HEADER TRANSPORT PROTEIN 19-MAR-13 4JQ0
TITLE VOLTAGE-GATED SODIUM CHANNEL 1.5 C-TERMINAL DOMAIN IN COMPLEX WITH
TITLE 2 FGF12B AND CA2+/CALMODULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIBROBLAST GROWTH FACTOR 12;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FGF-12, FIBROBLAST GROWTH FACTOR HOMOLOGOUS FACTOR 1, FHF-1,
COMPND 5 MYOCYTE-ACTIVATING FACTOR;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: CALMODULIN;
COMPND 9 CHAIN: C;
COMPND 10 SYNONYM: CAM;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: SODIUM CHANNEL PROTEIN TYPE 5 SUBUNIT ALPHA;
COMPND 14 CHAIN: D;
COMPND 15 SYNONYM: HH1, SODIUM CHANNEL PROTEIN CARDIAC MUSCLE SUBUNIT ALPHA,
COMPND 16 SODIUM CHANNEL PROTEIN TYPE V SUBUNIT ALPHA, VOLTAGE-GATED SODIUM
COMPND 17 CHANNEL SUBUNIT ALPHA NAV1.5;
COMPND 18 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: FGF12, FGF12B, FHF1;
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: CALM1, CALM, CAM, CAM1, CALM2, CAM2, CAMB, CALM3, CALML2,
SOURCE 13 CAM3, CAMC, CAMIII;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 16 MOL_ID: 3;
SOURCE 17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 18 ORGANISM_COMMON: HUMAN;
SOURCE 19 ORGANISM_TAXID: 9606;
SOURCE 20 GENE: SCN5A;
SOURCE 21 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 22 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS EF HAND, ION CHANNEL, MEMBRANE, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.WANG,B.C.CHUNG,H.YAN,H.G.WANG,S.Y.LEE,G.S.PITT
REVDAT 4 28-FEB-24 4JQ0 1 REMARK SEQADV LINK
REVDAT 3 03-DEC-14 4JQ0 1 AUTHOR
REVDAT 2 22-OCT-14 4JQ0 1 JRNL
REVDAT 1 21-MAY-14 4JQ0 0
JRNL AUTH C.WANG,B.C.CHUNG,H.YAN,H.G.WANG,S.Y.LEE,G.S.PITT
JRNL TITL STRUCTURAL ANALYSES OF CA(2+)/CAM INTERACTION WITH NAV
JRNL TITL 2 CHANNEL C-TERMINI REVEAL MECHANISMS OF CALCIUM-DEPENDENT
JRNL TITL 3 REGULATION.
JRNL REF NAT COMMUN V. 5 4896 2014
JRNL REFN ESSN 2041-1723
JRNL PMID 25232683
JRNL DOI 10.1038/NCOMMS5896
REMARK 2
REMARK 2 RESOLUTION. 3.84 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8_1069)
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) : 3.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.57
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.380
REMARK 3 COMPLETENESS FOR RANGE (%) : 40.5
REMARK 3 NUMBER OF REFLECTIONS : 3700
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.257
REMARK 3 R VALUE (WORKING SET) : 0.253
REMARK 3 FREE R VALUE : 0.320
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.460
REMARK 3 FREE R VALUE TEST SET COUNT : 202
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
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) : 0.610
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.400
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 : 0.010 3013
REMARK 3 ANGLE : 0.979 4114
REMARK 3 CHIRALITY : 0.057 492
REMARK 3 PLANARITY : 0.003 545
REMARK 3 DIHEDRAL : 11.328 988
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 15
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 12 THROUGH 73 )
REMARK 3 ORIGIN FOR THE GROUP (A): -82.1254 49.3693 -49.3605
REMARK 3 T TENSOR
REMARK 3 T11: 0.9015 T22: 1.1422
REMARK 3 T33: -0.4898 T12: 0.8652
REMARK 3 T13: -0.7673 T23: 0.2737
REMARK 3 L TENSOR
REMARK 3 L11: 1.7815 L22: 1.5602
REMARK 3 L33: 0.9149 L12: -0.1871
REMARK 3 L13: 0.6324 L23: -0.8560
REMARK 3 S TENSOR
REMARK 3 S11: -0.0119 S12: -0.4698 S13: 0.1608
REMARK 3 S21: -0.0864 S22: 1.1606 S23: 0.6474
REMARK 3 S31: 0.4262 S32: -0.0411 S33: 1.8888
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 74 THROUGH 83 )
REMARK 3 ORIGIN FOR THE GROUP (A): -82.6658 54.2479 -36.9030
REMARK 3 T TENSOR
REMARK 3 T11: 1.3124 T22: 1.0310
REMARK 3 T33: 1.1368 T12: 0.7139
REMARK 3 T13: -0.4231 T23: 0.1896
