HEADER MOTOR PROTEIN 03-SEP-04 1W7I
TITLE CRYSTAL STRUCTURE OF MYOSIN V MOTOR WITHOUT NUCLEOTIDE SOAKED IN 10 MM
TITLE 2 MGADP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYOSIN VA;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: MOTOR DOMAIN, RESIDUES 1-792;
COMPND 5 SYNONYM: MYOSIN 5A, DILUTE MYOSIN HEAVY CHAIN, NON-MUSCLE, MYOSIN
COMPND 6 HEAVY CHAIN P190, MYOSIN-V;
COMPND 7 ENGINEERED: YES;
COMPND 8 OTHER_DETAILS: SOAKED MGADP;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: MYOSIN LIGHT CHAIN 1, SLOW-TWITCH MUSCLE A ISOFORM;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: RESIDUES 59-208;
COMPND 13 SYNONYM: MLC1SA;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 12 ORGANISM_COMMON: HUMAN;
SOURCE 13 ORGANISM_TAXID: 9606;
SOURCE 14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 15 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 17 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS UNCONVENTIONAL MYOSIN, MYOSIN V, CHICKEN, MOLECULAR MOTOR, ATPASE,
KEYWDS 2 ELC, IQ MOTIF, MUSCLE PROTEIN, MGADP, MOTOR PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR P.-D.COUREUX,H.L.SWEENEY,A.HOUDUSSE
REVDAT 4 13-DEC-23 1W7I 1 REMARK
REVDAT 3 16-SEP-15 1W7I 1 COMPND SOURCE KEYWDS JRNL
REVDAT 3 2 1 REMARK VERSN FORMUL MASTER
REVDAT 2 24-FEB-09 1W7I 1 VERSN
REVDAT 1 22-FEB-05 1W7I 0
JRNL AUTH P.-D.COUREUX,H.L.SWEENEY,A.HOUDUSSE
JRNL TITL THREE MYOSIN V STRUCTURES DELINEATE ESSENTIAL FEATURES OF
JRNL TITL 2 CHEMO-MECHANICAL TRANSDUCTION
JRNL REF EMBO J. V. 23 4527 2004
JRNL REFN ISSN 0261-4189
JRNL PMID 15510214
JRNL DOI 10.1038/SJ.EMBOJ.7600458
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 111.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 21972
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : 0.252
REMARK 3 R VALUE (WORKING SET) : 0.248
REMARK 3 FREE R VALUE : 0.318
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1176
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6872
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 27
REMARK 3 SOLVENT ATOMS : 11
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 56.70
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.56000
REMARK 3 B22 (A**2) : -1.71000
REMARK 3 B33 (A**2) : -0.35000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 1.23000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.550
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.411
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.824
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1W7I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-SEP-04.
REMARK 100 THE DEPOSITION ID IS D_1290016006.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-APR-03
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.30
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.934
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21972
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 111.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 88.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.28400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.100
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 1OE9
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.70
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% PEG 8000, 50 MM MOPS PH 6.5, 2 MM
REMARK 280 DTT AND 2 MM NAN3, PH 6.30
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 49.62650
REMARK 290 SMTRY3 2 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 400
REMARK 400 COMPOUND
REMARK 400 MYOSIN VA: PROCESSIVE ACTIN-BASED MOTOR THAT CAN MOVE IN
REMARK 400 LARGE STEPS. POSSIBLY INVOLVED IN MELANOSOME TRANSPORT.
REMARK 400 USUALLYASSOCIATED WITH MYOSIN LIGHT-CHAINS.
REMARK 400
REMARK 400 MYOSIN LIGHT-CHAIN: THIS PROTEIN IS SIMILAR TO OTHER
REMARK 400 EF-HAND CALCIUM-BINDING PROTEINS BUT DOES NOT BIND
REMARK 400 CALCIUM.
