HEADER MOTOR PROTEIN 14-FEB-17 5N6A
TITLE CARDIAC MUSCLE MYOSIN MOTOR DOMAIN IN THE PRE-POWERSTROKE STATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MYOSIN-7;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: MYOSIN HEAVY CHAIN 7,MYOSIN HEAVY CHAIN SLOW ISOFORM,MYHC-
COMPND 5 SLOW,MYOSIN HEAVY CHAIN,CARDIAC MUSCLE BETA ISOFORM,MYHC-BETA
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS;
SOURCE 3 ORGANISM_COMMON: CATTLE;
SOURCE 4 ORGANISM_TAXID: 9913
KEYWDS MYOSIN, CARDIAC, PRE-POWERSTROKE, MOTOR PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR V.J.PLANELLES-HERRERO,J.J.HARTMAN,J.ROBERT-PAGANIN,F.I.MALIK,
AUTHOR 2 A.HOUDUSSE
REVDAT 3 17-JAN-24 5N6A 1 REMARK
REVDAT 2 16-AUG-17 5N6A 1 JRNL
REVDAT 1 09-AUG-17 5N6A 0
JRNL AUTH V.J.PLANELLES-HERRERO,J.J.HARTMAN,J.ROBERT-PAGANIN,
JRNL AUTH 2 F.I.MALIK,A.HOUDUSSE
JRNL TITL MECHANISTIC AND STRUCTURAL BASIS FOR ACTIVATION OF CARDIAC
JRNL TITL 2 MYOSIN FORCE PRODUCTION BY OMECAMTIV MECARBIL.
JRNL REF NAT COMMUN V. 8 190 2017
JRNL REFN ESSN 2041-1723
JRNL PMID 28775348
JRNL DOI 10.1038/S41467-017-00176-5
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.83
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 18783
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 + TEST SET) : 0.250
REMARK 3 R VALUE (WORKING SET) : 0.247
REMARK 3 FREE R VALUE : 0.320
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 940
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 9
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.29
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.67
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2979
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2840
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2830
REMARK 3 BIN R VALUE (WORKING SET) : 0.2810
REMARK 3 BIN FREE R VALUE : 0.3420
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 149
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5485
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 39
REMARK 3 SOLVENT ATOMS : 36
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 93.53
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 85.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.13640
REMARK 3 B22 (A**2) : -0.72830
REMARK 3 B33 (A**2) : -1.40810
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.530
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.527
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.901
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.843
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 5644 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 7635 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1928 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 148 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 830 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 5644 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 750 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 6469 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.23
