HEADER CALCIUM BINDING/TRANSPORT PROTEIN 23-OCT-18 6MUD
TITLE VOLTAGE-GATED SODIUM CHANNEL NAV1.5 C-TERMINAL DOMAIN IN COMPLEX WITH
TITLE 2 CA2+/CALMODULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN-1;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: SODIUM CHANNEL PROTEIN TYPE 5 SUBUNIT ALPHA;
COMPND 7 CHAIN: B;
COMPND 8 SYNONYM: HH1,SODIUM CHANNEL PROTEIN CARDIAC MUSCLE SUBUNIT ALPHA,
COMPND 9 SODIUM CHANNEL PROTEIN TYPE V SUBUNIT ALPHA,VOLTAGE-GATED SODIUM
COMPND 10 CHANNEL SUBUNIT ALPHA NAV1.5;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CALM1, CALM, CAM, CAM1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: SCN5A;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS VOLTAGE-GATED ION CHANNEL, TRANSPORT PROTEIN, EF-HAND DOMAIN, CALCIUM
KEYWDS 2 BINDING-TRANSPORT PROTEIN COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR B.R.GARDILL,C.C.TUNG,F.VAN PETEGEM
REVDAT 5 13-MAR-24 6MUD 1 REMARK
REVDAT 4 08-JAN-20 6MUD 1 REMARK
REVDAT 3 12-JUN-19 6MUD 1 JRNL
REVDAT 2 22-MAY-19 6MUD 1 JRNL
REVDAT 1 08-MAY-19 6MUD 0
JRNL AUTH B.R.GARDILL,R.E.RIVERA-ACEVEDO,C.C.TUNG,F.VAN PETEGEM
JRNL TITL CRYSTAL STRUCTURES OF CA2+-CALMODULIN BOUND TO NAVC-TERMINAL
JRNL TITL 2 REGIONS SUGGEST ROLE FOR EF-HAND DOMAIN IN BINDING AND
JRNL TITL 3 INACTIVATION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 116 10763 2019
JRNL REFN ESSN 1091-6490
JRNL PMID 31072926
JRNL DOI 10.1073/PNAS.1818618116
REMARK 2
REMARK 2 RESOLUTION. 2.69 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0222
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.69
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.31
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 3 NUMBER OF REFLECTIONS : 10016
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) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.269
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.400
REMARK 3 FREE R VALUE TEST SET COUNT : 459
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.69
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76
REMARK 3 REFLECTION IN BIN (WORKING SET) : 601
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 75.81
REMARK 3 BIN R VALUE (WORKING SET) : 0.4300
REMARK 3 BIN FREE R VALUE SET COUNT : 10
REMARK 3 BIN FREE R VALUE : 0.3380
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2203
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 15
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 71.22
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.54000
REMARK 3 B22 (A**2) : -3.79000
REMARK 3 B33 (A**2) : 6.33000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.849
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.354
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.334
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 35.519
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.915
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2246 ; 0.007 ; 0.014
REMARK 3 BOND LENGTHS OTHERS (A): 1990 ; 0.001 ; 0.017
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3017 ; 1.055 ; 1.660
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4684 ; 0.813 ; 1.641
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 274 ; 6.089 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 138 ;31.882 ;23.478