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 ALA A 2
REMARK 465 ALA A 3
REMARK 465 SER A 4
REMARK 465 THR A 382
REMARK 465 ALA A 383
REMARK 465 THR A 384
REMARK 465 GLU A 385
REMARK 465 ASP A 595
REMARK 465 GLU A 596
REMARK 465 GLU A 597
REMARK 465 LYS A 598
REMARK 465 ALA A 599
REMARK 465 ILE A 600
REMARK 465 SER A 601
REMARK 465 PRO A 602
REMARK 465 THR A 603
REMARK 465 SER A 604
REMARK 465 ALA A 605
REMARK 465 THR A 606
REMARK 465 PRO A 607
REMARK 465 SER A 608
REMARK 465 GLY A 609
REMARK 465 ARG A 610
REMARK 465 VAL A 611
REMARK 465 PRO A 612
REMARK 465 LEU A 613
REMARK 465 SER A 614
REMARK 465 ARG A 615
REMARK 465 THR A 616
REMARK 465 PRO A 617
REMARK 465 VAL A 618
REMARK 465 LYS A 619
REMARK 465 PRO A 620
REMARK 465 ALA A 621
REMARK 465 LYS A 622
REMARK 465 ALA A 623
REMARK 465 ARG A 624
REMARK 465 PRO A 625
REMARK 465 GLY A 626
REMARK 465 GLN A 627
REMARK 465 THR A 628
REMARK 465 SER A 629
REMARK 465 LYS A 630
REMARK 465 GLU A 631
REMARK 465 MET B 1
REMARK 465 ILE B 2
REMARK 465 GLY B 82
REMARK 465 GLN B 83
REMARK 465 GLY B 84
REMARK 465 VAL B 151
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 LEU A 6 CG CD1 CD2
REMARK 470 LYS A 9 CE NZ
REMARK 470 GLU A 19 CG CD OE1 OE2
REMARK 470 LYS A 23 CG CD CE NZ
REMARK 470 LEU A 27 CD1 CD2
REMARK 470 LYS A 29 CG CD CE NZ
REMARK 470 LYS A 32 CG CD CE NZ
REMARK 470 LYS A 36 CG CD CE NZ
REMARK 470 ARG A 41 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 43 CG CD OE1 OE2
REMARK 470 GLU A 44 CG CD OE1 OE2
REMARK 470 LYS A 46 CG CD CE NZ
REMARK 470 LYS A 55 CG CD CE NZ
REMARK 470 LYS A 57 CG CD CE NZ
REMARK 470 LEU A 80 CD1 CD2
REMARK 470 LYS A 97 CE NZ
REMARK 470 ILE A 105 CG1 CG2 CD1
REMARK 470 GLU A 121 CG CD OE1 OE2
REMARK 470 ASP A 122 CG OD1 OD2
REMARK 470 LYS A 148 CE NZ
REMARK 470 GLU A 154 CG CD OE1 OE2
REMARK 470 GLU A 189 CG CD OE1 OE2
REMARK 470 ASN A 191 CG OD1 ND2
REMARK 470 GLU A 194 CG CD OE1 OE2
REMARK 470 LYS A 195 CG CD CE NZ
REMARK 470 LYS A 230 CG CD CE NZ
REMARK 470 ARG A 231 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 234 CG1 CG2 CD1
REMARK 470 ARG A 327 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 353 CG CD CE NZ
REMARK 470 LEU A 380 CG CD1 CD2
REMARK 470 TYR A 387 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 389 CG CD CE NZ
REMARK 470 LYS A 421 CG CD CE NZ
REMARK 470 LEU A 423 CG CD1 CD2
REMARK 470 LYS A 471 CG CD CE NZ
REMARK 470 LYS A 479 CG CD CE NZ
REMARK 470 TRP A 484 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 484 CZ3 CH2
REMARK 470 LEU A 486 CG CD1 CD2
REMARK 470 LYS A 546 CG CD CE NZ
REMARK 470 LYS A 551 CD CE NZ
REMARK 470 GLU A 574 CG CD OE1 OE2