REMARK 3 L TENSOR
REMARK 3 L11: 2.6824 L22: 1.0672
REMARK 3 L33: 2.7329 L12: 0.8806
REMARK 3 L13: 1.9384 L23: 0.9181
REMARK 3 S TENSOR
REMARK 3 S11: -0.1853 S12: 0.5787 S13: 0.3978
REMARK 3 S21: -0.3667 S22: -0.0534 S23: 0.4630
REMARK 3 S31: -0.2234 S32: 0.0039 S33: -0.0638
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 84 THROUGH 152 )
REMARK 3 ORIGIN FOR THE GROUP (A): -72.5814 46.1915 -42.5207
REMARK 3 T TENSOR
REMARK 3 T11: 0.8232 T22: 1.9116
REMARK 3 T33: 0.2734 T12: 1.3429
REMARK 3 T13: -0.8057 T23: 0.1211
REMARK 3 L TENSOR
REMARK 3 L11: 1.0504 L22: 1.0423
REMARK 3 L33: 1.6072 L12: -0.2746
REMARK 3 L13: 0.6197 L23: -1.1600
REMARK 3 S TENSOR
REMARK 3 S11: -0.6592 S12: -0.6211 S13: 0.5290
REMARK 3 S21: 0.6645 S22: 0.0874 S23: -0.0938
REMARK 3 S31: 0.4603 S32: 0.3266 S33: -0.8173
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 7 THROUGH 20 )
REMARK 3 ORIGIN FOR THE GROUP (A): -69.2542 21.4254 -94.6687
REMARK 3 T TENSOR
REMARK 3 T11: 1.2693 T22: 2.2449
REMARK 3 T33: 0.6307 T12: -0.2767
REMARK 3 T13: 0.8620 T23: -0.3547
REMARK 3 L TENSOR
REMARK 3 L11: 1.1292 L22: 0.4732
REMARK 3 L33: 0.2038 L12: 0.0885
REMARK 3 L13: -0.3807 L23: -0.0784
REMARK 3 S TENSOR
REMARK 3 S11: 0.1481 S12: -0.6587 S13: 0.4063
REMARK 3 S21: 0.5836 S22: -0.6104 S23: 0.4980
REMARK 3 S31: 0.5959 S32: -0.3569 S33: -0.5250
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 21 THROUGH 40 )
REMARK 3 ORIGIN FOR THE GROUP (A): -83.4934 22.6080 -89.4570
REMARK 3 T TENSOR
REMARK 3 T11: 1.2935 T22: 2.2940
REMARK 3 T33: 1.8511 T12: -0.3384
REMARK 3 T13: 0.2836 T23: 0.2299
REMARK 3 L TENSOR
REMARK 3 L11: 5.3651 L22: 1.5496
REMARK 3 L33: 0.6699 L12: -2.7225
REMARK 3 L13: 1.7760 L23: -0.9659
REMARK 3 S TENSOR
REMARK 3 S11: 0.3018 S12: -0.8103 S13: -0.5454
REMARK 3 S21: 0.3057 S22: 0.2552 S23: 0.4599
REMARK 3 S31: 0.9801 S32: -0.2492 S33: -0.1642
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 41 THROUGH 56 )
REMARK 3 ORIGIN FOR THE GROUP (A): -83.7736 31.2611 -81.0886
REMARK 3 T TENSOR
REMARK 3 T11: 1.6495 T22: 1.9397
REMARK 3 T33: 1.8447 T12: 0.2710
REMARK 3 T13: -0.0971 T23: 0.6407
REMARK 3 L TENSOR
REMARK 3 L11: 5.6747 L22: 6.2537
REMARK 3 L33: 4.7398 L12: -5.7563
REMARK 3 L13: 3.0111 L23: -1.9710
REMARK 3 S TENSOR
REMARK 3 S11: 0.3166 S12: -0.1782 S13: -0.1474
REMARK 3 S21: 0.2058 S22: 0.1128 S23: 0.0742
REMARK 3 S31: -0.4285 S32: -0.1891 S33: -0.1102
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 57 THROUGH 99 )
REMARK 3 ORIGIN FOR THE GROUP (A): -67.0094 30.9645 -80.5006
REMARK 3 T TENSOR
REMARK 3 T11: 0.3780 T22: 1.9256
REMARK 3 T33: 0.7716 T12: -0.3701
REMARK 3 T13: 0.1461 T23: -0.0470
REMARK 3 L TENSOR
REMARK 3 L11: 1.0076 L22: 1.8316
REMARK 3 L33: 0.6787 L12: -0.0326
REMARK 3 L13: 0.6670 L23: 0.5033
REMARK 3 S TENSOR
REMARK 3 S11: -0.3058 S12: -0.5617 S13: 0.2293
REMARK 3 S21: -0.8805 S22: 0.1482 S23: 0.4923
REMARK 3 S31: -0.2813 S32: -0.3906 S33: 0.1759
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 100 THROUGH 112 )
REMARK 3 ORIGIN FOR THE GROUP (A): -66.7444 23.7008 -61.3248
REMARK 3 T TENSOR
REMARK 3 T11: 1.7677 T22: 0.9542
REMARK 3 T33: 1.4163 T12: 0.0318
REMARK 3 T13: -0.6829 T23: -0.0270
REMARK 3 L TENSOR
REMARK 3 L11: 4.8732 L22: 3.1550
REMARK 3 L33: 4.5254 L12: 0.2349
REMARK 3 L13: -4.4013 L23: -0.2278
REMARK 3 S TENSOR
REMARK 3 S11: -0.2994 S12: -0.5096 S13: -0.6292
REMARK 3 S21: 0.1193 S22: 0.3764 S23: 1.6229
REMARK 3 S31: -0.3036 S32: -1.7201 S33: -0.1066
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 113 THROUGH 118 )
REMARK 3 ORIGIN FOR THE GROUP (A): -73.0602 29.5012 -67.7038
REMARK 3 T TENSOR
REMARK 3 T11: 0.8573 T22: 1.5249
REMARK 3 T33: 0.9056 T12: 0.2263
REMARK 3 T13: 0.3285 T23: 0.2967
REMARK 3 L TENSOR
