HEADER CA-BINDING PROTEIN/MOTOR PROTEIN 31-JUL-11 3ZWH
TITLE CA2+-BOUND S100A4 C3S, C81S, C86S AND F45W MUTANT COMPLEXED WITH
TITLE 2 MYOSIN IIA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN S100-A4;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CALVASCULIN, METASTASIN, PLACENTAL CALCIUM-BINDING PROTEIN,
COMPND 5 PROTEIN MTS1, S100 CALCIUM-BINDING PROTEIN A4, S100A4;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: MYOSIN-9;
COMPND 10 CHAIN: Q;
COMPND 11 FRAGMENT: RESIDUES 1893-1937;
COMPND 12 SYNONYM: CELLULAR MYOSIN HEAVY CHAIN\,TYPE A, MYOSIN HEAVY CHAIN 9,
COMPND 13 MYOSIN HEAVY CHAIN\,NON-MUSCLE IIA, NON-MUSCLE MYOSIN HEAVY CHAIN A,
COMPND 14 NMMHC-A, NON-MUSCLE MYOSIN HEAVY CHAIN IIA, NMMHC II-A, NMMHC-IIA;
COMPND 15 ENGINEERED: YES;
COMPND 16 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 CELL_LINE: HEK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PBH4;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 CELL_LINE: HEK;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PBH4
KEYWDS CA-BINDING PROTEIN-MOTOR PROTEIN COMPLEX, S100 PROTEINS, EF-HAND
EXPDTA X-RAY DIFFRACTION
AUTHOR B.KISS,A.DUELLI,L.RADNAI,A.K.KEKESI,G.KATONA,L.NYITRAY
REVDAT 4 20-DEC-23 3ZWH 1 REMARK LINK
REVDAT 3 27-NOV-13 3ZWH 1 COMPND DBREF
REVDAT 2 23-MAY-12 3ZWH 1 AUTHOR JRNL
REVDAT 1 04-APR-12 3ZWH 0
JRNL AUTH B.KISS,A.DUELLI,L.RADNAI,K.A.KEKESI,G.KATONA,L.NYITRAY
JRNL TITL CRYSTAL STRUCTURE OF THE S100A4-NONMUSCLE MYOSIN IIA TAIL
JRNL TITL 2 FRAGMENT COMPLEX REVEALS AN ASYMMETRIC TARGET BINDING
JRNL TITL 3 MECHANISM.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 109 6048 2012
JRNL REFN ISSN 0027-8424
JRNL PMID 22460785
JRNL DOI 10.1073/PNAS.1114732109
REMARK 2
REMARK 2 RESOLUTION. 1.94 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.94
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.94
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 22109
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.175
REMARK 3 FREE R VALUE : 0.206
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1129
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 19.9374 - 3.8718 1.00 2849 120 0.1647 0.1812
REMARK 3 2 3.8718 - 3.0768 1.00 2660 145 0.1649 0.1681
REMARK 3 3 3.0768 - 2.6890 1.00 2627 131 0.1819 0.2421
REMARK 3 4 2.6890 - 2.4436 1.00 2591 151 0.1805 0.2185
REMARK 3 5 2.4436 - 2.2687 1.00 2584 146 0.1723 0.2313
REMARK 3 6 2.2687 - 2.1351 1.00 2541 166 0.1749 0.2147
REMARK 3 7 2.1351 - 2.0283 1.00 2567 144 0.1895 0.2244
REMARK 3 8 2.0283 - 1.9401 1.00 2561 126 0.2236 0.2581
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.10
REMARK 3 SHRINKAGE RADIUS : 0.83
REMARK 3 K_SOL : 0.34
REMARK 3 B_SOL : 34.33
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.550