REMARK 470 LYS A 578 CG CD CE NZ
REMARK 470 LYS A 581 CD CE NZ
REMARK 470 LYS A 584 CG CD CE NZ
REMARK 470 LYS A 585 CG CD CE NZ
REMARK 470 LYS A 587 CG CD CE NZ
REMARK 470 HIS A 632 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 633 CG CD CE NZ
REMARK 470 LYS A 634 CD CE NZ
REMARK 470 LYS A 668 CE NZ
REMARK 470 ILE A 693 CG1 CG2 CD1
REMARK 470 GLN A 717 CG CD OE1 NE2
REMARK 470 LYS A 718 CG CD CE NZ
REMARK 470 ARG A 724 CD NE CZ NH1 NH2
REMARK 470 LYS A 729 CD CE NZ
REMARK 470 LYS A 734 CG CD CE NZ
REMARK 470 LEU A 735 CG CD1 CD2
REMARK 470 LYS A 739 CG CD CE NZ
REMARK 470 ASP A 740 CG OD1 OD2
REMARK 470 LYS A 761 CG CD CE NZ
REMARK 470 LYS A 766 CE NZ
REMARK 470 ARG A 768 CD NE CZ NH1 NH2
REMARK 470 CYS A 771 SG
REMARK 470 ARG A 773 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 779 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 782 CG CD1 CD2
REMARK 470 LYS A 785 CD CE NZ
REMARK 470 LYS A 786 CE NZ
REMARK 470 MET A 788 CG SD CE
REMARK 470 ARG A 791 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 6 CG CD CE NZ
REMARK 470 GLU B 10 CG CD OE1 OE2
REMARK 470 GLU B 14 CG CD OE1 OE2
REMARK 470 GLU B 17 CD OE1 OE2
REMARK 470 LYS B 26 CE NZ
REMARK 470 LEU B 28 CG CD1 CD2
REMARK 470 LYS B 56 CG CD CE NZ
REMARK 470 SER B 57 OG
REMARK 470 ASP B 58 CG OD1 OD2
REMARK 470 LYS B 61 CD CE NZ
REMARK 470 ARG B 63 CG CD NE CZ NH1 NH2
REMARK 470 VAL B 65 CG1 CG2
REMARK 470 LYS B 79 CG CD CE NZ
REMARK 470 ASN B 80 CG OD1 ND2
REMARK 470 ARG B 81 CG CD NE CZ NH1 NH2
REMARK 470 THR B 85 OG1 CG2
REMARK 470 GLU B 87 CG CD OE1 OE2
REMARK 470 ASP B 88 CG OD1 OD2
REMARK 470 GLU B 91 CG CD OE1 OE2
REMARK 470 ARG B 94 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 98 CG CD CE NZ
REMARK 470 GLU B 99 CG CD OE1 OE2
REMARK 470 LYS B 103 CG CD CE NZ
REMARK 470 GLU B 108 CG CD OE1 OE2
REMARK 470 LEU B 109 CG CD1 CD2
REMARK 470 LYS B 119 CE NZ
REMARK 470 LEU B 129 CG CD1 CD2
REMARK 470 GLU B 133 CG CD OE1 OE2
REMARK 470 SER B 135 OG
REMARK 470 CYS B 138 SG
REMARK 470 ILE B 139 CG1 CG2 CD1
REMARK 470 TYR B 141 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU B 142 CG CD OE1 OE2
REMARK 470 LYS B 146 CG CD CE NZ
REMARK 470 HIS B 147 CG ND1 CD2 CE1 NE2
REMARK 470 ILE B 148 CG1 CG2 CD1
REMARK 470 LEU B 149 CG CD1 CD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE1 GLU A 144 OH TYR A 179 2.13
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 ASP A 30 CB - CG - OD2 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ASP A 95 CB - CG - OD2 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ASP A 507 CB - CG - OD2 ANGL. DEV. = 6.0 DEGREES
