HEADER CONTRACTILE PROTEIN/ACTIN-BINDING PROTEI14-MAY-14 4PKG
TITLE COMPLEX OF ATP-ACTIN WITH THE N-TERMINAL ACTIN-BINDING DOMAIN OF
TITLE 2 TROPOMODULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACTIN, ALPHA SKELETAL MUSCLE;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: ALPHA-ACTIN-1;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: GELSOLIN,TROPOMODULIN-1 CHIMERA;
COMPND 7 CHAIN: G;
COMPND 8 FRAGMENT: GELSOLIN (UNP RESIDUES 12-136), GGSGGSGGS LINKER, TMOD1
COMPND 9 ACTIN-BINDING SITE 1 (UNP RESIDUES 50-101);
COMPND 10 SYNONYM: AGEL,ACTIN-DEPOLYMERIZING FACTOR,ADF,BREVIN,ERYTHROCYTE
COMPND 11 TROPOMODULIN,E-TMOD;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 3 ORGANISM_COMMON: RABBIT;
SOURCE 4 ORGANISM_TAXID: 9986;
SOURCE 5 TISSUE: SKELETAL MUSCLE;
SOURCE 6 MOL_ID: 2;
SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 8 ORGANISM_COMMON: HUMAN;
SOURCE 9 ORGANISM_TAXID: 9606;
SOURCE 10 GENE: GSN, TMOD1, D9S57E, TMOD;
SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 12 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 13 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 14 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 15 EXPRESSION_SYSTEM_PLASMID: PTYB11
KEYWDS TMOD, ACTIN FILAMENT, POINTED-END CAPPING PROTEIN, TROPOMYOSIN,
KEYWDS 2 CONTRACTILE PROTEIN, ACTIN-BINDING PROTEIN, CONTRACTILE PROTEIN-
KEYWDS 3 ACTIN-BINDING PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.N.RAO,R.DOMINGUEZ
REVDAT 5 27-SEP-23 4PKG 1 REMARK LINK
REVDAT 4 25-DEC-19 4PKG 1 REMARK
REVDAT 3 06-SEP-17 4PKG 1 SOURCE JRNL REMARK
REVDAT 2 06-AUG-14 4PKG 1 JRNL
REVDAT 1 30-JUL-14 4PKG 0
JRNL AUTH J.N.RAO,Y.MADASU,R.DOMINGUEZ
JRNL TITL ACTIN CYTOSKELETON. MECHANISM OF ACTIN FILAMENT POINTED-END
JRNL TITL 2 CAPPING BY TROPOMODULIN.
JRNL REF SCIENCE V. 345 463 2014
JRNL REFN ESSN 1095-9203
JRNL PMID 25061212
JRNL DOI 10.1126/SCIENCE.1256159
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 67450
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.156
REMARK 3 FREE R VALUE : 0.187
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.970
REMARK 3 FREE R VALUE TEST SET COUNT : 2000
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 37.9414 - 4.3352 0.99 4925 151 0.1349 0.1479
REMARK 3 2 4.3352 - 3.4417 1.00 4770 145 0.1337 0.1574
REMARK 3 3 3.4417 - 3.0069 1.00 4715 144 0.1684 0.2115
REMARK 3 4 3.0069 - 2.7320 1.00 4716 144 0.1631 0.2114
REMARK 3 5 2.7320 - 2.5362 1.00 4677 143 0.1555 0.1711
REMARK 3 6 2.5362 - 2.3867 1.00 4663 143 0.1479 0.1825
REMARK 3 7 2.3867 - 2.2672 1.00 4655 142 0.1505 0.2000
REMARK 3 8 2.2672 - 2.1685 1.00 4623 141 0.1573 0.1917
REMARK 3 9 2.1685 - 2.0851 1.00 4680 144 0.1692 0.2005
REMARK 3 10 2.0851 - 2.0131 1.00 4627 141 0.1738 0.2137