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.49
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 24.31
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -22.6029 37.9161 -29.4712
REMARK 3 T TENSOR
REMARK 3 T11: -0.3047 T22: 0.4598
REMARK 3 T33: -0.2128 T12: -0.0399
REMARK 3 T13: -0.0092 T23: 0.0762
REMARK 3 L TENSOR
REMARK 3 L11: 0.9482 L22: 1.0647
REMARK 3 L33: 1.7968 L12: 0.3162
REMARK 3 L13: 0.0839 L23: 0.5530
REMARK 3 S TENSOR
REMARK 3 S11: 0.0998 S12: -0.1512 S13: 0.1351
REMARK 3 S21: 0.1301 S22: 0.0070 S23: 0.1596
REMARK 3 S31: 0.0904 S32: -0.3065 S33: -0.1069
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5N6A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1200003556.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-JUN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9762
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19862
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.020
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 13.40
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.28000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.3500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.02
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.13
REMARK 200 COMPLETENESS FOR SHELL (%) : 80.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.00
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.94000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.620
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 1QVI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 13% PEG 3350 (W/V), 5% TACSIMATE PH
REMARK 280 6.0, 5 MM TCEP, 10% GLYCEROL AND 3.3% DMSO, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 77.13000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 77.13000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 43.83000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 74.91500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 43.83000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 74.91500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 77.13000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 43.83000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 74.91500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 77.13000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 43.83000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 74.91500
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1420 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 33870 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1036 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 1
REMARK 465 VAL A 2
REMARK 465 ASP A 3
REMARK 465 ALA A 4
REMARK 465 GLU A 5
REMARK 465 MET A 6
REMARK 465 ALA A 7
REMARK 465 ALA A 8
REMARK 465 PHE A 9
REMARK 465 ILE A 201
REMARK 465 GLY A 202
REMARK 465 ASP A 203
REMARK 465 ARG A 204
REMARK 465 SER A 205
REMARK 465 LYS A 206
REMARK 465 LYS A 207
