HEADER TRANSPORT PROTEIN/CALCIUM BINDING 17-FEB-13 4J9Z
TITLE CALCIUM-CALMODULIN COMPLEXED WITH THE CALMODULIN BINDING DOMAIN FROM A
TITLE 2 SMALL CONDUCTANCE POTASSIUM CHANNEL SPLICE VARIANT AND NS309
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SMALL CONDUCTANCE CALCIUM-ACTIVATED POTASSIUM CHANNEL
COMPND 3 PROTEIN 2;
COMPND 4 CHAIN: B;
COMPND 5 FRAGMENT: CALMODULIN BINDING DOMAIN (UNP RESIDUES 396-487);
COMPND 6 SYNONYM: SK2A, SK2, SKCA 2, SKCA2, KCA2.2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: CALMODULIN;
COMPND 10 CHAIN: R;
COMPND 11 SYNONYM: CAM;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: KCNN2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 10 ORGANISM_COMMON: RAT;
SOURCE 11 ORGANISM_TAXID: 10116;
SOURCE 12 GENE: CALM1, CALM, CAM, CAM1, CALM2, CAM2, CAMB, CALM3, CAM3, CAMC;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CALCIUM BINDING, EF HAND, SK2A CHANNEL FRAGMENT, TRANSPORT PROTEIN-
KEYWDS 2 CALCIUM BINDING COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.ZHANG,J.M.PASCAL,J.-F.ZHANG
REVDAT 3 28-FEB-24 4J9Z 1 REMARK SEQADV LINK
REVDAT 2 03-APR-13 4J9Z 1 JRNL
REVDAT 1 27-MAR-13 4J9Z 0
JRNL AUTH M.ZHANG,J.M.PASCAL,J.F.ZHANG
JRNL TITL UNSTRUCTURED TO STRUCTURED TRANSITION OF AN INTRINSICALLY
JRNL TITL 2 DISORDERED PROTEIN PEPTIDE IN COUPLING CA2+-SENSING AND SK
JRNL TITL 3 CHANNEL ACTIVATION.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 110 4828 2013
JRNL REFN ISSN 0027-8424
JRNL PMID 23487779
JRNL DOI 10.1073/PNAS.1220253110
REMARK 2
REMARK 2 RESOLUTION. 1.66 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.1_1168
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) : 1.66
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.79
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 38789
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.221
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910
REMARK 3 FREE R VALUE TEST SET COUNT : 1905
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 27.7935 - 3.9972 0.98 2655 146 0.1865 0.1837
REMARK 3 2 3.9972 - 3.1741 1.00 2657 142 0.1659 0.2240
REMARK 3 3 3.1741 - 2.7733 1.00 2682 118 0.1901 0.2052
REMARK 3 4 2.7733 - 2.5199 1.00 2646 131 0.1949 0.2441
REMARK 3 5 2.5199 - 2.3394 1.00 2626 139 0.1945 0.2291
REMARK 3 6 2.3394 - 2.2015 1.00 2640 152 0.1834 0.2111
REMARK 3 7 2.2015 - 2.0913 1.00 2624 129 0.1837 0.2165
REMARK 3 8 2.0913 - 2.0003 1.00 2661 121 0.1998 0.2098
REMARK 3 9 2.0003 - 1.9233 1.00 2590 148 0.2003 0.2743
REMARK 3 10 1.9233 - 1.8570 1.00 2620 142 0.2112 0.2364
REMARK 3 11 1.8570 - 1.7989 1.00 2622 123 0.2208 0.2414
REMARK 3 12 1.7989 - 1.7475 0.99 2627 126 0.2380 0.3178
REMARK 3 13 1.7475 - 1.7015 0.99 2619 132 0.2501 0.3143
REMARK 3 14 1.7015 - 1.6600 1.00 2615 156 0.2576 0.3110
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) : 23.480