REMARK 3 11 2.0131 - 1.9502 1.00 4629 141 0.1852 0.2275
REMARK 3 12 1.9502 - 1.8944 1.00 4622 141 0.2101 0.2476
REMARK 3 13 1.8944 - 1.8446 1.00 4617 141 0.2348 0.2820
REMARK 3 14 1.8446 - 1.7996 0.98 4528 139 0.2710 0.2994
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.170
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.040
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 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 : 0.011 4511
REMARK 3 ANGLE : 1.295 6137
REMARK 3 CHIRALITY : 0.053 666
REMARK 3 PLANARITY : 0.006 789
REMARK 3 DIHEDRAL : 15.048 1723
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 5 THROUGH 78 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.6131 15.0960 -14.0957
REMARK 3 T TENSOR
REMARK 3 T11: 0.4272 T22: 0.2097
REMARK 3 T33: 0.3206 T12: 0.0414
REMARK 3 T13: -0.1205 T23: 0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 0.7707 L22: 2.7609
REMARK 3 L33: 1.6133 L12: 0.2425
REMARK 3 L13: 0.4254 L23: -1.5110
REMARK 3 S TENSOR
REMARK 3 S11: -0.1821 S12: -0.0025 S13: 0.3041
REMARK 3 S21: 0.0379 S22: 0.0505 S23: 0.2303
REMARK 3 S31: -0.7469 S32: -0.1207 S33: -0.0131
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 79 THROUGH 165 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5471 2.9500 -7.7872
REMARK 3 T TENSOR
REMARK 3 T11: 0.1871 T22: 0.1857
REMARK 3 T33: 0.2046 T12: -0.0060
REMARK 3 T13: -0.0479 T23: 0.0048
REMARK 3 L TENSOR
REMARK 3 L11: 0.9794 L22: 2.2596
REMARK 3 L33: 1.6798 L12: 0.2588
REMARK 3 L13: 0.5396 L23: -0.2177
REMARK 3 S TENSOR
REMARK 3 S11: -0.1078 S12: -0.1164 S13: 0.2007
REMARK 3 S21: 0.0007 S22: 0.0155 S23: -0.1041
REMARK 3 S31: -0.2992 S32: 0.0821 S33: 0.0999
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 166 THROUGH 320 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.8432 -6.4368 -26.6969
REMARK 3 T TENSOR
REMARK 3 T11: 0.3787 T22: 0.2290
REMARK 3 T33: 0.2715 T12: -0.0390
REMARK 3 T13: -0.1712 T23: 0.0194
REMARK 3 L TENSOR
REMARK 3 L11: 1.3810 L22: 1.9649
REMARK 3 L33: 2.1259 L12: -0.5604
REMARK 3 L13: 0.2737 L23: -0.7841
REMARK 3 S TENSOR
REMARK 3 S11: 0.0717 S12: 0.1468 S13: -0.0267
REMARK 3 S21: -0.6181 S22: 0.0283 S23: 0.3808
REMARK 3 S31: 0.0519 S32: -0.2619 S33: -0.0188
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 321 THROUGH 375 )
REMARK 3 ORIGIN FOR THE GROUP (A): 13.4158 -6.2962 -4.2221
REMARK 3 T TENSOR
REMARK 3 T11: 0.1798 T22: 0.1955
REMARK 3 T33: 0.2058 T12: 0.0197
REMARK 3 T13: -0.0502 T23: 0.0391
REMARK 3 L TENSOR
REMARK 3 L11: 1.4892 L22: 2.3579
REMARK 3 L33: 1.6426 L12: 0.5865
REMARK 3 L13: -0.2374 L23: -0.4579
REMARK 3 S TENSOR
REMARK 3 S11: 0.0860 S12: -0.4007 S13: -0.0531
REMARK 3 S21: 0.1219 S22: -0.0914 S23: -0.1993
REMARK 3 S31: 0.0969 S32: 0.0562 S33: 0.0364