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.12
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 24.04
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.14300
REMARK 3 B22 (A**2) : 0.14300
REMARK 3 B33 (A**2) : -0.28610
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 1966
REMARK 3 ANGLE : 0.671 2615
REMARK 3 CHIRALITY : 0.051 275
REMARK 3 PLANARITY : 0.003 342
REMARK 3 DIHEDRAL : 12.497 758
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 7
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 2:94)
REMARK 3 ORIGIN FOR THE GROUP (A): 19.4054 2.3887 11.5390
REMARK 3 T TENSOR
REMARK 3 T11: 0.0661 T22: 0.0805
REMARK 3 T33: 0.0709 T12: 0.0099
REMARK 3 T13: 0.0007 T23: 0.0243
REMARK 3 L TENSOR
REMARK 3 L11: 0.2816 L22: 1.0058
REMARK 3 L33: 0.6905 L12: 0.4689
REMARK 3 L13: 0.1058 L23: -0.2316
REMARK 3 S TENSOR
REMARK 3 S11: -0.0219 S12: -0.0677 S13: 0.0045
REMARK 3 S21: -0.0787 S22: 0.0374 S23: 0.0683
REMARK 3 S31: 0.0518 S32: -0.0162 S33: 0.0077
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN B AND RESID 1:74)
REMARK 3 ORIGIN FOR THE GROUP (A): 39.5072 10.3890 15.3482
REMARK 3 T TENSOR
REMARK 3 T11: 0.0567 T22: 0.2408
REMARK 3 T33: 0.1546 T12: -0.0269
REMARK 3 T13: -0.0306 T23: 0.0182
REMARK 3 L TENSOR
REMARK 3 L11: 0.5451 L22: 0.4651
REMARK 3 L33: 0.9598 L12: -0.2854
REMARK 3 L13: 0.0081 L23: -0.3475
REMARK 3 S TENSOR
REMARK 3 S11: -0.0472 S12: -0.2828 S13: -0.0148
REMARK 3 S21: -0.0015 S22: -0.1169 S23: -0.2986
REMARK 3 S31: -0.0307 S32: 0.3666 S33: -0.0404
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN B AND RESID 75:99)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.8313 7.5467 -0.2418
REMARK 3 T TENSOR
REMARK 3 T11: 0.1114 T22: 0.0879
REMARK 3 T33: 0.1021 T12: -0.0243
REMARK 3 T13: 0.0304 T23: -0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 0.2502 L22: 0.1478
REMARK 3 L33: 0.2369 L12: -0.0365
REMARK 3 L13: -0.2904 L23: -0.0509
REMARK 3 S TENSOR
REMARK 3 S11: -0.0309 S12: -0.0115 S13: -0.1725
REMARK 3 S21: -0.0849 S22: 0.0544 S23: -0.1001
REMARK 3 S31: 0.2265 S32: 0.0504 S33: -0.0061
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN Q AND RESID 1893:1902)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.0230 -2.1429 24.5280
REMARK 3 T TENSOR
REMARK 3 T11: 0.1194 T22: 0.1278
REMARK 3 T33: 0.1394 T12: 0.0090
REMARK 3 T13: 0.0064 T23: 0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 0.0396 L22: 0.0421
REMARK 3 L33: 0.0469 L12: 0.0356
REMARK 3 L13: -0.0530 L23: 0.0019
REMARK 3 S TENSOR
REMARK 3 S11: 0.0772 S12: -0.0201 S13: -0.1194
REMARK 3 S21: -0.0393 S22: -0.0549 S23: 0.5315
REMARK 3 S31: 0.0083 S32: -0.2808 S33: 0.0000
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: (CHAIN Q AND RESID 1903:1908)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.8175 11.7347 20.0613