REMARK 3 L11: 8.8533 L22: 6.1883
REMARK 3 L33: 6.1785 L12: 5.0199
REMARK 3 L13: 4.8007 L23: -0.7344
REMARK 3 S TENSOR
REMARK 3 S11: -0.1220 S12: 0.7870 S13: -1.1016
REMARK 3 S21: -0.6944 S22: 0.1005 S23: 0.1156
REMARK 3 S31: 1.2786 S32: -0.1751 S33: -0.0722
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 119 THROUGH 148 )
REMARK 3 ORIGIN FOR THE GROUP (A): -62.4517 17.5082 -68.7826
REMARK 3 T TENSOR
REMARK 3 T11: 0.9685 T22: 2.2590
REMARK 3 T33: 1.5205 T12: 0.5163
REMARK 3 T13: -0.0608 T23: -0.3452
REMARK 3 L TENSOR
REMARK 3 L11: 2.6953 L22: 4.3430
REMARK 3 L33: 5.7471 L12: 0.3834
REMARK 3 L13: -2.7933 L23: -1.8599
REMARK 3 S TENSOR
REMARK 3 S11: 0.0849 S12: -0.2300 S13: -0.7240
REMARK 3 S21: -0.3795 S22: 0.3878 S23: 0.2280
REMARK 3 S31: 0.5016 S32: 0.5864 S33: -0.0492
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1786 THROUGH 1807 )
REMARK 3 ORIGIN FOR THE GROUP (A): -47.9341 58.3729 -59.3790
REMARK 3 T TENSOR
REMARK 3 T11: 0.6021 T22: 2.1490
REMARK 3 T33: 1.7035 T12: -0.2660
REMARK 3 T13: -0.5308 T23: 0.3401
REMARK 3 L TENSOR
REMARK 3 L11: 0.1307 L22: 0.0141
REMARK 3 L33: 6.5614 L12: 0.0434
REMARK 3 L13: 0.6490 L23: 0.2105
REMARK 3 S TENSOR
REMARK 3 S11: -0.2708 S12: 0.8743 S13: 0.6456
REMARK 3 S21: -0.3487 S22: -0.0829 S23: -0.2730
REMARK 3 S31: -0.7736 S32: 0.1787 S33: 0.3896
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1808 THROUGH 1837 )
REMARK 3 ORIGIN FOR THE GROUP (A): -51.1261 45.7228 -61.8851
REMARK 3 T TENSOR
REMARK 3 T11: 0.3056 T22: 1.8032
REMARK 3 T33: 0.5885 T12: -0.2069
REMARK 3 T13: -0.3139 T23: 0.2273
REMARK 3 L TENSOR
REMARK 3 L11: 0.9650 L22: 2.5621
REMARK 3 L33: 1.2033 L12: 0.3302
REMARK 3 L13: 1.0749 L23: 0.2128
REMARK 3 S TENSOR
REMARK 3 S11: -0.3829 S12: 0.3038 S13: 0.7275
REMARK 3 S21: -0.0894 S22: -0.4936 S23: -0.3204
REMARK 3 S31: -0.1797 S32: -0.0896 S33: -0.7645
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1838 THROUGH 1862 )
REMARK 3 ORIGIN FOR THE GROUP (A): -57.8355 49.5958 -55.3423
REMARK 3 T TENSOR
REMARK 3 T11: 0.7464 T22: 1.7208
REMARK 3 T33: 1.5191 T12: 0.7162
REMARK 3 T13: -0.7225 T23: -0.1353
REMARK 3 L TENSOR
REMARK 3 L11: 0.3612 L22: 5.4989
REMARK 3 L33: 2.0755 L12: 0.6362
REMARK 3 L13: -0.5457 L23: -1.4027
REMARK 3 S TENSOR
REMARK 3 S11: -0.0264 S12: 0.6399 S13: -0.2014
REMARK 3 S21: 0.0795 S22: 0.2256 S23: -0.1388
REMARK 3 S31: 0.2100 S32: -0.0445 S33: -0.0059
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1863 THROUGH 1895 )
REMARK 3 ORIGIN FOR THE GROUP (A): -57.9906 57.0410 -48.4484
REMARK 3 T TENSOR
REMARK 3 T11: 1.9181 T22: 1.8697
REMARK 3 T33: 1.1848 T12: 0.4130
REMARK 3 T13: 0.0061 T23: 0.0569
REMARK 3 L TENSOR
REMARK 3 L11: 0.8469 L22: 0.2997
REMARK 3 L33: 0.3403 L12: 0.5204
REMARK 3 L13: 0.4381 L23: 0.3246
REMARK 3 S TENSOR
REMARK 3 S11: -0.5224 S12: -0.6355 S13: 1.1584
REMARK 3 S21: 1.0686 S22: 0.0798 S23: 0.1450
REMARK 3 S31: -1.3251 S32: 0.2896 S33: -0.0307
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1896 THROUGH 1927 )
REMARK 3 ORIGIN FOR THE GROUP (A): -66.7287 27.1125 -75.8013
REMARK 3 T TENSOR
REMARK 3 T11: 1.0212 T22: 0.5125
REMARK 3 T33: 1.5984 T12: -0.2552
REMARK 3 T13: 0.1643 T23: -0.3587
REMARK 3 L TENSOR
REMARK 3 L11: 0.0327 L22: 0.2046
REMARK 3 L33: 0.1292 L12: -0.0746
REMARK 3 L13: -0.0204 L23: 0.0210
REMARK 3 S TENSOR
REMARK 3 S11: 0.0963 S12: 0.3215 S13: -0.7308
REMARK 3 S21: -0.8567 S22: 0.1725 S23: 0.4267
REMARK 3 S31: 0.3382 S32: 0.0743 S33: -0.1296
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE DIFFRACTION DATA IS HEAVILY
REMARK 3 ANISOTROPIC (3.8/5.4/6.0 A). AFTER ANISOTROPIC SCALING, THE
REMARK 3 MODEL REFINES MUCH BETTER WITH INCLUSION OF HIGH-RESOLUTION
REMARK 3 REFLECTIONS RATHER THAN CUTTING THE DATA TO THE LOW RESOLUTION.