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 52 THROUGH 74 )
REMARK 3 ORIGIN FOR THE GROUP (A): 14.8247 -19.5376 11.5093
REMARK 3 T TENSOR
REMARK 3 T11: 0.1882 T22: 0.7106
REMARK 3 T33: 0.3117 T12: -0.0623
REMARK 3 T13: -0.1055 T23: 0.2898
REMARK 3 L TENSOR
REMARK 3 L11: 2.7172 L22: 2.6422
REMARK 3 L33: 2.6786 L12: -1.1610
REMARK 3 L13: 0.8161 L23: -0.7245
REMARK 3 S TENSOR
REMARK 3 S11: 0.1889 S12: -0.7916 S13: 0.0392
REMARK 3 S21: 0.4444 S22: -0.3826 S23: -0.6621
REMARK 3 S31: -0.0676 S32: 0.8391 S33: 0.0950
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 75 THROUGH 177 )
REMARK 3 ORIGIN FOR THE GROUP (A): 6.9545 -23.6240 5.0599
REMARK 3 T TENSOR
REMARK 3 T11: 0.1800 T22: 0.3869
REMARK 3 T33: 0.3215 T12: -0.0031
REMARK 3 T13: -0.0033 T23: 0.1892
REMARK 3 L TENSOR
REMARK 3 L11: 2.1836 L22: 1.4015
REMARK 3 L33: 1.2726 L12: 0.6738
REMARK 3 L13: 0.0230 L23: 0.0915
REMARK 3 S TENSOR
REMARK 3 S11: -0.0024 S12: -0.6382 S13: -0.5896
REMARK 3 S21: 0.2054 S22: -0.0300 S23: 0.0344
REMARK 3 S31: 0.0997 S32: 0.0632 S33: -0.0272
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 1058 THROUGH 1076 )
REMARK 3 ORIGIN FOR THE GROUP (A): -15.1858 19.5303 -28.8396
REMARK 3 T TENSOR
REMARK 3 T11: 0.8082 T22: 0.6079
REMARK 3 T33: 0.7728 T12: 0.2334
REMARK 3 T13: -0.2050 T23: 0.0232
REMARK 3 L TENSOR
REMARK 3 L11: 2.6238 L22: 3.5672
REMARK 3 L33: 5.3095 L12: -0.9456
REMARK 3 L13: 0.0952 L23: 0.3039
REMARK 3 S TENSOR
REMARK 3 S11: 0.1595 S12: 0.0975 S13: 0.5393
REMARK 3 S21: -0.1405 S22: -0.1930 S23: 0.9484
REMARK 3 S31: -0.4880 S32: -1.0750 S33: 0.0015
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 1077 THROUGH 1091 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.0964 23.6439 -7.4851
REMARK 3 T TENSOR
REMARK 3 T11: 0.9314 T22: 0.5490
REMARK 3 T33: 0.9100 T12: 0.1543
REMARK 3 T13: -0.0247 T23: -0.1356
REMARK 3 L TENSOR
REMARK 3 L11: 2.1362 L22: 2.3622
REMARK 3 L33: 1.9189 L12: -0.4016
REMARK 3 L13: -0.0782 L23: -0.5909
REMARK 3 S TENSOR
REMARK 3 S11: -0.0720 S12: 0.0400 S13: 0.3848
REMARK 3 S21: 0.1348 S22: -0.1948 S23: -0.1585
REMARK 3 S31: -0.9144 S32: -0.4909 S33: 0.0530
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 1092 THROUGH 1099 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.2357 12.7814 0.0111
REMARK 3 T TENSOR
REMARK 3 T11: 0.5744 T22: 0.7132
REMARK 3 T33: 0.8847 T12: -0.1922
REMARK 3 T13: -0.0926 T23: -0.2169
REMARK 3 L TENSOR
REMARK 3 L11: 1.5999 L22: 2.8284
REMARK 3 L33: 3.4202 L12: 1.1113
REMARK 3 L13: 0.9375 L23: -0.5959
REMARK 3 S TENSOR
REMARK 3 S11: -0.1704 S12: -0.4251 S13: 0.3869
REMARK 3 S21: 0.3649 S22: 0.0514 S23: -0.7328
REMARK 3 S31: -0.5479 S32: 0.4057 S33: 0.2113
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4PKG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-MAY-14.