REMARK 3 T TENSOR
REMARK 3 T11: 0.3143 T22: 0.1747
REMARK 3 T33: 0.1035 T12: 0.0389
REMARK 3 T13: 0.0100 T23: -0.0037
REMARK 3 L TENSOR
REMARK 3 L11: 0.0577 L22: 0.1475
REMARK 3 L33: -0.0020 L12: 0.0934
REMARK 3 L13: -0.0089 L23: -0.0212
REMARK 3 S TENSOR
REMARK 3 S11: -0.1159 S12: -0.2805 S13: 0.0656
REMARK 3 S21: 0.3524 S22: 0.0489 S23: 0.4245
REMARK 3 S31: -0.0017 S32: 0.0406 S33: -0.0012
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: (CHAIN Q AND RESID 1909:1930)
REMARK 3 ORIGIN FOR THE GROUP (A): 30.4985 20.2180 7.7556
REMARK 3 T TENSOR
REMARK 3 T11: 0.1132 T22: 0.1309
REMARK 3 T33: 0.1304 T12: -0.0271
REMARK 3 T13: 0.0030 T23: 0.0011
REMARK 3 L TENSOR
REMARK 3 L11: 0.1031 L22: -0.0018
REMARK 3 L33: 0.0374 L12: 0.0400
REMARK 3 L13: 0.0085 L23: -0.0143
REMARK 3 S TENSOR
REMARK 3 S11: 0.0835 S12: 0.0822 S13: 0.2437
REMARK 3 S21: 0.0917 S22: 0.0312 S23: -0.0738
REMARK 3 S31: -0.2732 S32: 0.0494 S33: 0.0001
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: (CHAIN Q AND RESID 1931:1935)
REMARK 3 ORIGIN FOR THE GROUP (A): 36.1526 12.4065 -3.3390
REMARK 3 T TENSOR
REMARK 3 T11: 0.2282 T22: 0.1329
REMARK 3 T33: 0.1532 T12: -0.0314
REMARK 3 T13: 0.0298 T23: 0.0541
REMARK 3 L TENSOR
REMARK 3 L11: 0.2175 L22: 0.2136
REMARK 3 L33: 0.3346 L12: 0.0818
REMARK 3 L13: 0.2118 L23: 0.2235
REMARK 3 S TENSOR
REMARK 3 S11: -0.1337 S12: 0.0523 S13: 0.0307
REMARK 3 S21: -0.1821 S22: -0.3508 S23: -0.1961
REMARK 3 S31: -0.1848 S32: 0.1865 S33: -0.0316
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: CHAIN A RES MET-1 AND RES ASP95-
REMARK 3 -LYS101, CHAIN B RES LYS100-LYS101 AND CHAIN Q ARG1936- -LYS1937,
REMARK 3 COULD NOT BE MODELLED DUE TO MISSING ELECTRON DENSITY
REMARK 4
REMARK 4 3ZWH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-JUL-11.
REMARK 100 THE DEPOSITION ID IS D_1290048871.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-JUN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.873
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : KB MIRROR
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22196
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 19.400
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 14.30
REMARK 200 R MERGE (I) : 0.16000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.4400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 14.60
REMARK 200 R MERGE FOR SHELL (I) : 0.95000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.540
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRY 3C1V
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.13
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000, 0.2 M NA-ACETATE PH 5.6,
REMARK 280 0.1 M NA-CITRATE.