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 423 ;19.353 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;24.758 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 298 ; 0.049 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2535 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 397 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1 A 64
REMARK 3 ORIGIN FOR THE GROUP (A): -6.932 -6.521 -37.752
REMARK 3 T TENSOR
REMARK 3 T11: 0.1355 T22: 0.0081
REMARK 3 T33: 0.4552 T12: -0.0071
REMARK 3 T13: 0.0030 T23: -0.0316
REMARK 3 L TENSOR
REMARK 3 L11: 5.4134 L22: 2.2341
REMARK 3 L33: 2.0475 L12: -1.0149
REMARK 3 L13: 2.0029 L23: -0.9614
REMARK 3 S TENSOR
REMARK 3 S11: -0.2388 S12: -0.1459 S13: 0.2982
REMARK 3 S21: 0.1558 S22: 0.0043 S23: -0.2223
REMARK 3 S31: -0.0195 S32: -0.0992 S33: 0.2346
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 65 A 147
REMARK 3 ORIGIN FOR THE GROUP (A): -30.552 11.441 -24.863
REMARK 3 T TENSOR
REMARK 3 T11: 0.1982 T22: 0.2013
REMARK 3 T33: 0.4069 T12: -0.0737
REMARK 3 T13: -0.0365 T23: -0.0605
REMARK 3 L TENSOR
REMARK 3 L11: 2.7013 L22: 4.6351
REMARK 3 L33: 2.3536 L12: -2.6209
REMARK 3 L13: -1.7283 L23: 1.0259
REMARK 3 S TENSOR
REMARK 3 S11: -0.0102 S12: -0.3799 S13: 0.2543
REMARK 3 S21: 0.5114 S22: 0.2829 S23: -0.3079
REMARK 3 S31: -0.0556 S32: 0.0434 S33: -0.2727
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1785 B 1801
REMARK 3 ORIGIN FOR THE GROUP (A): -32.826 22.420 -61.364
REMARK 3 T TENSOR
REMARK 3 T11: 0.6273 T22: 0.5637
REMARK 3 T33: 0.5132 T12: -0.2205
REMARK 3 T13: 0.0382 T23: 0.1488
REMARK 3 L TENSOR
REMARK 3 L11: 0.4455 L22: 7.7752
REMARK 3 L33: 4.4793 L12: 1.2657
REMARK 3 L13: 0.0770 L23: -3.8720
REMARK 3 S TENSOR
REMARK 3 S11: -0.3757 S12: 0.3223 S13: 0.1221
REMARK 3 S21: -0.9804 S22: 0.3194 S23: 0.1037
REMARK 3 S31: -0.0260 S32: 0.3950 S33: 0.0563
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1802 B 1837
REMARK 3 ORIGIN FOR THE GROUP (A): -30.323 16.905 -51.248
REMARK 3 T TENSOR
REMARK 3 T11: 0.2280 T22: 0.2500
REMARK 3 T33: 0.4305 T12: 0.0065
REMARK 3 T13: 0.0963 T23: 0.0711
REMARK 3 L TENSOR
REMARK 3 L11: 4.7463 L22: 7.1684
REMARK 3 L33: 3.4803 L12: 2.5132
REMARK 3 L13: -0.6817 L23: 2.5468
REMARK 3 S TENSOR
REMARK 3 S11: -0.2513 S12: 0.2543 S13: 0.0197
REMARK 3 S21: -0.4969 S22: 0.1744 S23: -0.4692
REMARK 3 S31: 0.0944 S32: 0.6271 S33: 0.0769
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1838 B 1862
REMARK 3 ORIGIN FOR THE GROUP (A): -38.931 18.067 -50.085
REMARK 3 T TENSOR
REMARK 3 T11: 0.2245 T22: 0.2417
REMARK 3 T33: 0.2925 T12: -0.0134
REMARK 3 T13: -0.0007 T23: 0.0250
REMARK 3 L TENSOR
REMARK 3 L11: 0.4497 L22: 9.3894
REMARK 3 L33: 1.0706 L12: 0.6882
REMARK 3 L13: -0.4129 L23: -0.1494
REMARK 3 S TENSOR
REMARK 3 S11: -0.1891 S12: 0.1722 S13: 0.0183
REMARK 3 S21: -0.2902 S22: 0.1722 S23: -0.0773
REMARK 3 S31: 0.0435 S32: -0.1716 S33: 0.0169
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1863 B 1878
REMARK 3 ORIGIN FOR THE GROUP (A): -46.070 28.099 -56.039
REMARK 3 T TENSOR
REMARK 3 T11: 0.1710 T22: 0.3169
REMARK 3 T33: 0.4344 T12: 0.1054
REMARK 3 T13: -0.0884 T23: -0.0288
REMARK 3 L TENSOR
REMARK 3 L11: 0.0433 L22: 9.6717
REMARK 3 L33: 7.9802 L12: 0.3662
REMARK 3 L13: 0.4440 L23: -0.4784
REMARK 3 S TENSOR
REMARK 3 S11: -0.0578 S12: -0.0053 S13: 0.0562
REMARK 3 S21: -0.4013 S22: -0.0242 S23: 0.4986
REMARK 3 S31: -0.7038 S32: -0.1097 S33: 0.0820
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1887 B 1894
REMARK 3 ORIGIN FOR THE GROUP (A): -45.653 8.156 -49.658