REMARK 500 ASP A 510 CB - CG - OD2 ANGL. DEV. = 8.0 DEGREES
REMARK 500 ASP A 674 CB - CG - OD2 ANGL. DEV. = 7.2 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 TYR A 10 -22.40 82.73
REMARK 500 VAL A 21 -56.70 66.60
REMARK 500 LEU A 42 -165.29 -104.49
REMARK 500 GLU A 44 9.75 150.10
REMARK 500 ASP A 47 106.23 -167.79
REMARK 500 LEU A 48 142.53 144.70
REMARK 500 LYS A 57 14.18 50.41
REMARK 500 SER A 96 18.62 -148.29
REMARK 500 LYS A 148 -80.30 -71.00
REMARK 500 GLN A 149 -26.71 -34.54
REMARK 500 ARG A 152 -9.14 -52.64
REMARK 500 TYR A 179 -72.86 -58.51
REMARK 500 PHE A 180 -30.77 -37.27
REMARK 500 VAL A 183 56.26 -102.26
REMARK 500 SER A 184 -30.64 -150.22
REMARK 500 SER A 186 137.94 70.18
REMARK 500 SER A 188 -84.63 -66.54
REMARK 500 ASN A 191 58.28 37.18
REMARK 500 GLU A 193 -60.01 -27.73
REMARK 500 TYR A 232 77.45 39.44
REMARK 500 ILE A 261 -38.56 -38.03
REMARK 500 PHE A 274 47.46 -108.54
REMARK 500 ARG A 278 77.07 56.21
REMARK 500 SER A 293 78.16 -111.26
REMARK 500 ASP A 319 -38.99 -35.71
REMARK 500 VAL A 338 105.83 -55.36
REMARK 500 ASP A 346 76.34 30.05
REMARK 500 PRO A 351 149.42 -38.79
REMARK 500 LYS A 353 73.39 49.85
REMARK 500 THR A 443 92.80 -163.00
REMARK 500 PHE A 444 -160.51 -79.78
REMARK 500 SER A 448 -157.99 -122.88
REMARK 500 MET A 503 11.64 53.91
REMARK 500 ASN A 533 -42.95 77.55
REMARK 500 ASP A 570 58.38 -160.86
REMARK 500 SER A 582 51.66 -102.49
REMARK 500 LYS A 585 11.84 -157.95
REMARK 500 LYS A 633 103.17 69.15
REMARK 500 GLU A 649 -75.95 -67.66
REMARK 500 THR A 650 -55.34 -22.57
REMARK 500 PHE A 671 67.39 10.79
REMARK 500 ALA A 684 36.16 -73.13
REMARK 500 CYS A 685 14.66 -144.75
REMARK 500 LEU A 737 -80.79 -71.18
REMARK 500 ASP A 738 112.15 -31.94
REMARK 500 ARG A 792 48.83 -91.54
REMARK 500 ARG B 21 32.63 -99.13
REMARK 500 VAL B 22 -44.33 -140.93
REMARK 500 ASN B 42 58.28 -141.71
REMARK 500 SER B 62 -20.74 -144.95
REMARK 500
REMARK 500 THIS ENTRY HAS 55 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 1796
DBREF 1W7I A 1 792 UNP Q02440 MY5A_CHICK 1 792
DBREF 1W7I A 793 795 PDB 1W7I 1W7I 793 795
DBREF 1W7I B 1 1 PDB 1W7I 1W7I 1 1
DBREF 1W7I B 2 151 UNP P14649 MLEY_HUMAN 59 208
SEQRES 1 A 795 MET ALA ALA SER GLU LEU TYR THR LYS TYR ALA ARG VAL
SEQRES 2 A 795 TRP ILE PRO ASP PRO GLU GLU VAL TRP LYS SER ALA GLU
SEQRES 3 A 795 LEU LEU LYS ASP TYR LYS PRO GLY ASP LYS VAL LEU GLN
SEQRES 4 A 795 LEU ARG LEU GLU GLU GLY LYS ASP LEU GLU TYR CYS LEU
SEQRES 5 A 795 ASP PRO LYS THR LYS GLU LEU PRO PRO LEU ARG ASN PRO
SEQRES 6 A 795 ASP ILE LEU VAL GLY GLU ASN ASP LEU THR ALA LEU SER
SEQRES 7 A 795 TYR LEU HIS GLU PRO ALA VAL LEU HIS ASN LEU LYS VAL