REMARK 465 GLU A 208
REMARK 465 GLN A 209
REMARK 465 ALA A 210
REMARK 465 THR A 211
REMARK 465 GLY A 212
REMARK 465 LYS A 213
REMARK 465 GLY A 214
REMARK 465 THR A 215
REMARK 465 LEU A 297
REMARK 465 LEU A 298
REMARK 465 ILE A 569
REMARK 465 LYS A 570
REMARK 465 GLY A 571
REMARK 465 LYS A 572
REMARK 465 ASP A 628
REMARK 465 THR A 629
REMARK 465 PRO A 630
REMARK 465 ILE A 631
REMARK 465 GLU A 632
REMARK 465 LYS A 633
REMARK 465 GLY A 634
REMARK 465 LYS A 635
REMARK 465 GLY A 636
REMARK 465 LYS A 637
REMARK 465 ALA A 638
REMARK 465 LYS A 639
REMARK 465 LYS A 640
REMARK 465 GLY A 641
REMARK 465 SER A 642
REMARK 465 SER A 643
REMARK 465 ARG A 719
REMARK 465 GLN A 720
REMARK 465 ARG A 721
REMARK 465 TYR A 722
REMARK 465 ARG A 723
REMARK 465 ILE A 724
REMARK 465 LEU A 725
REMARK 465 ASN A 726
REMARK 465 PRO A 727
REMARK 465 ALA A 728
REMARK 465 ALA A 729
REMARK 465 ILE A 730
REMARK 465 PRO A 731
REMARK 465 GLU A 732
REMARK 465 GLY A 733
REMARK 465 GLN A 734
REMARK 465 PHE A 735
REMARK 465 SER A 748
REMARK 465 LEU A 749
REMARK 465 MET A 776
REMARK 465 ARG A 777
REMARK 465 ASP A 778
REMARK 465 GLU A 779
REMARK 465 ARG A 780
REMARK 465 LEU A 781
REMARK 465 SER A 782
REMARK 465 ARG A 783
REMARK 465 ILE A 784
REMARK 465 ILE A 785
REMARK 465 THR A 786
REMARK 465 ARG A 787
REMARK 465 ILE A 788
REMARK 465 GLN A 789
REMARK 465 ALA A 790
REMARK 465 GLN A 791
REMARK 465 SER A 792
REMARK 465 ARG A 793
REMARK 465 GLY A 794
REMARK 465 VAL A 795
REMARK 465 LEU A 796
REMARK 465 SER A 797
REMARK 465 ARG A 798
REMARK 465 MET A 799
REMARK 465 GLU A 800
REMARK 465 PHE A 801
REMARK 465 LYS A 802
REMARK 465 LYS A 803
REMARK 465 LEU A 804
REMARK 465 LEU A 805
REMARK 465 GLU A 806
REMARK 465 ARG A 807
REMARK 465 ARG A 808
REMARK 465 ASP A 809
REMARK 465 SER A 810
REMARK 465 LEU A 811
REMARK 465 LEU A 812
REMARK 465 ILE A 813
REMARK 465 ILE A 814
REMARK 465 GLN A 815
REMARK 465 TRP A 816
REMARK 465 ASN A 817
REMARK 465 ILE A 818
REMARK 465 ARG A 819
REMARK 465 ALA A 820
REMARK 465 PHE A 821
REMARK 465 MET A 822
REMARK 465 GLY A 823
REMARK 465 VAL A 824
REMARK 465 LYS A 825
REMARK 465 ASN A 826
REMARK 465 TRP A 827
REMARK 465 PRO A 828
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 GLU A 11 CG CD OE1 OE2
REMARK 470 ARG A 23 NE CZ NH1 NH2
REMARK 470 LEU A 24 CG CD1 CD2
REMARK 470 ASP A 32 CG OD1 OD2
REMARK 470 LYS A 67 CG CD CE NZ
REMARK 470 LYS A 72 CG CD CE NZ
REMARK 470 LYS A 86 CG CD CE NZ
REMARK 470 MET A 92 SD CE
REMARK 470 GLU A 107 CD OE1 OE2
REMARK 470 VAL A 123 CG2
REMARK 470 THR A 124 OG1 CG2
REMARK 470 ILE A 125 CG2 CD1
REMARK 470 VAL A 139 CG2
REMARK 470 LYS A 146 CG CD CE NZ
REMARK 470 ILE A 154 CG2 CD1
REMARK 470 ILE A 157 CG2 CD1
REMARK 470 TYR A 164 CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ARG A 190 CD NE CZ NH1 NH2
REMARK 470 SER A 260 OG
REMARK 470 LEU A 267 CG CD1 CD2
REMARK 470 LYS A 278 CG CD CE NZ
REMARK 470 GLU A 296 CG CD OE1 OE2
REMARK 470 MET A 300 CG SD CE