REMARK 3 T TENSOR
REMARK 3 T11: 0.0977 T22: 0.2830
REMARK 3 T33: 0.3651 T12: -0.0817
REMARK 3 T13: 0.0516 T23: 0.0130
REMARK 3 L TENSOR
REMARK 3 L11: 1.6292 L22: 6.4448
REMARK 3 L33: 8.7070 L12: 0.6997
REMARK 3 L13: 3.6447 L23: -0.2780
REMARK 3 S TENSOR
REMARK 3 S11: -0.0793 S12: 0.0913 S13: -0.0001
REMARK 3 S21: 0.0196 S22: 0.2011 S23: 0.4038
REMARK 3 S31: -0.1960 S32: 0.1659 S33: -0.1218
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1895 B 1920
REMARK 3 ORIGIN FOR THE GROUP (A): -31.521 5.311 -25.964
REMARK 3 T TENSOR
REMARK 3 T11: 0.2249 T22: 0.1178
REMARK 3 T33: 0.3789 T12: -0.0373
REMARK 3 T13: -0.0347 T23: -0.0302
REMARK 3 L TENSOR
REMARK 3 L11: 1.3336 L22: 3.9651
REMARK 3 L33: 11.5792 L12: -2.0243
REMARK 3 L13: 3.8948 L23: -5.7806
REMARK 3 S TENSOR
REMARK 3 S11: 0.0807 S12: 0.0839 S13: 0.1023
REMARK 3 S21: -0.0561 S22: -0.1919 S23: -0.2307
REMARK 3 S31: 0.4026 S32: 0.1923 S33: 0.1112
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 6MUD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-OCT-18.
REMARK 100 THE DEPOSITION ID IS D_1000237596.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-SEP-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-D
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033000
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : K-B PAIR OF BIMORPH MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS NOVEMBER 11, 2013
REMARK 200 DATA SCALING SOFTWARE : XDS NOVEMBER 11, 2013
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10476
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.690
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.9
REMARK 200 DATA REDUNDANCY : 3.250
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.69
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 83.3
REMARK 200 DATA REDUNDANCY IN SHELL : 2.39
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.890
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.14
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5-15 % (W/V) PEG 4000, 0.1 M TRIS, PH
REMARK 280 9.5, 0.1 M MGCL2, AND 5 % (V/V) ISOPROPANOL, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
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+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 0.00000
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 0.00000
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 32.78950
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.01600
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 70.34200
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 32.78950
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.01600
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 70.34200
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 32.78950
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 42.01600
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.34200
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 32.78950
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 42.01600
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 70.34200
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: 1660 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17250 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL
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 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 0
REMARK 465 LYS A 148
REMARK 465 SER B 1783
REMARK 465 ASN B 1784