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.49200
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 31.98600
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 31.98600
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 34.74600
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 31.98600
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 31.98600
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 104.23800
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 31.98600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 31.98600
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 34.74600
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 31.98600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 31.98600
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 104.23800
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 69.49200
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11960 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -112.1 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, Q
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 A2044 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A2046 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 3 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, PHE 45 TO TRP
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 81 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, CYS 86 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, CYS 3 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, PHE 45 TO TRP
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, CYS 81 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, CYS 86 TO SER
REMARK 400 ENGINEERED RESIDUE IN CHAIN Q, ARG 1893 TO TYR
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 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ASP A 95
REMARK 465 LYS A 96
REMARK 465 GLN A 97
REMARK 465 PRO A 98
REMARK 465 ARG A 99
REMARK 465 LYS A 100
REMARK 465 LYS A 101
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 LYS B 100
REMARK 465 LYS B 101
REMARK 465 ARG Q 1936
REMARK 465 LYS Q 1937
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ARG B 66 CZ NH1 NH2
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 51 88.43 -161.35
REMARK 500 ASP B 25 109.34 -57.58
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 CA A 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER A 20 O
REMARK 620 2 GLU A 23 O 94.6
REMARK 620 3 ASP A 25 O 75.8 84.8
REMARK 620 4 LYS A 28 O 87.7 170.1 86.5
REMARK 620 5 GLU A 33 OE1 99.7 107.9 167.0 81.1
REMARK 620 6 GLU A 33 OE2 77.2 69.8 140.9 120.1 46.6
REMARK 620 7 HOH A2038 O 168.0 89.8 93.5 86.2 89.5 114.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 63 OD1
REMARK 620 2 ASN A 65 OD1 85.6
REMARK 620 3 ASP A 67 OD1 83.3 78.5
REMARK 620 4 GLU A 69 O 82.5 157.3 81.0
REMARK 620 5 GLU A 74 OE1 117.4 121.6 150.3 81.1
REMARK 620 6 GLU A 74 OE2 95.8 77.1 155.5 123.2 49.6
REMARK 620 7 HOH A2087 O 161.0 84.5 78.9 100.9 81.5 97.8
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 SER B 20 O
REMARK 620 2 GLU B 23 O 92.8