REMARK 3 (6.0 A). ANISOTROPY ALSO GIVES RISE TO THE LOW DATA COMPLETENESS.
REMARK 4
REMARK 4 4JQ0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAR-13.
REMARK 100 THE DEPOSITION ID IS D_1000078358.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-AUG-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 22-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL - LIQUID NITROGEN
REMARK 200 COOLED
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 3705
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.830
REMARK 200 RESOLUTION RANGE LOW (A) : 46.068
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 40.6
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.87
REMARK 200 COMPLETENESS FOR SHELL (%) : 13.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX (AUTOMR: 1.8_1069)
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 64.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.48
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.18 M MGSO4, 0.1 M
REMARK 280 SODIUM IODIDE, AND CACL2, PH 7.5, EVAPORATION, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+2/3
REMARK 290 6555 -X,-X+Y,-Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 40.03667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 80.07333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 80.07333
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 40.03667
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: 3610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -73.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D
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 -56
REMARK 465 ALA A -55
REMARK 465 ALA A -54
REMARK 465 ALA A -53
REMARK 465 ILE A -52
REMARK 465 ALA A -51
REMARK 465 SER A -50
REMARK 465 SER A -49
REMARK 465 LEU A -48
REMARK 465 ILE A -47
REMARK 465 ARG A -46
REMARK 465 GLN A -45
REMARK 465 LYS A -44
REMARK 465 ARG A -43
REMARK 465 GLN A -42
REMARK 465 ALA A -41
REMARK 465 ARG A -40
REMARK 465 GLU A -39
REMARK 465 SER A -38
REMARK 465 ASN A -37
REMARK 465 SER A -36
REMARK 465 ASP A -35
REMARK 465 ARG A -34
REMARK 465 VAL A -33
REMARK 465 SER A -32
REMARK 465 ALA A -31
REMARK 465 SER A -30
REMARK 465 LYS A -29
REMARK 465 ARG A -28
REMARK 465 ARG A -27
REMARK 465 SER A -26
REMARK 465 SER A -25
REMARK 465 PRO A -24
REMARK 465 SER A -23
REMARK 465 LYS A -22
REMARK 465 ASP A -21
REMARK 465 GLY A -20
REMARK 465 ARG A -19
REMARK 465 SER A -18
REMARK 465 LEU A -17
REMARK 465 CYS A -16
REMARK 465 GLU A -15
REMARK 465 ARG A -14
REMARK 465 HIS A -13
REMARK 465 VAL A -12
REMARK 465 LEU A -11
REMARK 465 GLY A -10
REMARK 465 VAL A -9
REMARK 465 PHE A -8
REMARK 465 SER A -7
REMARK 465 LYS A -6
REMARK 465 VAL A -5
REMARK 465 ARG A -4
REMARK 465 PHE A -3
REMARK 465 CYS A -2
REMARK 465 SER A -1
REMARK 465 GLY A 0
REMARK 465 ARG A 1
REMARK 465 LYS A 2
REMARK 465 ARG A 3
REMARK 465 PRO A 4
REMARK 465 VAL A 5
REMARK 465 ARG A 6
REMARK 465 ARG A 7
REMARK 465 ARG A 8
REMARK 465 PRO A 9
REMARK 465 GLU A 10
REMARK 465 PRO A 11
REMARK 465 GLU A 153
REMARK 465 PRO A 154
REMARK 465 SER A 155
REMARK 465 LEU A 156
REMARK 465 HIS A 157
REMARK 465 GLU A 158
REMARK 465 ILE A 159
REMARK 465 GLY A 160
REMARK 465 GLU A 161
REMARK 465 LYS A 162
REMARK 465 GLN A 163
REMARK 465 GLY A 164
REMARK 465 ARG A 165
REMARK 465 SER A 166
REMARK 465 ARG A 167
REMARK 465 LYS A 168
REMARK 465 SER A 169
REMARK 465 SER A 170
REMARK 465 GLY A 171
REMARK 465 THR A 172
REMARK 465 PRO A 173