REMARK 470 TYR A 308 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 327 CG CD OE1 OE2
REMARK 470 MET A 357 SD CE
REMARK 470 PHE A 359 CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 367 CD CE NZ
REMARK 470 GLN A 368 CG CD OE1 NE2
REMARK 470 ARG A 369 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 370 CG CD OE1 OE2
REMARK 470 GLU A 371 CG CD OE1 OE2
REMARK 470 GLU A 374 CD OE1 OE2
REMARK 470 LYS A 383 CD CE NZ
REMARK 470 TYR A 386 CD1 CD2 CE1 CE2 CZ OH
REMARK 470 MET A 388 CG SD CE
REMARK 470 HIS A 401 ND1 CD2 CE1 NE2
REMARK 470 TYR A 410 CD2 CE1 CE2 CZ OH
REMARK 470 VAL A 417 CG2
REMARK 470 GLN A 418 CD OE1 NE2
REMARK 470 TYR A 422 CD1 CD2 CE1 CE2 CZ OH
REMARK 470 VAL A 431 CG1
REMARK 470 GLU A 433 CD OE1 OE2
REMARK 470 GLN A 451 CG CD OE1 NE2
REMARK 470 ARG A 453 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 454 CD OE1 NE2
REMARK 470 PHE A 456 CD1 CD2 CE1 CE2 CZ
REMARK 470 PHE A 470 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 484 CD CE NZ
REMARK 470 VAL A 495 CG1 CG2
REMARK 470 LYS A 502 CG CD CE NZ
REMARK 470 LYS A 503 CG CD CE NZ
REMARK 470 LYS A 526 CG CD CE NZ
REMARK 470 MET A 539 CG SD CE
REMARK 470 LYS A 549 CD CE NZ
REMARK 470 LYS A 551 CG CD CE NZ
REMARK 470 ASP A 554 OD1 OD2
REMARK 470 LEU A 579 CG CD1 CD2
REMARK 470 ASP A 607 CG OD1 OD2
REMARK 470 LYS A 615 CD CE NZ
REMARK 470 MET A 616 SD CE
REMARK 470 GLN A 645 CG CD OE1 NE2
REMARK 470 ARG A 663 CD NE CZ NH1 NH2
REMARK 470 THR A 678 CG2
REMARK 470 ASN A 686 CG OD1 ND2
REMARK 470 MET A 690 SD CE
REMARK 470 PHE A 718 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 762 CG CD CE NZ
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 GLU A 11 -142.11 -167.49
REMARK 500 LEU A 16 116.78 -160.09
REMARK 500 ARG A 17 -62.30 66.77
REMARK 500 ARG A 23 -178.48 68.54
REMARK 500 ARG A 23 -178.48 61.39
REMARK 500 PHE A 31 -87.59 -115.70
REMARK 500 ASP A 32 -155.84 57.10
REMARK 500 GLU A 55 -91.21 -166.96
REMARK 500 GLU A 62 -68.97 69.41
REMARK 500 THR A 63 -7.28 63.24
REMARK 500 HIS A 65 12.65 -156.08
REMARK 500 LYS A 67 -143.58 -160.38
REMARK 500 THR A 68 127.75 -28.67
REMARK 500 VAL A 71 89.58 -55.32
REMARK 500 LYS A 72 -59.07 -136.86
REMARK 500 GLU A 73 -127.44 50.54
REMARK 500 VAL A 76 -74.32 38.91
REMARK 500 LEU A 77 96.98 51.96
REMARK 500 PRO A 82 -0.47 -57.30
REMARK 500 ASP A 85 119.12 -37.05
REMARK 500 ALA A 91 1.68 -66.86
REMARK 500 LEU A 120 -71.27 -118.85
REMARK 500 ASN A 126 123.02 -37.26
REMARK 500 HIS A 153 141.07 -175.07
REMARK 500 ILE A 198 -52.52 -145.26
REMARK 500 ASN A 240 51.22 -114.06
REMARK 500 SER A 260 -166.53 -167.90
REMARK 500 TYR A 266 -142.48 -129.23
REMARK 500 LEU A 267 74.59 -57.79
REMARK 500 ALA A 279 -15.47 76.93
REMARK 500 THR A 304 -119.90 -142.40
REMARK 500 PRO A 307 -141.06 -85.07
REMARK 500 TYR A 308 -84.33 41.87
REMARK 500 ILE A 313 -40.32 -136.86
REMARK 500 SER A 314 48.29 -66.30
REMARK 500 LYS A 365 -136.76 -84.69
REMARK 500 ARG A 369 -8.41 -47.08
REMARK 500 GLU A 370 -78.80 -73.55
REMARK 500 GLU A 371 61.56 -157.62