REMARK 100 THE DEPOSITION ID IS D_1000201557.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-OCT-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X6A
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : CHANNEL CUT SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 67450
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 13.40
REMARK 200 R MERGE (I) : 0.05000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 43.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 8.20
REMARK 200 R MERGE FOR SHELL (I) : 0.57600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.500
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: PDB ENTRY 1EQY
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.86
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.18 M SODIUM FLUORIDE, 11% W/V
REMARK 280 PEG3350, 1% V/V PEG1000, 1% V/V PEG400, PH 7.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 34.73550
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.19800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.93300
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.19800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.73550
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.93300
REMARK 290 SMTRY3 4 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: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6570 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G
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 CYS A 0
REMARK 465 ASP A 1
REMARK 465 GLU A 2
REMARK 465 ASP A 3
REMARK 465 GLU A 4
REMARK 465 GLY G 178
REMARK 465 SER G 179
REMARK 465 GLY G 180
REMARK 465 GLY G 181
REMARK 465 SER G 182
REMARK 465 GLY G 183
REMARK 465 GLY G 184
REMARK 465 SER G 185
REMARK 465 GLN G 1050
REMARK 465 LYS G 1051
REMARK 465 ASP G 1052
REMARK 465 GLN G 1053
REMARK 465 THR G 1054
REMARK 465 THR G 1055
REMARK 465 LYS G 1056
REMARK 465 ALA G 1057
REMARK 465 GLN G 1100
REMARK 465 LYS G 1101
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 HH TYR A 169 OD2 ASP G 137 1.48
REMARK 500 OH TYR A 169 OD2 ASP G 137 2.15
REMARK 500 OG SER A 271 O HOH A 718 2.15
REMARK 500 O HOH G 1429 O HOH G 1460 2.16
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 MET A 47 -174.68 -61.15
REMARK 500 MET A 47 -173.69 -62.95
REMARK 500 LYS A 50 107.64 -57.49
REMARK 500 ALA A 181 -158.97 -161.28
REMARK 500 ASN A 296 56.21 -143.51
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 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 167 OE1
REMARK 620 2 HOH A 699 O 70.4
REMARK 620 3 ASP G 136 OD1 142.7 145.5
REMARK 620 4 ASP G 136 OD2 93.5 163.4 49.7
REMARK 620 5 GLY G 141 O 139.5 78.9 74.7 117.4
REMARK 620 6 ALA G 143 O 95.5 84.4 82.7 93.2 107.4
REMARK 620 7 HOH G1422 O 76.3 89.0 106.2 91.3 77.4 170.9
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ATP A 401 O3G
REMARK 620 2 ATP A 401 O1B 77.1
REMARK 620 3 HOH A 556 O 77.3 92.3
REMARK 620 4 HOH A 557 O 147.4 82.6 78.3
REMARK 620 5 HOH A 719 O 135.6 92.8 147.0 70.1