REMARK 465 PHE B 1879
REMARK 465 MET B 1880
REMARK 465 ALA B 1881
REMARK 465 ALA B 1882
REMARK 465 ASN B 1883
REMARK 465 PRO B 1884
REMARK 465 SER B 1885
REMARK 465 LYS B 1886
REMARK 465 LEU B 1921
REMARK 465 LYS B 1922
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 2 53.09 -108.53
REMARK 500 LYS A 115 172.17 -54.66
REMARK 500 ASP B1802 59.11 -145.35
REMARK 500 SER B1812 3.93 -64.98
REMARK 500 VAL B1843 -166.33 -75.91
REMARK 500 GLN B1918 33.81 -97.11
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 ARG A 90 0.12 SIDE CHAIN
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 A1001 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 20 OD1
REMARK 620 2 ASP A 22 OD1 77.4
REMARK 620 3 ASP A 24 OD1 82.8 81.8
REMARK 620 4 THR A 26 O 88.1 162.4 86.5
REMARK 620 5 GLU A 31 OE1 123.2 120.3 147.4 76.1
REMARK 620 6 GLU A 31 OE2 94.3 73.5 155.1 118.1 51.7
REMARK 620 7 HOH A1107 O 157.3 102.5 74.8 87.0 76.9 107.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1002 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 56 OD1
REMARK 620 2 ASP A 58 OD1 72.7
REMARK 620 3 ASN A 60 OD1 93.0 85.0
REMARK 620 4 THR A 62 O 71.5 139.9 79.5
REMARK 620 5 GLU A 67 OE1 95.4 126.3 148.7 74.8
REMARK 620 6 GLU A 67 OE2 83.7 76.3 161.1 116.6 50.1
REMARK 620 7 HOH A1101 O 152.0 91.1 108.5 128.9 75.7 70.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1004 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 93 OD1
REMARK 620 2 ASP A 95 OD1 82.5
REMARK 620 3 ASN A 97 OD1 84.4 92.7
REMARK 620 4 TYR A 99 O 92.3 170.1 78.3
REMARK 620 5 GLU A 104 OE1 95.6 56.1 148.3 133.2
REMARK 620 6 GLU A 104 OE2 108.3 105.5 158.8 84.1 49.6
REMARK 620 7 HOH A1103 O 163.3 93.3 79.7 89.3 95.4 88.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A1003 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 129 OD1
REMARK 620 2 ASP A 131 OD2 81.0
REMARK 620 3 ASP A 133 OD1 79.8 85.5
REMARK 620 4 GLN A 135 O 81.4 158.3 78.8
REMARK 620 5 GLU A 140 OE1 112.9 107.7 162.5 90.8
REMARK 620 6 GLU A 140 OE2 86.5 66.7 150.7 124.7 45.9
REMARK 620 7 HOH A1106 O 163.2 82.3 100.6 115.2 70.9 85.4
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 CA A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 1003
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 1004
DBREF 6MUD A 0 148 UNP P0DP23 CALM1_HUMAN 1 149
DBREF 6MUD B 1786 1922 UNP Q14524 SCN5A_HUMAN 1786 1922
SEQADV 6MUD SER B 1783 UNP Q14524 EXPRESSION TAG
SEQADV 6MUD ASN B 1784 UNP Q14524 EXPRESSION TAG
SEQADV 6MUD ALA B 1785 UNP Q14524 EXPRESSION TAG
SEQRES 1 A 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 A 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 A 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 A 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 A 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 A 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 A 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 A 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 A 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 A 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 A 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 A 149 GLN MET MET THR ALA LYS
SEQRES 1 B 140 SER ASN ALA LEU SER GLU ASP ASP PHE ASP MET PHE TYR
SEQRES 2 B 140 GLU ILE TRP GLU LYS PHE ASP PRO GLU ALA THR GLN PHE
SEQRES 3 B 140 ILE GLU TYR SER VAL LEU SER ASP PHE ALA ASP ALA LEU