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.77
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 : 0.007 2177
REMARK 3 ANGLE : 1.161 2937
REMARK 3 CHIRALITY : 0.079 324
REMARK 3 PLANARITY : 0.005 381
REMARK 3 DIHEDRAL : 14.937 855
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 395 THROUGH 404 )
REMARK 3 ORIGIN FOR THE GROUP (A): 26.1290 64.7622 47.4856
REMARK 3 T TENSOR
REMARK 3 T11: 0.3509 T22: 0.3661
REMARK 3 T33: 0.3277 T12: 0.1114
REMARK 3 T13: -0.0558 T23: -0.0982
REMARK 3 L TENSOR
REMARK 3 L11: 0.0182 L22: 0.0361
REMARK 3 L33: 0.0209 L12: 0.0046
REMARK 3 L13: 0.0032 L23: -0.0299
REMARK 3 S TENSOR
REMARK 3 S11: -0.1982 S12: -0.2155 S13: 0.1914
REMARK 3 S21: 0.2696 S22: 0.0544 S23: -0.3253
REMARK 3 S31: -0.2589 S32: -0.1802 S33: -0.0002
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 405 THROUGH 413 )
REMARK 3 ORIGIN FOR THE GROUP (A): 44.4823 58.0342 42.5116
REMARK 3 T TENSOR
REMARK 3 T11: 0.3801 T22: 0.4412
REMARK 3 T33: 0.3261 T12: -0.1483
REMARK 3 T13: 0.0276 T23: 0.0754
REMARK 3 L TENSOR
REMARK 3 L11: 0.0149 L22: 0.0013
REMARK 3 L33: 0.0029 L12: 0.0054
REMARK 3 L13: -0.0067 L23: -0.0027
REMARK 3 S TENSOR
REMARK 3 S11: -0.0414 S12: -0.0319 S13: -0.0515
REMARK 3 S21: -0.0156 S22: 0.0670 S23: -0.1013
REMARK 3 S31: 0.0425 S32: 0.1628 S33: 0.0007
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 414 THROUGH 445 )
REMARK 3 ORIGIN FOR THE GROUP (A): 59.7330 59.0234 24.0015
REMARK 3 T TENSOR
REMARK 3 T11: 0.2393 T22: 0.2872
REMARK 3 T33: 0.2842 T12: -0.0540
REMARK 3 T13: 0.0223 T23: -0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 0.6474 L22: 0.3949
REMARK 3 L33: 0.4072 L12: 0.0993
REMARK 3 L13: -0.0377 L23: 0.0701
REMARK 3 S TENSOR
REMARK 3 S11: -0.2016 S12: 0.2406 S13: -0.6041
REMARK 3 S21: -0.0710 S22: 0.1155 S23: -0.2230
REMARK 3 S31: 0.3692 S32: 0.0783 S33: 0.0164
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 446 THROUGH 491 )
REMARK 3 ORIGIN FOR THE GROUP (A): 41.6892 55.9922 33.5308
REMARK 3 T TENSOR
REMARK 3 T11: 0.2147 T22: 0.1933
REMARK 3 T33: 0.2059 T12: 0.0095
REMARK 3 T13: -0.0140 T23: -0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 0.8305 L22: 0.1712
REMARK 3 L33: 0.3330 L12: 0.1021
REMARK 3 L13: 0.4467 L23: -0.0738
REMARK 3 S TENSOR
REMARK 3 S11: -0.2207 S12: 0.1743 S13: -0.0852
REMARK 3 S21: 0.0246 S22: 0.0892 S23: -0.0638
REMARK 3 S31: -0.0598 S32: -0.2104 S33: -0.0484
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'R' AND (RESID 2 THROUGH 28 )
REMARK 3 ORIGIN FOR THE GROUP (A): 28.8458 50.9149 59.3906
REMARK 3 T TENSOR
REMARK 3 T11: 0.7916 T22: 0.6280
REMARK 3 T33: -0.0013 T12: 0.3695
REMARK 3 T13: 0.0539 T23: 0.0798
REMARK 3 L TENSOR
REMARK 3 L11: 0.4372 L22: 0.1074
REMARK 3 L33: 0.8205 L12: 0.0629
REMARK 3 L13: 0.1318 L23: -0.2601
REMARK 3 S TENSOR
REMARK 3 S11: -0.2232 S12: -0.2821 S13: 0.2053
REMARK 3 S21: 0.6028 S22: 0.1133 S23: 0.1095