REMARK 620 6 HOH A 720 O 96.0 170.7 80.1 100.7 96.5
REMARK 620 7 HOH A 736 O 67.2 98.5 139.3 141.9 71.8 84.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA G1201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY G 92 O
REMARK 620 2 ASP G 93 OD1 75.1
REMARK 620 3 GLU G 124 OE1 76.5 100.7
REMARK 620 4 GLU G 124 OE2 123.2 88.8 53.2
REMARK 620 5 VAL G 172 O 148.2 88.7 134.3 82.8
REMARK 620 6 HOH G1348 O 103.6 175.8 75.1 88.7 94.2
REMARK 620 7 HOH G1360 O 78.3 97.8 143.4 158.5 77.0 85.7
REMARK 620 N 1 2 3 4 5 6
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA G 1201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4PKH RELATED DB: PDB
REMARK 900 RELATED ID: 4PKI RELATED DB: PDB
DBREF 4PKG A -1 375 UNP P68135 ACTS_RABIT 1 377
DBREF 4PKG G 52 176 UNP P06396 GELS_HUMAN 12 136
DBREF 4PKG G 1050 1101 UNP P28289 TMOD1_HUMAN 50 101
SEQADV 4PKG GLY G 177 UNP P06396 LINKER
SEQADV 4PKG GLY G 178 UNP P06396 LINKER
SEQADV 4PKG SER G 179 UNP P06396 LINKER
SEQADV 4PKG GLY G 180 UNP P06396 LINKER
SEQADV 4PKG GLY G 181 UNP P06396 LINKER
SEQADV 4PKG SER G 182 UNP P06396 LINKER
SEQADV 4PKG GLY G 183 UNP P06396 LINKER
SEQADV 4PKG GLY G 184 UNP P06396 LINKER
SEQADV 4PKG SER G 185 UNP P06396 LINKER
SEQRES 1 A 377 MET CYS ASP GLU ASP GLU THR THR ALA LEU VAL CYS ASP
SEQRES 2 A 377 ASN GLY SER GLY LEU VAL LYS ALA GLY PHE ALA GLY ASP
SEQRES 3 A 377 ASP ALA PRO ARG ALA VAL PHE PRO SER ILE VAL GLY ARG
SEQRES 4 A 377 PRO ARG HIS GLN GLY VAL MET VAL GLY MET GLY GLN LYS
SEQRES 5 A 377 ASP SER TYR VAL GLY ASP GLU ALA GLN SER LYS ARG GLY
SEQRES 6 A 377 ILE LEU THR LEU LYS TYR PRO ILE GLU HIC GLY ILE ILE
SEQRES 7 A 377 THR ASN TRP ASP ASP MET GLU LYS ILE TRP HIS HIS THR
SEQRES 8 A 377 PHE TYR ASN GLU LEU ARG VAL ALA PRO GLU GLU HIS PRO
SEQRES 9 A 377 THR LEU LEU THR GLU ALA PRO LEU ASN PRO LYS ALA ASN
SEQRES 10 A 377 ARG GLU LYS MET THR GLN ILE MET PHE GLU THR PHE ASN
SEQRES 11 A 377 VAL PRO ALA MET TYR VAL ALA ILE GLN ALA VAL LEU SER
SEQRES 12 A 377 LEU TYR ALA SER GLY ARG THR THR GLY ILE VAL LEU ASP
SEQRES 13 A 377 SER GLY ASP GLY VAL THR HIS ASN VAL PRO ILE TYR GLU
SEQRES 14 A 377 GLY TYR ALA LEU PRO HIS ALA ILE MET ARG LEU ASP LEU
SEQRES 15 A 377 ALA GLY ARG ASP LEU THR ASP TYR LEU MET LYS ILE LEU
SEQRES 16 A 377 THR GLU ARG GLY TYR SER PHE VAL THR THR ALA GLU ARG
SEQRES 17 A 377 GLU ILE VAL ARG ASP ILE LYS GLU LYS LEU CYS TYR VAL
SEQRES 18 A 377 ALA LEU ASP PHE GLU ASN GLU MET ALA THR ALA ALA SER
SEQRES 19 A 377 SER SER SER LEU GLU LYS SER TYR GLU LEU PRO ASP GLY
SEQRES 20 A 377 GLN VAL ILE THR ILE GLY ASN GLU ARG PHE ARG CYS PRO
SEQRES 21 A 377 GLU THR LEU PHE GLN PRO SER PHE ILE GLY MET GLU SER
SEQRES 22 A 377 ALA GLY ILE HIS GLU THR THR TYR ASN SER ILE MET LYS
SEQRES 23 A 377 CYS ASP ILE ASP ILE ARG LYS ASP LEU TYR ALA ASN ASN
SEQRES 24 A 377 VAL MET SER GLY GLY THR THR MET TYR PRO GLY ILE ALA
SEQRES 25 A 377 ASP ARG MET GLN LYS GLU ILE THR ALA LEU ALA PRO SER
SEQRES 26 A 377 THR MET LYS ILE LYS ILE ILE ALA PRO PRO GLU ARG LYS