REMARK 500 GLU A 379 58.28 -94.51
REMARK 500 MET A 388 64.76 14.02
REMARK 500 LEU A 395 -49.27 76.38
REMARK 500 HIS A 401 75.27 -118.10
REMARK 500 TYR A 410 90.42 -66.83
REMARK 500 ALA A 445 32.48 -77.39
REMARK 500 THR A 446 -60.20 -144.95
REMARK 500 LYS A 450 -86.50 -165.39
REMARK 500 GLN A 451 59.10 -151.67
REMARK 500 ARG A 453 -176.27 145.25
REMARK 500 GLN A 454 -151.13 68.49
REMARK 500
REMARK 500 THIS ENTRY HAS 73 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 903 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 185 OG1
REMARK 620 2 SER A 242 OG 78.0
REMARK 620 3 ADP A 901 O3B 90.1 157.1
REMARK 620 4 PO4 A 902 O4 151.8 101.5 79.9
REMARK 620 5 HOH A1003 O 107.2 92.5 109.8 101.0
REMARK 620 6 HOH A1004 O 79.2 69.2 89.5 74.5 159.3
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 904
DBREF 5N6A A 1 828 UNP Q9BE39 MYH7_BOVIN 1 828
SEQRES 1 A 828 MET VAL ASP ALA GLU MET ALA ALA PHE GLY GLU ALA ALA
SEQRES 2 A 828 PRO TYR LEU ARG LYS SER GLU LYS GLU ARG LEU GLU ALA
SEQRES 3 A 828 GLN THR ARG PRO PHE ASP LEU LYS LYS ASP VAL PHE VAL
SEQRES 4 A 828 PRO ASP ASP LYS GLU GLU PHE VAL LYS ALA THR ILE LEU
SEQRES 5 A 828 SER ARG GLU GLY GLY LYS VAL THR ALA GLU THR GLU HIS
SEQRES 6 A 828 GLY LYS THR VAL THR VAL LYS GLU ASP GLN VAL LEU GLN
SEQRES 7 A 828 GLN ASN PRO PRO LYS PHE ASP LYS ILE GLU ASP MET ALA
SEQRES 8 A 828 MET LEU THR PHE LEU HIS GLU PRO ALA VAL LEU TYR ASN
SEQRES 9 A 828 LEU LYS GLU ARG TYR ALA SER TRP MET ILE TYR THR TYR
SEQRES 10 A 828 SER GLY LEU PHE CYS VAL THR ILE ASN PRO TYR LYS TRP
SEQRES 11 A 828 LEU PRO VAL TYR ASN ALA GLU VAL VAL ALA ALA TYR ARG
SEQRES 12 A 828 GLY LYS LYS ARG SER GLU ALA PRO PRO HIS ILE PHE SER
SEQRES 13 A 828 ILE SER ASP ASN ALA TYR GLN TYR MET LEU THR ASP ARG
SEQRES 14 A 828 GLU ASN GLN SER ILE LEU ILE THR GLY GLU SER GLY ALA
SEQRES 15 A 828 GLY LYS THR VAL ASN THR LYS ARG VAL ILE GLN TYR PHE
SEQRES 16 A 828 ALA VAL ILE ALA ALA ILE GLY ASP ARG SER LYS LYS GLU
SEQRES 17 A 828 GLN ALA THR GLY LYS GLY THR LEU GLU ASP GLN ILE ILE
SEQRES 18 A 828 GLN ALA ASN PRO ALA LEU GLU ALA PHE GLY ASN ALA LYS
SEQRES 19 A 828 THR VAL ARG ASN ASP ASN SER SER ARG PHE GLY LYS PHE
SEQRES 20 A 828 ILE ARG ILE HIS PHE GLY ALA THR GLY LYS LEU ALA SER
SEQRES 21 A 828 ALA ASP ILE GLU THR TYR LEU LEU GLU LYS SER ARG VAL
SEQRES 22 A 828 ILE PHE GLN LEU LYS ALA GLU ARG ASP TYR HIS ILE PHE
SEQRES 23 A 828 TYR GLN ILE LEU SER ASN LYS LYS PRO GLU LEU LEU ASP
SEQRES 24 A 828 MET LEU LEU ILE THR ASN ASN PRO TYR ASP TYR ALA PHE
SEQRES 25 A 828 ILE SER GLN GLY GLU THR THR VAL ALA SER ILE ASP ASP
SEQRES 26 A 828 ALA GLU GLU LEU MET ALA THR ASP ASN ALA PHE ASP VAL
SEQRES 27 A 828 LEU GLY PHE THR THR GLU GLU LYS ASN SER MET TYR LYS
SEQRES 28 A 828 LEU THR GLY ALA ILE MET HIS PHE GLY ASN MET LYS PHE
SEQRES 29 A 828 LYS LEU LYS GLN ARG GLU GLU GLN ALA GLU PRO ASP GLY
SEQRES 30 A 828 THR GLU GLU ALA ASP LYS SER ALA TYR LEU MET GLY LEU
SEQRES 31 A 828 ASN SER ALA ASP LEU LEU LYS GLY LEU CYS HIS PRO ARG