REMARK 3 S31: -0.5047 S32: -0.1370 S33: -0.6402
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'R' AND (RESID 29 THROUGH 64 )
REMARK 3 ORIGIN FOR THE GROUP (A): 35.6114 45.4204 47.2276
REMARK 3 T TENSOR
REMARK 3 T11: 0.2874 T22: 0.3006
REMARK 3 T33: 0.1843 T12: 0.1153
REMARK 3 T13: -0.0439 T23: -0.0454
REMARK 3 L TENSOR
REMARK 3 L11: 0.5802 L22: 0.7015
REMARK 3 L33: 0.0325 L12: -0.1777
REMARK 3 L13: -0.1313 L23: -0.0307
REMARK 3 S TENSOR
REMARK 3 S11: -0.4429 S12: -0.6257 S13: 0.2487
REMARK 3 S21: 0.7079 S22: 0.4120 S23: -0.2045
REMARK 3 S31: 0.1883 S32: 0.2325 S33: -0.0494
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'R' AND (RESID 65 THROUGH 74 )
REMARK 3 ORIGIN FOR THE GROUP (A): 36.0689 54.5160 57.3144
REMARK 3 T TENSOR
REMARK 3 T11: 0.5138 T22: 0.4621
REMARK 3 T33: 0.3492 T12: 0.2367
REMARK 3 T13: -0.2601 T23: -0.2986
REMARK 3 L TENSOR
REMARK 3 L11: 0.0479 L22: 0.1850
REMARK 3 L33: 1.0415 L12: 0.0488
REMARK 3 L13: -0.0980 L23: 0.2434
REMARK 3 S TENSOR
REMARK 3 S11: -0.0088 S12: 0.0572 S13: -0.1950
REMARK 3 S21: 0.1742 S22: 0.2432 S23: -0.3792
REMARK 3 S31: 0.2393 S32: 0.4563 S33: -0.0219
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'R' AND (RESID 75 THROUGH 92 )
REMARK 3 ORIGIN FOR THE GROUP (A): 23.8725 65.5975 39.3960
REMARK 3 T TENSOR
REMARK 3 T11: 0.3120 T22: 0.2762
REMARK 3 T33: 0.3372 T12: 0.0809
REMARK 3 T13: -0.0701 T23: -0.0735
REMARK 3 L TENSOR
REMARK 3 L11: 1.0116 L22: 0.0558
REMARK 3 L33: 0.4147 L12: 0.0854
REMARK 3 L13: 0.2388 L23: -0.0387
REMARK 3 S TENSOR
REMARK 3 S11: -0.0546 S12: 0.0544 S13: 0.3266
REMARK 3 S21: 0.4284 S22: 0.2260 S23: -0.4208
REMARK 3 S31: 0.0064 S32: 0.4392 S33: 0.0932
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'R' AND (RESID 93 THROUGH 134 )
REMARK 3 ORIGIN FOR THE GROUP (A): 5.8154 63.1992 32.5149
REMARK 3 T TENSOR
REMARK 3 T11: 0.2089 T22: 0.2410
REMARK 3 T33: 0.3356 T12: 0.0241
REMARK 3 T13: -0.0238 T23: 0.0349
REMARK 3 L TENSOR
REMARK 3 L11: 0.4241 L22: 0.3673
REMARK 3 L33: 0.0998 L12: -0.4390
REMARK 3 L13: 0.2215 L23: -0.1847
REMARK 3 S TENSOR
REMARK 3 S11: 0.1751 S12: -0.0463 S13: -0.3369
REMARK 3 S21: -0.1107 S22: 0.1064 S23: 0.3948
REMARK 3 S31: 0.0175 S32: -0.1705 S33: 0.0018
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'R' AND (RESID 135 THROUGH 147 )
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6755 72.1024 36.4353
REMARK 3 T TENSOR
REMARK 3 T11: 0.2814 T22: 0.2264
REMARK 3 T33: 0.3317 T12: 0.0555
REMARK 3 T13: -0.0295 T23: -0.0313
REMARK 3 L TENSOR
REMARK 3 L11: 0.0460 L22: 0.0399
REMARK 3 L33: 0.0132 L12: 0.0006
REMARK 3 L13: 0.0172 L23: -0.0112
REMARK 3 S TENSOR
REMARK 3 S11: -0.1581 S12: -0.0797 S13: 0.4638
REMARK 3 S21: 0.2209 S22: 0.0850 S23: -0.3119
REMARK 3 S31: -0.0910 S32: -0.1447 S33: 0.0001
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 4J9Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-MAR-13.