REMARK 465 THR A 174
REMARK 465 MET A 175
REMARK 465 ASN A 176
REMARK 465 GLY A 177
REMARK 465 GLY A 178
REMARK 465 LYS A 179
REMARK 465 VAL A 180
REMARK 465 VAL A 181
REMARK 465 ASN A 182
REMARK 465 GLN A 183
REMARK 465 ASP A 184
REMARK 465 SER A 185
REMARK 465 THR A 186
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 ASP C 3
REMARK 465 GLN C 4
REMARK 465 LEU C 5
REMARK 465 THR C 6
REMARK 465 LYS C 149
REMARK 465 MET D 1750
REMARK 465 GLY D 1751
REMARK 465 SER D 1752
REMARK 465 SER D 1753
REMARK 465 HIS D 1754
REMARK 465 HIS D 1755
REMARK 465 HIS D 1756
REMARK 465 HIS D 1757
REMARK 465 HIS D 1758
REMARK 465 HIS D 1759
REMARK 465 SER D 1760
REMARK 465 SER D 1761
REMARK 465 GLY D 1762
REMARK 465 LEU D 1763
REMARK 465 VAL D 1764
REMARK 465 PRO D 1765
REMARK 465 ARG D 1766
REMARK 465 GLY D 1767
REMARK 465 SER D 1768
REMARK 465 HIS D 1769
REMARK 465 MET D 1770
REMARK 465 ALA D 1771
REMARK 465 SER D 1772
REMARK 465 GLU D 1773
REMARK 465 ASN D 1774
REMARK 465 PHE D 1775
REMARK 465 SER D 1776
REMARK 465 VAL D 1777
REMARK 465 ALA D 1778
REMARK 465 THR D 1779
REMARK 465 GLU D 1780
REMARK 465 GLU D 1781
REMARK 465 SER D 1782
REMARK 465 THR D 1783
REMARK 465 GLU D 1784
REMARK 465 PRO D 1785
REMARK 465 PHE D 1928
REMARK 465 ARG D 1929
REMARK 465 GLN D 1930
REMARK 465 GLN D 1931
REMARK 465 ALA D 1932
REMARK 465 GLY D 1933
REMARK 465 SER D 1934
REMARK 465 GLY D 1935
REMARK 465 LEU D 1936
REMARK 465 SER D 1937
REMARK 465 GLU D 1938
REMARK 465 GLU D 1939
REMARK 465 ASP D 1940
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 LYS A 14 CG CD CE NZ
REMARK 470 GLN A 29 CG CD OE1 NE2
REMARK 470 TYR A 46 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU A 56 CG CD1 CD2
REMARK 470 ARG A 57 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 65 CG CD CE NZ
REMARK 470 TYR A 69 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 75 CG CD OE1 OE2
REMARK 470 TYR A 77 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS A 89 CG CD CE NZ
REMARK 470 LYS A 91 CG CD CE NZ
REMARK 470 TYR A 102 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU A 111 CG CD OE1 OE2
REMARK 470 LYS A 122 CG CD CE NZ
REMARK 470 LYS A 128 CG CD CE NZ
REMARK 470 ARG A 131 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 133 CG CD CE NZ
REMARK 470 SER A 138 OG
REMARK 470 SER A 139 OG
REMARK 470 ILE A 146 CG1 CG2 CD1
REMARK 470 GLU A 147 CG CD OE1 OE2
REMARK 470 MET A 150 CG SD CE
REMARK 470 ARG A 152 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 8 CG CD OE1 OE2
REMARK 470 GLU C 12 CG CD OE1 OE2
REMARK 470 PHE C 13 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS C 14 CG CD CE NZ
REMARK 470 GLU C 15 CG CD OE1 OE2
REMARK 470 PHE C 17 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS C 22 CG CD CE NZ
REMARK 470 THR C 27 OG1 CG2
REMARK 470 THR C 29 OG1 CG2
REMARK 470 LYS C 31 CG CD CE NZ
REMARK 470 ARG C 38 CG CD NE CZ NH1 NH2
REMARK 470 ASN C 43 CG OD1 ND2
REMARK 470 GLU C 46 CG CD OE1 OE2
REMARK 470 GLN C 50 CG CD OE1 NE2
REMARK 470 ASP C 51 CG OD1 OD2
REMARK 470 GLU C 55 CG CD OE1 OE2
REMARK 470 THR C 63 OG1 CG2
REMARK 470 PHE C 69 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 MET C 72 CG SD CE
REMARK 470 ARG C 75 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 76 CG CD CE NZ
REMARK 470 LYS C 78 CG CD CE NZ
REMARK 470 THR C 80 OG1 CG2
REMARK 470 ASP C 81 CG OD1 OD2
REMARK 470 GLU C 83 CG CD OE1 OE2
REMARK 470 GLU C 84 CG CD OE1 OE2
REMARK 470 GLU C 85 CG CD OE1 OE2