SEQRES 8 A 795 ARG PHE ILE ASP SER LYS LEU ILE TYR THR TYR CYS GLY
SEQRES 9 A 795 ILE VAL LEU VAL ALA ILE ASN PRO TYR GLU GLN LEU PRO
SEQRES 10 A 795 ILE TYR GLY GLU ASP ILE ILE ASN ALA TYR SER GLY GLN
SEQRES 11 A 795 ASN MET GLY ASP MET ASP PRO HIS ILE PHE ALA VAL ALA
SEQRES 12 A 795 GLU GLU ALA TYR LYS GLN MET ALA ARG ASP GLU ARG ASN
SEQRES 13 A 795 GLN SER ILE ILE VAL SER GLY GLU SER GLY ALA GLY LYS
SEQRES 14 A 795 THR VAL SER ALA LYS TYR ALA MET ARG TYR PHE ALA THR
SEQRES 15 A 795 VAL SER GLY SER ALA SER GLU ALA ASN VAL GLU GLU LYS
SEQRES 16 A 795 VAL LEU ALA SER ASN PRO ILE MET GLU SER ILE GLY ASN
SEQRES 17 A 795 ALA LYS THR THR ARG ASN ASP ASN SER SER ARG PHE GLY
SEQRES 18 A 795 LYS TYR ILE GLU ILE GLY PHE ASP LYS ARG TYR ARG ILE
SEQRES 19 A 795 ILE GLY ALA ASN MET ARG THR TYR LEU LEU GLU LYS SER
SEQRES 20 A 795 ARG VAL VAL PHE GLN ALA GLU GLU GLU ARG ASN TYR HIS
SEQRES 21 A 795 ILE PHE TYR GLN LEU CYS ALA SER ALA ALA LEU PRO GLU
SEQRES 22 A 795 PHE LYS THR LEU ARG LEU GLY ASN ALA ASN TYR PHE HIS
SEQRES 23 A 795 TYR THR LYS GLN GLY GLY SER PRO VAL ILE ASP GLY ILE
SEQRES 24 A 795 ASP ASP ALA LYS GLU MET VAL ASN THR ARG GLN ALA CYS
SEQRES 25 A 795 THR LEU LEU GLY ILE SER ASP SER TYR GLN MET GLY ILE
SEQRES 26 A 795 PHE ARG ILE LEU ALA GLY ILE LEU HIS LEU GLY ASN VAL
SEQRES 27 A 795 GLU PHE ALA SER ARG ASP SER ASP SER CYS ALA ILE PRO
SEQRES 28 A 795 PRO LYS HIS ASP PRO LEU THR ILE PHE CYS ASP LEU MET
SEQRES 29 A 795 GLY VAL ASP TYR GLU GLU MET ALA HIS TRP LEU CYS HIS
SEQRES 30 A 795 ARG LYS LEU ALA THR ALA THR GLU THR TYR ILE LYS PRO
SEQRES 31 A 795 ILE SER LYS LEU HIS ALA ILE ASN ALA ARG ASP ALA LEU
SEQRES 32 A 795 ALA LYS HIS ILE TYR ALA ASN LEU PHE ASN TRP ILE VAL
SEQRES 33 A 795 ASP HIS VAL ASN LYS ALA LEU HIS SER THR VAL LYS GLN
SEQRES 34 A 795 HIS SER PHE ILE GLY VAL LEU ASP ILE TYR GLY PHE GLU
SEQRES 35 A 795 THR PHE GLU ILE ASN SER PHE GLU GLN PHE CYS ILE ASN
SEQRES 36 A 795 TYR ALA ASN GLU LYS LEU GLN GLN GLN PHE ASN MET HIS
SEQRES 37 A 795 VAL PHE LYS LEU GLU GLN GLU GLU TYR MET LYS GLU GLN
SEQRES 38 A 795 ILE PRO TRP THR LEU ILE ASP PHE TYR ASP ASN GLN PRO
SEQRES 39 A 795 CYS ILE ASN LEU ILE GLU ALA LYS MET GLY VAL LEU ASP
SEQRES 40 A 795 LEU LEU ASP GLU GLU CYS LYS MET PRO LYS GLY SER ASP
SEQRES 41 A 795 ASP THR TRP ALA GLN LYS LEU TYR ASN THR HIS LEU ASN
SEQRES 42 A 795 LYS CYS ALA LEU PHE GLU LYS PRO ARG LEU SER ASN LYS
SEQRES 43 A 795 ALA PHE ILE ILE LYS HIS PHE ALA ASP LYS VAL GLU TYR
SEQRES 44 A 795 GLN CYS GLU GLY PHE LEU GLU LYS ASN LYS ASP THR VAL
SEQRES 45 A 795 TYR GLU GLU GLN ILE LYS VAL LEU LYS SER SER LYS LYS
SEQRES 46 A 795 PHE LYS LEU LEU PRO GLU LEU PHE GLN ASP GLU GLU LYS
