 2 AC1 6 HOH A 805 HOH A 808
SITE 1 AC2 11 SER A 103 GLY A 104 LYS A 107 ASN A 154
SITE 2 AC2 11 SER A 157 SER A 158 TYR A 388 GLY A 389
SITE 3 AC2 11 MG A 790 ADP A 791 HOH A 805
SITE 1 AC3 6 THR B 108 SER B 158 ADP B 794 VO4 B 795
SITE 2 AC3 6 HOH B 796 HOH B 797
SITE 1 AC4 11 SER B 103 GLY B 104 LYS B 107 ASN B 154
SITE 2 AC4 11 SER B 157 SER B 158 TYR B 388 GLY B 389
SITE 3 AC4 11 MG B 793 ADP B 794 HOH B 797
SITE 1 AC5 6 THR C 108 SER C 158 ADP C 891 VO4 C 892
SITE 2 AC5 6 HOH C 897 HOH C 909
SITE 1 AC6 10 SER C 103 GLY C 104 LYS C 107 ASN C 154
SITE 2 AC6 10 SER C 157 SER C 158 TYR C 388 GLY C 389
SITE 3 AC6 10 MG C 890 ADP C 891
SITE 1 AC7 5 THR D 108 SER D 158 ADP D 894 VO4 D 895
SITE 2 AC7 5 HOH D 906
SITE 1 AC8 10 SER D 103 GLY D 104 LYS D 107 ASN D 154
SITE 2 AC8 10 SER D 157 SER D 158 GLY D 389 MG D 893
SITE 3 AC8 10 ADP D 894 HOH D 906
SITE 1 AC9 14 ASN A 49 LYS A 52 TYR A 57 GLY A 104
SITE 2 AC9 14 ALA A 105 GLY A 106 LYS A 107 THR A 108
SITE 3 AC9 14 GLU A 109 ASN A 154 ASN A 156 MG A 790
SITE 4 AC9 14 VO4 A 792 HOH A 805
SITE 1 BC1 14 ASN B 49 LYS B 52 TYR B 57 GLY B 104
SITE 2 BC1 14 ALA B 105 GLY B 106 LYS B 107 THR B 108
SITE 3 BC1 14 GLU B 109 ASN B 154 ASN B 156 MG B 793
SITE 4 BC1 14 VO4 B 795 HOH B 797
SITE 1 BC2 17 ASN C 49 PRO C 50 LYS C 52 TYR C 57
SITE 2 BC2 17 GLU C 102 GLY C 104 ALA C 105 GLY C 106
SITE 3 BC2 17 LYS C 107 THR C 108 GLU C 109 ASN C 154
SITE 4 BC2 17 ASN C 156 MG C 890 VO4 C 892 HOH C 897
SITE 5 BC2 17 HOH C 909
SITE 1 BC3 17 ASN D 49 PRO D 50 LYS D 52 TYR D 57
SITE 2 BC3 17 GLU D 102 GLY D 104 ALA D 105 GLY D 106
SITE 3 BC3 17 LYS D 107 THR D 108 GLU D 109 ASN D 154
SITE 4 BC3 17 ASN D 156 MG D 893 VO4 D 895 HOH D 905
SITE 5 BC3 17 HOH D 906
CRYST1 51.818 143.667 236.050 90.00 94.86 90.00 P 1 21 1 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 0.019298 0.000000 0.001641 0.00000
SCALE2 0.000000 0.006961 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004252 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