REMARK 470 ARG C 87 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 91 CG CD NE CZ NH1 NH2
REMARK 470 PHE C 93 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 TYR C 100 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 SER C 102 OG
REMARK 470 GLU C 105 CG CD OE1 OE2
REMARK 470 ARG C 107 CG CD NE CZ NH1 NH2
REMARK 470 LEU C 113 CG CD1 CD2
REMARK 470 GLU C 115 CG CD OE1 OE2
REMARK 470 LYS C 116 CG CD CE NZ
REMARK 470 ASP C 119 CG OD1 OD2
REMARK 470 GLU C 120 CG CD OE1 OE2
REMARK 470 GLU C 121 CG CD OE1 OE2
REMARK 470 ASP C 123 CG OD1 OD2
REMARK 470 GLU C 124 CG CD OE1 OE2
REMARK 470 ARG C 127 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 128 CG CD OE1 OE2
REMARK 470 GLN C 136 CG CD OE1 NE2
REMARK 470 TYR C 139 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU C 140 CG CD OE1 OE2
REMARK 470 GLU C 141 CG CD OE1 OE2
REMARK 470 PHE C 142 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN C 144 CG CD OE1 NE2
REMARK 470 THR C 147 OG1 CG2
REMARK 470 TYR D1795 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLU D1799 CG CD OE1 OE2
REMARK 470 THR D1806 OG1 CG2
REMARK 470 MET D1851 CG SD CE
REMARK 470 LEU D1854 CG CD1 CD2
REMARK 470 PHE D1855 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS D1859 CG CD CE NZ
REMARK 470 ARG D1860 CG CD NE CZ NH1 NH2
REMARK 470 GLU D1867 CG CD OE1 OE2
REMARK 470 LYS D1872 CG CD CE NZ
REMARK 470 GLN D1874 CG CD OE1 NE2
REMARK 470 GLU D1877 CG CD OE1 OE2
REMARK 470 LYS D1878 CG CD CE NZ
REMARK 470 LEU D1896 CG CD1 CD2
REMARK 470 ARG D1897 CG CD NE CZ NH1 NH2
REMARK 470 ARG D1898 CG CD NE CZ NH1 NH2
REMARK 470 LYS D1899 CG CD CE NZ
REMARK 470 GLU D1901 CG CD OE1 OE2
REMARK 470 GLU D1902 CG CD OE1 OE2
REMARK 470 SER D1904 OG
REMARK 470 MET D1906 CG SD CE
REMARK 470 GLN D1909 CG CD OE1 NE2
REMARK 470 ARG D1910 CG CD NE CZ NH1 NH2
REMARK 470 PHE D1912 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG D1913 CG CD NE CZ NH1 NH2
REMARK 470 ARG D1914 CG CD NE CZ NH1 NH2
REMARK 470 LEU D1916 CG CD1 CD2
REMARK 470 LEU D1917 CG CD1 CD2
REMARK 470 GLN D1918 CG CD OE1 NE2
REMARK 470 ARG D1919 CG CD NE CZ NH1 NH2
REMARK 470 LYS D1922 CG CD CE NZ
REMARK 470 HIS D1923 CG ND1 CD2 CE1 NE2
REMARK 470 PHE D1926 CG CD1 CD2 CE1 CE2 CZ
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 PRO A 32 -36.60 -37.25
REMARK 500 PRO A 53 85.44 -68.16
REMARK 500 ASN A 73 -129.24 -72.43
REMARK 500 TYR A 98 -22.80 -147.03
REMARK 500 GLN A 109 88.16 -67.00
REMARK 500 GLN A 110 -19.97 -44.66
REMARK 500 THR C 80 -60.01 -101.48
REMARK 500 GLU C 84 -5.33 78.40
REMARK 500 GLU C 85 46.54 -102.57
REMARK 500 ASP D1839 95.79 -62.02
REMARK 500 SER D1885 -177.43 63.53
REMARK 500 LEU D1896 -109.85 10.02
REMARK 500 ARG D1897 -61.51 -8.90
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 C 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 21 OD1
REMARK 620 2 ASP C 23 OD1 55.4
REMARK 620 3 ASP C 25 OD1 59.8 69.3
REMARK 620 4 THR C 27 O 96.7 138.6 70.0
REMARK 620 5 GLU C 32 OE2 128.6 100.4 160.8 120.8
REMARK 620 6 GLU C 32 OE1 127.2 148.2 142.1 72.2 51.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 59 OD2
REMARK 620 2 ASN C 61 OD1 122.7
REMARK 620 3 THR C 63 O 168.2 59.4
REMARK 620 4 GLU C 68 OE1 107.8 123.4 66.1
REMARK 620 5 GLU C 68 OE2 70.5 131.9 99.4 44.9
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 203 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 94 OD1
REMARK 620 2 ASP C 96 OD1 80.8
REMARK 620 3 ASN C 98 OD1 68.1 68.4