REMARK 620 3 ASP B 25 O 85.0 83.3
REMARK 620 4 LYS B 28 O 92.0 159.3 77.1
REMARK 620 5 GLU B 33 OE1 97.6 123.2 153.0 76.0
REMARK 620 6 GLU B 33 OE2 78.3 78.0 154.1 122.7 50.5
REMARK 620 7 HOH B2022 O 168.4 89.7 84.1 81.8 90.5 113.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 63 OD1
REMARK 620 2 ASN B 65 OD1 79.6
REMARK 620 3 ASP B 67 OD1 83.7 84.1
REMARK 620 4 GLU B 69 O 84.1 155.7 76.3
REMARK 620 5 GLU B 74 OE1 117.2 122.2 147.5 81.3
REMARK 620 6 GLU B 74 OE2 89.6 79.1 162.8 118.8 48.9
REMARK 620 7 HOH B2028 O 160.2 89.9 78.5 100.0 82.6 104.9
REMARK 620 N 1 2 3 4 5 6
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR PROVIDED.
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1095
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 1096
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI B 1100
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AZI Q 2936
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1M31 RELATED DB: PDB
REMARK 900 THREE-DIMENSIONAL SOLUTION STRUCTURE OF APO-MTS1
DBREF 3ZWH A 1 101 UNP P26447 S10A4_HUMAN 1 101
DBREF 3ZWH B 1 101 UNP P26447 S10A4_HUMAN 1 101
DBREF 3ZWH Q 1893 1937 UNP P35579 MYH9_HUMAN 1893 1937
SEQADV 3ZWH GLY A -2 UNP P26447 EXPRESSION TAG
SEQADV 3ZWH SER A -1 UNP P26447 EXPRESSION TAG
SEQADV 3ZWH HIS A 0 UNP P26447 EXPRESSION TAG
SEQADV 3ZWH SER A 3 UNP P26447 CYS 3 ENGINEERED MUTATION
SEQADV 3ZWH TRP A 45 UNP P26447 PHE 45 ENGINEERED MUTATION
SEQADV 3ZWH SER A 81 UNP P26447 CYS 81 ENGINEERED MUTATION
SEQADV 3ZWH SER A 86 UNP P26447 CYS 86 ENGINEERED MUTATION
SEQADV 3ZWH GLY B -2 UNP P26447 EXPRESSION TAG
SEQADV 3ZWH SER B -1 UNP P26447 EXPRESSION TAG
SEQADV 3ZWH HIS B 0 UNP P26447 EXPRESSION TAG
SEQADV 3ZWH SER B 3 UNP P26447 CYS 3 ENGINEERED MUTATION
SEQADV 3ZWH TRP B 45 UNP P26447 PHE 45 ENGINEERED MUTATION
SEQADV 3ZWH SER B 81 UNP P26447 CYS 81 ENGINEERED MUTATION
SEQADV 3ZWH SER B 86 UNP P26447 CYS 86 ENGINEERED MUTATION
SEQADV 3ZWH TYR Q 1893 UNP P35579 ARG 1893 ENGINEERED MUTATION
SEQRES 1 A 104 GLY SER HIS MET ALA SER PRO LEU GLU LYS ALA LEU ASP
SEQRES 2 A 104 VAL MET VAL SER THR PHE HIS LYS TYR SER GLY LYS GLU
SEQRES 3 A 104 GLY ASP LYS PHE LYS LEU ASN LYS SER GLU LEU LYS GLU
SEQRES 4 A 104 LEU LEU THR ARG GLU LEU PRO SER TRP LEU GLY LYS ARG
SEQRES 5 A 104 THR ASP GLU ALA ALA PHE GLN LYS LEU MET SER ASN LEU
SEQRES 6 A 104 ASP SER ASN ARG ASP ASN GLU VAL ASP PHE GLN GLU TYR
SEQRES 7 A 104 CYS VAL PHE LEU SER SER ILE ALA MET MET SER ASN GLU
SEQRES 8 A 104 PHE PHE GLU GLY PHE PRO ASP LYS GLN PRO ARG LYS LYS
SEQRES 1 B 104 GLY SER HIS MET ALA SER PRO LEU GLU LYS ALA LEU ASP
SEQRES 2 B 104 VAL MET VAL SER THR PHE HIS LYS TYR SER GLY LYS GLU
SEQRES 3 B 104 GLY ASP LYS PHE LYS LEU ASN LYS SER GLU LEU LYS GLU
SEQRES 4 B 104 LEU LEU THR ARG GLU LEU PRO SER TRP LEU GLY LYS ARG
SEQRES 5 B 104 THR ASP GLU ALA ALA PHE GLN LYS LEU MET SER ASN LEU
SEQRES 6 B 104 ASP SER ASN ARG ASP ASN GLU VAL ASP PHE GLN GLU TYR
SEQRES 7 B 104 CYS VAL PHE LEU SER SER ILE ALA MET MET SER ASN GLU
SEQRES 8 B 104 PHE PHE GLU GLY PHE PRO ASP LYS GLN PRO ARG LYS LYS