SEQRES 4 B 140 SER GLU PRO LEU ARG ILE ALA LYS PRO ASN GLN ILE SER
SEQRES 5 B 140 LEU ILE ASN MET ASP LEU PRO MET VAL SER GLY ASP ARG
SEQRES 6 B 140 ILE HIS CYS MET ASP ILE LEU PHE ALA PHE THR LYS ARG
SEQRES 7 B 140 VAL LEU GLY GLU SER GLY GLU MET ASP ALA LEU LYS ILE
SEQRES 8 B 140 GLN MET GLU GLU LYS PHE MET ALA ALA ASN PRO SER LYS
SEQRES 9 B 140 ILE SER TYR GLU PRO ILE THR THR THR LEU ARG ARG LYS
SEQRES 10 B 140 HIS GLU GLU VAL SER ALA MET VAL ILE GLN ARG ALA PHE
SEQRES 11 B 140 ARG ARG HIS LEU LEU GLN ARG SER LEU LYS
HET CA A1001 1
HET CA A1002 1
HET CA A1003 1
HET CA A1004 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 4(CA 2+)
FORMUL 7 HOH *15(H2 O)
HELIX 1 AA1 THR A 5 ASP A 20 1 16
HELIX 2 AA2 THR A 28 LEU A 39 1 12
HELIX 3 AA3 THR A 44 ASP A 56 1 13
HELIX 4 AA4 PHE A 65 ASP A 80 1 16
HELIX 5 AA5 ASP A 80 ASP A 93 1 14
HELIX 6 AA6 SER A 101 MET A 109 1 9
HELIX 7 AA7 THR A 117 ASP A 129 1 13
HELIX 8 AA8 ASN A 137 MET A 144 1 8
HELIX 9 AA9 SER B 1787 ASP B 1802 1 16
HELIX 10 AB1 VAL B 1813 LEU B 1821 1 9
HELIX 11 AB2 ASN B 1831 MET B 1838 1 8
HELIX 12 AB3 CYS B 1850 GLY B 1863 1 14
HELIX 13 AB4 SER B 1865 LYS B 1878 1 14
HELIX 14 AB5 THR B 1895 GLN B 1918 1 24
SHEET 1 AA1 2 THR A 26 ILE A 27 0
SHEET 2 AA1 2 ILE A 63 ASP A 64 -1 O ILE A 63 N ILE A 27
SHEET 1 AA2 2 PHE B1808 GLU B1810 0
SHEET 2 AA2 2 ARG B1847 HIS B1849 -1 O ILE B1848 N ILE B1809
SHEET 1 AA3 2 PRO B1841 MET B1842 0
SHEET 2 AA3 2 THR B1893 THR B1894 -1 O THR B1893 N MET B1842
LINK OD1 ASP A 20 CA CA A1001 1555 1555 2.41
LINK OD1 ASP A 22 CA CA A1001 1555 1555 2.13
LINK OD1 ASP A 24 CA CA A1001 1555 1555 2.34
LINK O THR A 26 CA CA A1001 1555 1555 2.25
LINK OE1 GLU A 31 CA CA A1001 1555 1555 2.42
LINK OE2 GLU A 31 CA CA A1001 1555 1555 2.66
LINK OD1 ASP A 56 CA CA A1002 1555 1555 2.21
LINK OD1 ASP A 58 CA CA A1002 1555 1555 2.23
LINK OD1 ASN A 60 CA CA A1002 1555 1555 2.69
LINK O THR A 62 CA CA A1002 1555 1555 2.42
LINK OE1 GLU A 67 CA CA A1002 1555 1555 2.66
LINK OE2 GLU A 67 CA CA A1002 1555 1555 2.49
LINK OD1 ASP A 93 CA CA A1004 1555 1555 2.23
LINK OD1 ASP A 95 CA CA A1004 1555 1555 2.14
LINK OD1 ASN A 97 CA CA A1004 1555 1555 2.34
LINK O TYR A 99 CA CA A1004 1555 1555 2.04
LINK OE1 GLU A 104 CA CA A1004 1555 1555 2.81
LINK OE2 GLU A 104 CA CA A1004 1555 1555 2.42
LINK OD1 ASP A 129 CA CA A1003 1555 1555 2.34
LINK OD2 ASP A 131 CA CA A1003 1555 1555 2.15
LINK OD1 ASP A 133 CA CA A1003 1555 1555 2.25
LINK O GLN A 135 CA CA A1003 1555 1555 2.28
LINK OE1 GLU A 140 CA CA A1003 1555 1555 2.55
LINK OE2 GLU A 140 CA CA A1003 1555 1555 2.98
LINK CA CA A1001 O HOH A1107 1555 1555 2.27
LINK CA CA A1002 O HOH A1101 1555 1555 2.00
LINK CA CA A1003 O HOH A1106 1555 1555 2.19
LINK CA CA A1004 O HOH A1103 1555 1555 2.36
CISPEP 1 GLU B 1823 PRO B 1824 0 8.42
CISPEP 2 LYS B 1829 PRO B 1830 0 -2.26
SITE 1 AC1 6 ASP A 20 ASP A 22 ASP A 24 THR A 26
SITE 2 AC1 6 GLU A 31 HOH A1107
SITE 1 AC2 6 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 AC2 6 GLU A 67 HOH A1101
SITE 1 AC3 6 ASP A 129 ASP A 131 ASP A 133 GLN A 135
SITE 2 AC3 6 GLU A 140 HOH A1106
SITE 1 AC4 6 ASP A 93 ASP A 95 ASN A 97 TYR A 99
SITE 2 AC4 6 GLU A 104 HOH A1103
CRYST1 65.579 84.032 140.684 90.00 90.00 90.00 I 2 2 2 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 0.015249 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011900 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007108 0.00000
(ATOM LINES ARE NOT SHOWN.)
END