REMARK 620 4 TYR C 100 O 77.8 127.1 58.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 204 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 130 OD1
REMARK 620 2 ASP C 132 OD1 103.5
REMARK 620 3 ASP C 134 OD1 110.9 87.3
REMARK 620 4 GLN C 136 O 97.5 158.8 87.3
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 204
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4JPZ RELATED DB: PDB
DBREF 4JQ0 A -56 186 UNP P61328 FGF12_HUMAN 1 243
DBREF 4JQ0 C 1 149 UNP P62158 CALM_HUMAN 1 149
DBREF 4JQ0 D 1773 1940 UNP Q14524 SCN5A_HUMAN 1773 1940
SEQADV 4JQ0 MET D 1750 UNP Q14524 EXPRESSION TAG
SEQADV 4JQ0 GLY D 1751 UNP Q14524 EXPRESSION TAG
SEQADV 4JQ0 SER D 1752 UNP Q14524 EXPRESSION TAG
SEQADV 4JQ0 SER D 1753 UNP Q14524 EXPRESSION TAG
SEQADV 4JQ0 HIS D 1754 UNP Q14524 EXPRESSION TAG
SEQADV 4JQ0 HIS D 1755 UNP Q14524 EXPRESSION TAG
SEQADV 4JQ0 HIS D 1756 UNP Q14524 EXPRESSION TAG
SEQADV 4JQ0 HIS D 1757 UNP Q14524 EXPRESSION TAG
SEQADV 4JQ0 HIS D 1758 UNP Q14524 EXPRESSION TAG
SEQADV 4JQ0 HIS D 1759 UNP Q14524 EXPRESSION TAG
SEQADV 4JQ0 SER D 1760 UNP Q14524 EXPRESSION TAG
SEQADV 4JQ0 SER D 1761 UNP Q14524 EXPRESSION TAG
SEQADV 4JQ0 GLY D 1762 UNP Q14524 EXPRESSION TAG
SEQADV 4JQ0 LEU D 1763 UNP Q14524 EXPRESSION TAG
SEQADV 4JQ0 VAL D 1764 UNP Q14524 EXPRESSION TAG
SEQADV 4JQ0 PRO D 1765 UNP Q14524 EXPRESSION TAG
SEQADV 4JQ0 ARG D 1766 UNP Q14524 EXPRESSION TAG
SEQADV 4JQ0 GLY D 1767 UNP Q14524 EXPRESSION TAG
SEQADV 4JQ0 SER D 1768 UNP Q14524 EXPRESSION TAG
SEQADV 4JQ0 HIS D 1769 UNP Q14524 EXPRESSION TAG
SEQADV 4JQ0 MET D 1770 UNP Q14524 EXPRESSION TAG
SEQADV 4JQ0 ALA D 1771 UNP Q14524 EXPRESSION TAG
SEQADV 4JQ0 SER D 1772 UNP Q14524 EXPRESSION TAG
SEQRES 1 A 243 MET ALA ALA ALA ILE ALA SER SER LEU ILE ARG GLN LYS
SEQRES 2 A 243 ARG GLN ALA ARG GLU SER ASN SER ASP ARG VAL SER ALA
SEQRES 3 A 243 SER LYS ARG ARG SER SER PRO SER LYS ASP GLY ARG SER
SEQRES 4 A 243 LEU CYS GLU ARG HIS VAL LEU GLY VAL PHE SER LYS VAL
SEQRES 5 A 243 ARG PHE CYS SER GLY ARG LYS ARG PRO VAL ARG ARG ARG
SEQRES 6 A 243 PRO GLU PRO GLN LEU LYS GLY ILE VAL THR ARG LEU PHE
SEQRES 7 A 243 SER GLN GLN GLY TYR PHE LEU GLN MET HIS PRO ASP GLY
SEQRES 8 A 243 THR ILE ASP GLY THR LYS ASP GLU ASN SER ASP TYR THR
SEQRES 9 A 243 LEU PHE ASN LEU ILE PRO VAL GLY LEU ARG VAL VAL ALA
SEQRES 10 A 243 ILE GLN GLY VAL LYS ALA SER LEU TYR VAL ALA MET ASN
SEQRES 11 A 243 GLY GLU GLY TYR LEU TYR SER SER ASP VAL PHE THR PRO
SEQRES 12 A 243 GLU CYS LYS PHE LYS GLU SER VAL PHE GLU ASN TYR TYR
SEQRES 13 A 243 VAL ILE TYR SER SER THR LEU TYR ARG GLN GLN GLU SER
SEQRES 14 A 243 GLY ARG ALA TRP PHE LEU GLY LEU ASN LYS GLU GLY GLN
SEQRES 15 A 243 ILE MET LYS GLY ASN ARG VAL LYS LYS THR LYS PRO SER
SEQRES 16 A 243 SER HIS PHE VAL PRO LYS PRO ILE GLU VAL CYS MET TYR
SEQRES 17 A 243 ARG GLU PRO SER LEU HIS GLU ILE GLY GLU LYS GLN GLY
SEQRES 18 A 243 ARG SER ARG LYS SER SER GLY THR PRO THR MET ASN GLY
SEQRES 19 A 243 GLY LYS VAL VAL ASN GLN ASP SER THR
SEQRES 1 C 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 C 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 C 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 C 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 C 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 C 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 C 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 C 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 C 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 C 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 C 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 C 149 GLN MET MET THR ALA LYS