SEQRES 47 A 795 ALA ILE SER PRO THR SER ALA THR PRO SER GLY ARG VAL
SEQRES 48 A 795 PRO LEU SER ARG THR PRO VAL LYS PRO ALA LYS ALA ARG
SEQRES 49 A 795 PRO GLY GLN THR SER LYS GLU HIS LYS LYS THR VAL GLY
SEQRES 50 A 795 HIS GLN PHE ARG ASN SER LEU HIS LEU LEU MET GLU THR
SEQRES 51 A 795 LEU ASN ALA THR THR PRO HIS TYR VAL ARG CYS ILE LYS
SEQRES 52 A 795 PRO ASN ASP PHE LYS PHE PRO PHE THR PHE ASP GLU LYS
SEQRES 53 A 795 ARG ALA VAL GLN GLN LEU ARG ALA CYS GLY VAL LEU GLU
SEQRES 54 A 795 THR ILE ARG ILE SER ALA ALA GLY PHE PRO SER ARG TRP
SEQRES 55 A 795 THR TYR GLN GLU PHE PHE SER ARG TYR ARG VAL LEU MET
SEQRES 56 A 795 LYS GLN LYS ASP VAL LEU SER ASP ARG LYS GLN THR CYS
SEQRES 57 A 795 LYS ASN VAL LEU GLU LYS LEU ILE LEU ASP LYS ASP LYS
SEQRES 58 A 795 TYR GLN PHE GLY LYS THR LYS ILE PHE PHE ARG ALA GLY
SEQRES 59 A 795 GLN VAL ALA TYR LEU GLU LYS ILE ARG ALA ASP LYS LEU
SEQRES 60 A 795 ARG ALA ALA CYS ILE ARG ILE GLN LYS THR ILE ARG GLY
SEQRES 61 A 795 TRP LEU MET ARG LYS LYS TYR MET ARG MET ARG ARG GLY
SEQRES 62 A 795 ASP ALA
SEQRES 1 B 151 MET ILE GLU PHE ASN LYS ASP GLN LEU GLU GLU PHE LYS
SEQRES 2 B 151 GLU ALA PHE GLU LEU PHE ASP ARG VAL GLY ASP GLY LYS
SEQRES 3 B 151 ILE LEU TYR SER GLN CYS GLY ASP VAL MET ARG ALA LEU
SEQRES 4 B 151 GLY GLN ASN PRO THR ASN ALA GLU VAL LEU LYS VAL LEU
SEQRES 5 B 151 GLY ASN PRO LYS SER ASP GLU LEU LYS SER ARG ARG VAL
SEQRES 6 B 151 ASP PHE GLU THR PHE LEU PRO MET LEU GLN ALA VAL ALA
SEQRES 7 B 151 LYS ASN ARG GLY GLN GLY THR TYR GLU ASP TYR LEU GLU
SEQRES 8 B 151 GLY PHE ARG VAL PHE ASP LYS GLU GLY ASN GLY LYS VAL
SEQRES 9 B 151 MET GLY ALA GLU LEU ARG HIS VAL LEU THR THR LEU GLY
SEQRES 10 B 151 GLU LYS MET THR GLU GLU GLU VAL GLU THR VAL LEU ALA
SEQRES 11 B 151 GLY HIS GLU ASP SER ASN GLY CYS ILE ASN TYR GLU ALA
SEQRES 12 B 151 PHE LEU LYS HIS ILE LEU SER VAL
HET ADP A1796 27
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
FORMUL 3 ADP C10 H15 N5 O10 P2
FORMUL 4 HOH *11(H2 O)
HELIX 1 1 PRO A 65 VAL A 69 5 5
HELIX 2 2 LEU A 74 LEU A 77 5 4
HELIX 3 3 HIS A 81 LYS A 97 1 17
HELIX 4 4 GLY A 120 SER A 128 1 9
HELIX 5 5 ASN A 131 MET A 135 5 5
HELIX 6 6 HIS A 138 ARG A 152 1 15
HELIX 7 7 GLY A 168 VAL A 183 1 16
HELIX 8 8 ASN A 191 GLY A 207 1 17
HELIX 9 9 GLU A 245 VAL A 250 5 6
HELIX 10 10 TYR A 259 ALA A 267 1 9
HELIX 11 11 LEU A 271 LYS A 275 5 5
HELIX 12 12 PHE A 285 GLN A 290 1 6
HELIX 13 13 ASP A 300 GLY A 316 1 17
HELIX 14 14 SER A 318 VAL A 338 1 21
HELIX 15 15 HIS A 354 GLY A 365 1 12
HELIX 16 16 ASP A 367 CYS A 376 1 10
HELIX 17 17 SER A 392 LEU A 423 1 32
HELIX 18 18 SER A 448 GLU A 480 1 33