SEQRES 32 A 828 VAL LYS VAL GLY ASN GLU TYR VAL THR LYS GLY GLN ASN
SEQRES 33 A 828 VAL GLN GLN VAL VAL TYR ALA LYS GLY ALA LEU ALA LYS
SEQRES 34 A 828 ALA VAL TYR GLU ARG MET PHE ASN TRP MET VAL THR ARG
SEQRES 35 A 828 ILE ASN ALA THR LEU GLU THR LYS GLN PRO ARG GLN TYR
SEQRES 36 A 828 PHE ILE GLY VAL LEU ASP ILE ALA GLY PHE GLU ILE PHE
SEQRES 37 A 828 ASP PHE ASN SER PHE GLU GLN LEU CYS ILE ASN PHE THR
SEQRES 38 A 828 ASN GLU LYS LEU GLN GLN PHE PHE ASN HIS HIS MET PHE
SEQRES 39 A 828 VAL LEU GLU GLN GLU GLU TYR LYS LYS GLU GLY ILE GLU
SEQRES 40 A 828 TRP GLU PHE ILE ASP PHE GLY MET ASP LEU GLN ALA CYS
SEQRES 41 A 828 ILE ASP LEU ILE GLU LYS PRO MET GLY ILE MET SER ILE
SEQRES 42 A 828 LEU GLU GLU GLU CYS MET PHE PRO LYS ALA THR ASP MET
SEQRES 43 A 828 THR PHE LYS ALA LYS LEU PHE ASP ASN HIS LEU GLY LYS
SEQRES 44 A 828 SER SER ASN PHE GLN LYS PRO ARG ASN ILE LYS GLY LYS
SEQRES 45 A 828 PRO GLU ALA HIS PHE SER LEU ILE HIS TYR ALA GLY THR
SEQRES 46 A 828 VAL ASP TYR ASN ILE ILE GLY TRP LEU GLN LYS ASN LYS
SEQRES 47 A 828 ASP PRO LEU ASN GLU THR VAL VAL ASP LEU TYR LYS LYS
SEQRES 48 A 828 SER SER LEU LYS MET LEU SER SER LEU PHE ALA ASN TYR
SEQRES 49 A 828 ALA GLY PHE ASP THR PRO ILE GLU LYS GLY LYS GLY LYS
SEQRES 50 A 828 ALA LYS LYS GLY SER SER PHE GLN THR VAL SER ALA LEU
SEQRES 51 A 828 HIS ARG GLU ASN LEU ASN LYS LEU MET THR ASN LEU ARG
SEQRES 52 A 828 SER THR HIS PRO HIS PHE VAL ARG CYS ILE ILE PRO ASN
SEQRES 53 A 828 GLU THR LYS SER PRO GLY VAL ILE ASP ASN PRO LEU VAL
SEQRES 54 A 828 MET HIS GLN LEU ARG CYS ASN GLY VAL LEU GLU GLY ILE
SEQRES 55 A 828 ARG ILE CYS ARG LYS GLY PHE PRO ASN ARG ILE LEU TYR
SEQRES 56 A 828 GLY ASP PHE ARG GLN ARG TYR ARG ILE LEU ASN PRO ALA
SEQRES 57 A 828 ALA ILE PRO GLU GLY GLN PHE ILE ASP SER ARG LYS GLY
SEQRES 58 A 828 ALA GLU LYS LEU LEU GLY SER LEU ASP ILE ASP HIS ASN
SEQRES 59 A 828 GLN TYR LYS PHE GLY HIS THR LYS VAL PHE PHE LYS ALA
SEQRES 60 A 828 GLY LEU LEU GLY LEU LEU GLU GLU MET ARG ASP GLU ARG
SEQRES 61 A 828 LEU SER ARG ILE ILE THR ARG ILE GLN ALA GLN SER ARG
SEQRES 62 A 828 GLY VAL LEU SER ARG MET GLU PHE LYS LYS LEU LEU GLU
SEQRES 63 A 828 ARG ARG ASP SER LEU LEU ILE ILE GLN TRP ASN ILE ARG
SEQRES 64 A 828 ALA PHE MET GLY VAL LYS ASN TRP PRO
HET ADP A 901 27
HET PO4 A 902 5
HET MG A 903 1
HET GOL A 904 6
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM PO4 PHOSPHATE ION
HETNAM MG MAGNESIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 ADP C10 H15 N5 O10 P2
FORMUL 3 PO4 O4 P 3-
FORMUL 4 MG MG 2+
FORMUL 5 GOL C3 H8 O3
FORMUL 6 HOH *36(H2 O)
HELIX 1 AA1 ASP A 89 LEU A 93 5 5
HELIX 2 AA2 HIS A 97 ALA A 110 1 14
HELIX 3 AA3 ASN A 135 ARG A 143 1 9
HELIX 4 AA4 HIS A 153 ASP A 168 1 16
HELIX 5 AA5 GLY A 183 VAL A 197 1 15
HELIX 6 AA6 ASP A 218 ASN A 224 1 7
HELIX 7 AA7 PRO A 225 LEU A 227 5 3
HELIX 8 AA8 GLU A 269 VAL A 273 5 5
HELIX 9 AA9 TYR A 283 ASN A 292 1 10
HELIX 10 AB1 ASP A 324 LEU A 339 1 16
HELIX 11 AB2 THR A 342 GLY A 360 1 19
HELIX 12 AB3 ASP A 382 LEU A 387 1 6