SEQRES 27 A 377 TYR SER VAL TRP ILE GLY GLY SER ILE LEU ALA SER LEU
SEQRES 28 A 377 SER THR PHE GLN GLN MET TRP ILE THR LYS GLN GLU TYR
SEQRES 29 A 377 ASP GLU ALA GLY PRO SER ILE VAL HIS ARG LYS CYS PHE
SEQRES 1 G 186 MET VAL VAL GLU HIS PRO GLU PHE LEU LYS ALA GLY LYS
SEQRES 2 G 186 GLU PRO GLY LEU GLN ILE TRP ARG VAL GLU LYS PHE ASP
SEQRES 3 G 186 LEU VAL PRO VAL PRO THR ASN LEU TYR GLY ASP PHE PHE
SEQRES 4 G 186 THR GLY ASP ALA TYR VAL ILE LEU LYS THR VAL GLN LEU
SEQRES 5 G 186 ARG ASN GLY ASN LEU GLN TYR ASP LEU HIS TYR TRP LEU
SEQRES 6 G 186 GLY ASN GLU CYS SER GLN ASP GLU SER GLY ALA ALA ALA
SEQRES 7 G 186 ILE PHE THR VAL GLN LEU ASP ASP TYR LEU ASN GLY ARG
SEQRES 8 G 186 ALA VAL GLN HIS ARG GLU VAL GLN GLY PHE GLU SER ALA
SEQRES 9 G 186 THR PHE LEU GLY TYR PHE LYS SER GLY LEU LYS TYR LYS
SEQRES 10 G 186 LYS GLY GLY VAL ALA SER GLY PHE GLY GLY SER GLY GLY
SEQRES 11 G 186 SER GLY GLY SER GLN LYS ASP GLN THR THR LYS ALA PRO
SEQRES 12 G 186 THR GLY PRO PHE LYS ARG GLU GLU LEU LEU ASP HIS LEU
SEQRES 13 G 186 GLU LYS GLN ALA LYS GLU PHE LYS ASP ARG GLU ASP LEU
SEQRES 14 G 186 VAL PRO TYR THR GLY GLU LYS ARG GLY LYS VAL TRP VAL
SEQRES 15 G 186 PRO LYS GLN LYS
MODRES 4PKG HIC A 73 HIS MODIFIED RESIDUE
HET HIC A 73 20
HET ATP A 401 42
HET CA A 402 1
HET CA A 403 1
HET CA G1201 1
HETNAM HIC 4-METHYL-HISTIDINE
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
HETNAM CA CALCIUM ION
FORMUL 1 HIC C7 H11 N3 O2
FORMUL 3 ATP C10 H16 N5 O13 P3
FORMUL 4 CA 3(CA 2+)
FORMUL 7 HOH *511(H2 O)
HELIX 1 AA1 GLY A 55 LYS A 61 1 7
HELIX 2 AA2 ASN A 78 GLU A 93 1 16
HELIX 3 AA3 ALA A 97 HIS A 101 5 5
HELIX 4 AA4 PRO A 112 THR A 126 1 15
HELIX 5 AA5 GLN A 137 SER A 145 1 9
HELIX 6 AA6 PRO A 172 ILE A 175 5 4
HELIX 7 AA7 ALA A 181 GLY A 197 1 17
HELIX 8 AA8 THR A 202 ALA A 204 5 3
HELIX 9 AA9 GLU A 205 CYS A 217 1 13
HELIX 10 AB1 ASP A 222 SER A 233 1 12
HELIX 11 AB2 ASN A 252 GLN A 263 1 12
HELIX 12 AB3 PRO A 264 GLY A 268 5 5
HELIX 13 AB4 GLY A 273 LYS A 284 1 12
HELIX 14 AB5 ASP A 286 ALA A 295 1 10
HELIX 15 AB6 GLY A 301 MET A 305 5 5
HELIX 16 AB7 GLY A 308 ALA A 321 1 14
HELIX 17 AB8 TYR A 337 LEU A 349 1 13
HELIX 18 AB9 SER A 350 GLN A 353 5 4
HELIX 19 AC1 LYS A 359 GLY A 366 1 8
HELIX 20 AC2 ILE A 369 CYS A 374 1 6
HELIX 21 AC3 HIS G 56 ALA G 62 1 7
HELIX 22 AC4 PRO G 82 TYR G 86 5 5
HELIX 23 AC5 SER G 121 LEU G 139 1 19
HELIX 24 AC6 SER G 154 TYR G 160 1 7
HELIX 25 AC7 LYS G 1063 GLU G 1077 1 15
SHEET 1 AA1 6 ALA A 29 PRO A 32 0
SHEET 2 AA1 6 LEU A 16 PHE A 21 -1 N VAL A 17 O PHE A 31
SHEET 3 AA1 6 LEU A 8 ASN A 12 -1 N ASP A 11 O LYS A 18
SHEET 4 AA1 6 THR A 103 GLU A 107 1 O LEU A 104 N CYS A 10
SHEET 5 AA1 6 ALA A 131 ILE A 136 1 O TYR A 133 N LEU A 105
SHEET 6 AA1 6 ILE A 357 THR A 358 -1 O ILE A 357 N MET A 132
SHEET 1 AA2 3 TYR A 53 VAL A 54 0
SHEET 2 AA2 3 VAL A 35 PRO A 38 -1 N GLY A 36 O TYR A 53
SHEET 3 AA2 3 LEU A 65 LYS A 68 -1 O THR A 66 N ARG A 37
SHEET 1 AA3 2 ILE A 71 GLU A 72 0