SEQRES 1 Q 45 TYR ARG LYS LEU GLN ARG GLU LEU GLU ASP ALA THR GLU
SEQRES 2 Q 45 THR ALA ASP ALA MET ASN ARG GLU VAL SER SER LEU LYS
SEQRES 3 Q 45 ASN LYS LEU ARG ARG GLY ASP LEU PRO PHE VAL VAL PRO
SEQRES 4 Q 45 ARG ARG MET ALA ARG LYS
HET CA A 501 1
HET CA A 502 1
HET ACT A1095 4
HET ACT A1096 4
HET CA B 501 1
HET CA B 502 1
HET AZI B1100 3
HET AZI Q2936 3
HETNAM CA CALCIUM ION
HETNAM ACT ACETATE ION
HETNAM AZI AZIDE ION
FORMUL 4 CA 4(CA 2+)
FORMUL 6 ACT 2(C2 H3 O2 1-)
FORMUL 10 AZI 2(N3 1-)
FORMUL 12 HOH *201(H2 O)
HELIX 1 1 SER A 3 GLY A 21 1 19
HELIX 2 2 ASN A 30 LEU A 42 1 13
HELIX 3 3 PRO A 43 LEU A 46 5 4
HELIX 4 4 ASP A 51 ASP A 63 1 13
HELIX 5 5 ASP A 71 PHE A 93 1 23
HELIX 6 6 SER B 3 GLY B 21 1 19
HELIX 7 7 ASN B 30 LEU B 42 1 13
HELIX 8 8 PRO B 43 TRP B 45 5 3
HELIX 9 9 ASP B 51 ASP B 63 1 13
HELIX 10 10 ASP B 71 GLY B 92 1 22
HELIX 11 11 ARG Q 1898 THR Q 1904 1 7
HELIX 12 12 ALA Q 1907 ARG Q 1923 1 17
LINK O SER A 20 CA CA A 501 1555 1555 2.49
LINK O GLU A 23 CA CA A 501 1555 1555 2.50
LINK O ASP A 25 CA CA A 501 1555 1555 2.49
LINK O LYS A 28 CA CA A 501 1555 1555 2.46
LINK OE1 GLU A 33 CA CA A 501 1555 1555 2.54
LINK OE2 GLU A 33 CA CA A 501 1555 1555 2.93
LINK OD1 ASP A 63 CA CA A 502 1555 1555 2.48
LINK OD1 ASN A 65 CA CA A 502 1555 1555 2.46
LINK OD1 ASP A 67 CA CA A 502 1555 1555 2.54
LINK O GLU A 69 CA CA A 502 1555 1555 2.47
LINK OE1 GLU A 74 CA CA A 502 1555 1555 2.56
LINK OE2 GLU A 74 CA CA A 502 1555 1555 2.68
LINK CA CA A 501 O HOH A2038 1555 1555 2.67
LINK CA CA A 502 O HOH A2087 1555 1555 2.61
LINK O SER B 20 CA CA B 501 1555 1555 2.40
LINK O GLU B 23 CA CA B 501 1555 1555 2.53
LINK O ASP B 25 CA CA B 501 1555 1555 2.49
LINK O LYS B 28 CA CA B 501 1555 1555 2.44
LINK OE1 GLU B 33 CA CA B 501 1555 1555 2.44
LINK OE2 GLU B 33 CA CA B 501 1555 1555 2.68
LINK OD1 ASP B 63 CA CA B 502 1555 1555 2.65
LINK OD1 ASN B 65 CA CA B 502 1555 1555 2.50
LINK OD1 ASP B 67 CA CA B 502 1555 1555 2.69
LINK O GLU B 69 CA CA B 502 1555 1555 2.48
LINK OE1 GLU B 74 CA CA B 502 1555 1555 2.58
LINK OE2 GLU B 74 CA CA B 502 1555 1555 2.72
LINK CA CA B 501 O HOH B2022 1555 1555 2.36
LINK CA CA B 502 O HOH B2028 1555 1555 2.77
SITE 1 AC1 6 SER A 20 GLU A 23 ASP A 25 LYS A 28
SITE 2 AC1 6 GLU A 33 HOH A2038
SITE 1 AC2 6 ASP A 63 ASN A 65 ASP A 67 GLU A 69
SITE 2 AC2 6 GLU A 74 HOH A2087
SITE 1 AC3 6 SER B 20 GLU B 23 ASP B 25 LYS B 28
SITE 2 AC3 6 GLU B 33 HOH B2022
SITE 1 AC4 6 ASP B 63 ASN B 65 ASP B 67 GLU B 69
SITE 2 AC4 6 GLU B 74 HOH B2028
SITE 1 AC5 6 LEU A 46 ACT A1096 HOH A2058 HOH A2072
SITE 2 AC5 6 HOH A2073 ARG Q1912
SITE 1 AC6 4 LEU A 46 GLY A 47 ACT A1095 HOH A2100
SITE 1 AC7 4 PRO B 4 HOH B2002 HOH B2012 HOH B2069
SITE 1 AC8 7 LYS Q1920 LEU Q1921 GLY Q1924 ASP Q1925
SITE 2 AC8 7 LEU Q1926 VAL Q1929 PRO Q1931
CRYST1 63.972 63.972 138.984 90.00 90.00 90.00 P 41 21 2 16
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 0.015632 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015632 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007195 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