HELIX 13 AB4 SER A 392 HIS A 401 1 10
HELIX 14 AB5 ASN A 416 GLU A 448 1 33
HELIX 15 AB6 SER A 472 PHE A 494 1 23
HELIX 16 AB7 VAL A 495 GLY A 505 1 11
HELIX 17 AB8 LEU A 517 GLU A 525 1 9
HELIX 18 AB9 GLY A 529 PHE A 540 1 12
HELIX 19 AC1 THR A 544 LEU A 557 1 14
HELIX 20 AC2 TRP A 593 LYS A 598 1 6
HELIX 21 AC3 ASN A 602 LYS A 611 1 10
HELIX 22 AC4 LEU A 614 ASN A 623 1 10
HELIX 23 AC5 THR A 646 ARG A 663 1 18
HELIX 24 AC6 ASP A 685 MET A 690 1 6
HELIX 25 AC7 HIS A 691 GLY A 697 1 7
HELIX 26 AC8 LYS A 766 GLU A 775 1 10
SHEET 1 AA1 4 LYS A 58 THR A 60 0
SHEET 2 AA1 4 PHE A 46 ARG A 54 -1 N LEU A 52 O VAL A 59
SHEET 3 AA1 4 ASP A 36 PRO A 40 -1 N VAL A 39 O VAL A 47
SHEET 4 AA1 4 GLN A 78 GLN A 79 -1 O GLN A 79 N ASP A 36
SHEET 1 AA2 7 TYR A 115 TYR A 117 0
SHEET 2 AA2 7 CYS A 122 ILE A 125 -1 O VAL A 123 N THR A 116
SHEET 3 AA2 7 HIS A 666 ILE A 673 1 O ARG A 671 N THR A 124
SHEET 4 AA2 7 GLN A 172 GLY A 178 1 N LEU A 175 O HIS A 668
SHEET 5 AA2 7 PHE A 456 ASP A 461 1 O GLY A 458 N ILE A 174
SHEET 6 AA2 7 LYS A 246 PHE A 252 -1 N ILE A 250 O ILE A 457
SHEET 7 AA2 7 LEU A 258 THR A 265 -1 O ASP A 262 N ARG A 249
SHEET 1 AA3 2 ASN A 232 ALA A 233 0
SHEET 2 AA3 2 SER A 241 SER A 242 -1 O SER A 241 N ALA A 233
SHEET 1 AA4 2 LYS A 365 GLN A 368 0
SHEET 2 AA4 2 GLN A 372 GLU A 374 -1 O GLN A 372 N LYS A 367
SHEET 1 AA5 2 ARG A 403 VAL A 406 0
SHEET 2 AA5 2 GLU A 409 THR A 412 -1 O VAL A 411 N VAL A 404
SHEET 1 AA6 3 PHE A 563 GLN A 564 0
SHEET 2 AA6 3 PHE A 577 LEU A 579 -1 O SER A 578 N GLN A 564
SHEET 3 AA6 3 VAL A 586 TYR A 588 -1 O TYR A 588 N PHE A 577
SHEET 1 AA7 3 ASN A 711 ARG A 712 0
SHEET 2 AA7 3 PHE A 764 PHE A 765 -1 O PHE A 765 N ASN A 711
SHEET 3 AA7 3 TYR A 756 LYS A 757 -1 N LYS A 757 O PHE A 764
LINK OG1 THR A 185 MG MG A 903 1555 1555 1.97
LINK OG SER A 242 MG MG A 903 1555 1555 2.29
LINK O3B ADP A 901 MG MG A 903 1555 1555 2.14
LINK O4 PO4 A 902 MG MG A 903 1555 1555 2.04
LINK MG MG A 903 O HOH A1003 1555 1555 2.79
LINK MG MG A 903 O HOH A1004 1555 1555 2.42
CISPEP 1 GLU A 509 PHE A 510 0 1.77
CISPEP 2 PRO A 527 MET A 528 0 1.50
CISPEP 3 LYS A 762 VAL A 763 0 -0.38
SITE 1 AC1 19 ILE A 114 ASN A 126 PRO A 127 TYR A 128
SITE 2 AC1 19 LYS A 129 TRP A 130 TYR A 134 GLU A 179
SITE 3 AC1 19 GLY A 181 ALA A 182 GLY A 183 LYS A 184
SITE 4 AC1 19 THR A 185 VAL A 186 ASN A 238 PO4 A 902
SITE 5 AC1 19 MG A 903 HOH A1004 HOH A1010
SITE 1 AC2 11 SER A 180 GLY A 181 LYS A 184 ASN A 238
SITE 2 AC2 11 SER A 241 SER A 242 ARG A 243 GLY A 464
SITE 3 AC2 11 ADP A 901 MG A 903 HOH A1004
SITE 1 AC3 7 THR A 185 SER A 242 ASP A 461 ADP A 901
SITE 2 AC3 7 PO4 A 902 HOH A1003 HOH A1004
SITE 1 AC4 5 GLU A 574 ALA A 575 HIS A 576 ASN A 589
SITE 2 AC4 5 ILE A 590
CRYST1 87.660 149.830 154.260 90.00 90.00 90.00 C 2 2 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.011408 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006674 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006483 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