SEQRES 1 D 191 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 191 LEU VAL PRO ARG GLY SER HIS MET ALA SER GLU ASN PHE
SEQRES 3 D 191 SER VAL ALA THR GLU GLU SER THR GLU PRO LEU SER GLU
SEQRES 4 D 191 ASP ASP PHE ASP MET PHE TYR GLU ILE TRP GLU LYS PHE
SEQRES 5 D 191 ASP PRO GLU ALA THR GLN PHE ILE GLU TYR SER VAL LEU
SEQRES 6 D 191 SER ASP PHE ALA ASP ALA LEU SER GLU PRO LEU ARG ILE
SEQRES 7 D 191 ALA LYS PRO ASN GLN ILE SER LEU ILE ASN MET ASP LEU
SEQRES 8 D 191 PRO MET VAL SER GLY ASP ARG ILE HIS CYS MET ASP ILE
SEQRES 9 D 191 LEU PHE ALA PHE THR LYS ARG VAL LEU GLY GLU SER GLY
SEQRES 10 D 191 GLU MET ASP ALA LEU LYS ILE GLN MET GLU GLU LYS PHE
SEQRES 11 D 191 MET ALA ALA ASN PRO SER LYS ILE SER TYR GLU PRO ILE
SEQRES 12 D 191 THR THR THR LEU ARG ARG LYS HIS GLU GLU VAL SER ALA
SEQRES 13 D 191 MET VAL ILE GLN ARG ALA PHE ARG ARG HIS LEU LEU GLN
SEQRES 14 D 191 ARG SER LEU LYS HIS ALA SER PHE LEU PHE ARG GLN GLN
SEQRES 15 D 191 ALA GLY SER GLY LEU SER GLU GLU ASP
HET CA C 201 1
HET CA C 202 1
HET CA C 203 1
HET CA C 204 1
HETNAM CA CALCIUM ION
FORMUL 4 CA 4(CA 2+)
HELIX 1 1 SER A 44 TYR A 46 5 3
HELIX 2 2 THR A 85 CYS A 88 5 4
HELIX 3 3 LYS A 128 VAL A 132 5 5
HELIX 4 4 GLU C 8 ASP C 21 1 14
HELIX 5 5 THR C 29 LEU C 40 1 12
HELIX 6 6 THR C 45 GLU C 55 1 11
HELIX 7 7 ASP C 65 LYS C 78 1 14
HELIX 8 8 ILE C 86 ASP C 94 1 9
HELIX 9 9 ALA C 103 LEU C 113 1 11
HELIX 10 10 THR C 118 ASP C 130 1 13
HELIX 11 11 TYR C 139 THR C 147 1 9
HELIX 12 12 SER D 1787 ASP D 1802 1 16
HELIX 13 13 TYR D 1811 LEU D 1821 1 11
HELIX 14 14 ASN D 1831 MET D 1838 1 8
HELIX 15 15 CYS D 1850 GLY D 1863 1 14
HELIX 16 16 GLY D 1866 ASN D 1883 1 18
HELIX 17 17 LEU D 1896 PHE D 1926 1 31
LINK OD1 ASP C 21 CA CA C 202 1555 1555 3.05
LINK OD1 ASP C 23 CA CA C 202 1555 1555 2.66
LINK OD1 ASP C 25 CA CA C 202 1555 1555 2.48
LINK O THR C 27 CA CA C 202 1555 1555 2.45
LINK OE2 GLU C 32 CA CA C 202 1555 1555 2.37
LINK OE1 GLU C 32 CA CA C 202 1555 1555 2.65
LINK OD2 ASP C 59 CA CA C 201 1555 1555 2.64
LINK OD1 ASN C 61 CA CA C 201 1555 1555 2.40
LINK O THR C 63 CA CA C 201 1555 1555 2.93
LINK OE1 GLU C 68 CA CA C 201 1555 1555 2.49
LINK OE2 GLU C 68 CA CA C 201 1555 1555 3.07
LINK OD1 ASP C 94 CA CA C 203 1555 1555 2.56
LINK OD1 ASP C 96 CA CA C 203 1555 1555 2.44
LINK OD1 ASN C 98 CA CA C 203 1555 1555 3.13
LINK O TYR C 100 CA CA C 203 1555 1555 2.37
LINK OD1 ASP C 130 CA CA C 204 1555 1555 1.93
LINK OD1 ASP C 132 CA CA C 204 1555 1555 2.13
LINK OD1 ASP C 134 CA CA C 204 1555 1555 1.97
LINK O GLN C 136 CA CA C 204 1555 1555 2.27
CISPEP 1 GLU D 1823 PRO D 1824 0 0.94
CISPEP 2 LYS D 1829 PRO D 1830 0 -0.08
CISPEP 3 SER D 1844 GLY D 1845 0 -0.41
CISPEP 4 SER D 1865 GLY D 1866 0 1.29
CISPEP 5 PHE D 1926 LEU D 1927 0 -1.97
SITE 1 AC1 4 ASP C 59 ASN C 61 THR C 63 GLU C 68
SITE 1 AC2 5 ASP C 21 ASP C 23 ASP C 25 THR C 27
SITE 2 AC2 5 GLU C 32
SITE 1 AC3 4 ASP C 94 ASP C 96 ASN C 98 TYR C 100
SITE 1 AC4 4 ASP C 130 ASP C 132 ASP C 134 GLN C 136
CRYST1 115.200 115.200 120.110 90.00 90.00 120.00 P 31 2 1 6
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 0.008681 0.005012 0.000000 0.00000
SCALE2 0.000000 0.010023 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008326 0.00000
(ATOM LINES ARE NOT SHOWN.)
END