HELIX 19 19 ASN A 492 ALA A 501 1 10
HELIX 20 20 GLY A 504 MET A 515 1 12
HELIX 21 21 SER A 519 LEU A 532 1 14
HELIX 22 22 GLY A 563 LYS A 569 1 7
HELIX 23 23 TYR A 573 SER A 582 1 10
HELIX 24 24 LYS A 587 LEU A 592 1 6
HELIX 25 25 THR A 635 ALA A 653 1 19
HELIX 26 26 ASP A 674 ALA A 684 1 11
HELIX 27 27 GLY A 686 ALA A 695 1 10
HELIX 28 28 TYR A 704 TYR A 711 1 8
HELIX 29 29 ARG A 712 MET A 715 5 4
HELIX 30 30 ASP A 723 ILE A 736 1 14
HELIX 31 31 ASP A 738 ASP A 740 5 3
HELIX 32 32 GLY A 754 ARG A 792 1 39
HELIX 33 33 ASN B 5 PHE B 19 1 15
HELIX 34 34 SER B 30 LEU B 39 1 10
HELIX 35 35 THR B 44 GLY B 53 1 10
HELIX 36 36 LYS B 56 LYS B 61 1 6
HELIX 37 37 PHE B 67 LYS B 79 1 13
HELIX 38 38 TYR B 86 PHE B 96 1 11
HELIX 39 39 GLY B 106 THR B 115 1 10
HELIX 40 40 THR B 121 LEU B 129 1 9
HELIX 41 41 TYR B 141 SER B 150 1 10
SHEET 1 AA 4 ARG A 12 ASP A 17 0
SHEET 2 AA 4 VAL A 21 LEU A 27 -1 O VAL A 21 N ASP A 17
SHEET 3 AA 4 VAL A 37 LEU A 42 -1 O ARG A 41 N GLU A 26
SHEET 4 AA 4 GLY A 45 CYS A 51 -1 O GLY A 45 N LEU A 42
SHEET 1 AB 7 TYR A 100 CYS A 103 0
SHEET 2 AB 7 VAL A 106 ILE A 110 -1 O VAL A 106 N CYS A 103
SHEET 3 AB 7 THR A 655 ILE A 662 1 O TYR A 658 N LEU A 107
SHEET 4 AB 7 GLN A 157 SER A 162 1 O SER A 158 N HIS A 657
SHEET 5 AB 7 SER A 431 ASP A 437 1 O PHE A 432 N GLN A 157
SHEET 6 AB 7 GLY A 221 PHE A 228 -1 O LYS A 222 N ASP A 437
SHEET 7 AB 7 ILE A 234 TYR A 242 -1 N ILE A 235 O GLY A 227
SHEET 1 AC 2 ASN A 208 ALA A 209 0
SHEET 2 AC 2 SER A 217 SER A 218 -1 O SER A 217 N ALA A 209
SHEET 1 AD 2 ALA A 341 ARG A 343 0
SHEET 2 AD 2 SER A 347 ALA A 349 -1 O SER A 347 N ARG A 343
SHEET 1 AE 2 HIS A 377 LEU A 380 0
SHEET 2 AE 2 TYR A 387 PRO A 390 -1 O TYR A 387 N LEU A 380
SHEET 1 AF 3 PHE A 538 GLU A 539 0
SHEET 2 AF 3 ALA A 547 LYS A 551 -1 O ILE A 549 N GLU A 539
SHEET 3 AF 3 LYS A 556 GLN A 560 -1 O VAL A 557 N ILE A 550
SHEET 1 AG 3 SER A 700 THR A 703 0
SHEET 2 AG 3 LYS A 748 PHE A 751 -1 O ILE A 749 N TRP A 702
SHEET 3 AG 3 TYR A 742 PHE A 744 -1 O GLN A 743 N PHE A 750
SHEET 1 BA 2 LYS B 26 LEU B 28 0
SHEET 2 BA 2 ARG B 64 ASP B 66 -1 O VAL B 65 N ILE B 27
SHEET 1 BB 2 LYS B 103 MET B 105 0
SHEET 2 BB 2 CYS B 138 ASN B 140 -1 O ILE B 139 N VAL B 104
SITE 1 AC1 10 ASN A 111 PRO A 112 GLU A 114 TYR A 119
SITE 2 AC1 10 GLY A 166 GLY A 168 LYS A 169 THR A 170
SITE 3 AC1 10 VAL A 171 HOH A2005
CRYST1 54.926 99.253 112.513 90.00 101.78 90.00 P 1 21 1 2
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 0.018206 0.000000 0.003797 0.00000
SCALE2 0.000000 0.010075 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009079 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