SHEET 2 AA3 2 ILE A 75 ILE A 76 -1 O ILE A 75 N GLU A 72
SHEET 1 AA4 3 TYR A 169 ALA A 170 0
SHEET 2 AA4 3 THR A 160 TYR A 166 -1 N TYR A 166 O TYR A 169
SHEET 3 AA4 3 MET A 176 LEU A 178 -1 O LEU A 178 N THR A 160
SHEET 1 AA5 5 TYR A 169 ALA A 170 0
SHEET 2 AA5 5 THR A 160 TYR A 166 -1 N TYR A 166 O TYR A 169
SHEET 3 AA5 5 GLY A 150 SER A 155 -1 N GLY A 150 O ILE A 165
SHEET 4 AA5 5 ASN A 297 SER A 300 1 O SER A 300 N LEU A 153
SHEET 5 AA5 5 ILE A 329 ILE A 330 1 O ILE A 330 N ASN A 297
SHEET 1 AA6 2 LYS A 238 GLU A 241 0
SHEET 2 AA6 2 VAL A 247 ILE A 250 -1 O ILE A 248 N TYR A 240
SHEET 1 AA7 5 ASP G 77 PRO G 80 0
SHEET 2 AA7 5 GLY G 67 GLU G 74 -1 N ARG G 72 O VAL G 79
SHEET 3 AA7 5 ALA G 94 GLN G 102 -1 O THR G 100 N GLY G 67
SHEET 4 AA7 5 LEU G 108 LEU G 116 -1 O HIS G 113 N ILE G 97
SHEET 5 AA7 5 ALA G 143 VAL G 149 1 O GLU G 148 N TYR G 114
SHEET 1 AA8 2 ASP G 88 PHE G 90 0
SHEET 2 AA8 2 LYS G 166 LYS G 168 1 O LYS G 166 N PHE G 89
LINK C GLU A 72 N HIC A 73 1555 1555 1.32
LINK C HIC A 73 N GLY A 74 1555 1555 1.34
LINK OE1 GLU A 167 CA CA A 403 1555 1555 2.88
LINK O3G ATP A 401 CA CA A 402 1555 1555 2.37
LINK O1B ATP A 401 CA CA A 402 1555 1555 2.28
LINK CA CA A 402 O HOH A 556 1555 1555 2.41
LINK CA CA A 402 O HOH A 557 1555 1555 2.32
LINK CA CA A 402 O HOH A 719 1555 1555 2.36
LINK CA CA A 402 O HOH A 720 1555 1555 2.28
LINK CA CA A 402 O HOH A 736 1555 1555 2.55
LINK CA CA A 403 O HOH A 699 1555 1555 2.58
LINK CA CA A 403 OD1 ASP G 136 1555 1555 2.78
LINK CA CA A 403 OD2 ASP G 136 1555 1555 2.29
LINK CA CA A 403 O GLY G 141 1555 1555 2.56
LINK CA CA A 403 O ALA G 143 1555 1555 2.33
LINK CA CA A 403 O HOH G1422 1555 1555 2.48
LINK O GLY G 92 CA CA G1201 1555 1555 2.22
LINK OD1 ASP G 93 CA CA G1201 1555 1555 2.31
LINK OE1 GLU G 124 CA CA G1201 1555 1555 2.48
LINK OE2 GLU G 124 CA CA G1201 1555 1555 2.43
LINK O VAL G 172 CA CA G1201 1555 1555 2.38
LINK CA CA G1201 O HOH G1348 1555 1555 2.29
LINK CA CA G1201 O HOH G1360 1555 1555 2.35
CISPEP 1 VAL A 45 GLY A 46 0 8.70
CISPEP 2 MET G 52 VAL G 53 0 4.24
SITE 1 AC1 28 GLY A 13 SER A 14 GLY A 15 LEU A 16
SITE 2 AC1 28 LYS A 18 GLY A 156 ASP A 157 GLY A 158
SITE 3 AC1 28 VAL A 159 GLY A 182 ARG A 210 LYS A 213
SITE 4 AC1 28 GLU A 214 GLY A 301 GLY A 302 THR A 303
SITE 5 AC1 28 MET A 305 TYR A 306 LYS A 336 CA A 402
SITE 6 AC1 28 HOH A 555 HOH A 556 HOH A 557 HOH A 561
SITE 7 AC1 28 HOH A 571 HOH A 579 HOH A 731 HOH A 736
SITE 1 AC2 6 ATP A 401 HOH A 556 HOH A 557 HOH A 719
SITE 2 AC2 6 HOH A 720 HOH A 736
SITE 1 AC3 6 GLU A 167 HOH A 699 ASP G 136 GLY G 141
SITE 2 AC3 6 ALA G 143 HOH G1422
SITE 1 AC4 6 GLY G 92 ASP G 93 GLU G 124 VAL G 172
SITE 2 AC4 6 HOH G1348 HOH G1360
CRYST1 69.471 75.866 136.396 90.00 90.00 90.00 P 21 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.014394 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013181 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007332 0.00000
(ATOM LINES ARE NOT SHOWN.)
END