REMARK 100 THE DEPOSITION ID IS D_1000077782.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAY-12
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 : 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) : 1.0781
REMARK 200 MONOCHROMATOR : SI(111) CHANNEL CUT
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 : SCALA 3.3.20
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38789
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.660
REMARK 200 RESOLUTION RANGE LOW (A) : 27.790
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 5.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.05200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.70
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 5.10
REMARK 200 R MERGE FOR SHELL (I) : 0.73300
REMARK 200 R SYM FOR SHELL (I) : 0.73300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 57.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.87
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.25 M LITHIUM SULFATE, 0.5 M AMMONIUM
REMARK 280 SULFATE, 0.1 M SODIUM CITRATE, PH 5.6, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
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 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 38.60000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 33.42500
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 38.60000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 33.42500
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 15140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22730 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -220.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, R
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 72.89217
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 64.68672
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 B 394
REMARK 465 HIS B 492
REMARK 465 HIS B 493
REMARK 465 HIS B 494
REMARK 465 HIS B 495
REMARK 465 MET R 0
REMARK 465 ALA R 1
REMARK 465 LYS R 148
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 HIS B 406 CG ND1 CD2 CE1 NE2
REMARK 470 MET B 412 CG SD CE
REMARK 470 HIS B 491 CG ND1 CD2 CE1 NE2
REMARK 470 ASP R 2 CG OD1 OD2
REMARK 470 GLN R 3 CG CD OE1 NE2
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 O GLY R 25 O HOH R 367 2.00
REMARK 500 O HOH B 619 O HOH B 647 2.07
REMARK 500 O HOH B 638 O HOH B 647 2.11
REMARK 500 OE1 GLU R 87 O HOH R 393 2.13
REMARK 500 O HOH R 392 O HOH R 395 2.13
REMARK 500 O HIS B 491 O HOH B 637 2.16
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 640 O HOH B 640 2656 1.65
REMARK 500 O ASP R 131 O HOH B 646 4556 2.05
REMARK 500 O HOH B 646 O HOH B 646 2656 2.09
REMARK 500 O HOH B 647 O HOH B 647 2656 2.12
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 LYS B 397 -111.04 46.74
REMARK 500 VAL B 407 61.27 -106.34
REMARK 500 PHE B 410 19.31 58.85
REMARK 500 MET B 412 -2.90 77.47
REMARK 500 LYS R 75 33.68 -145.08
REMARK 500 LYS R 115 157.07 81.27
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 MET B 412 ASP B 413 142.94
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 R 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP R 20 OD1
REMARK 620 2 ASP R 22 OD1 75.3
REMARK 620 3 ASP R 24 OD1 83.5 75.6
REMARK 620 4 THR R 26 O 78.1 146.2 80.9
REMARK 620 5 GLU R 31 OE2 98.6 78.7 152.8 126.2
REMARK 620 6 GLU R 31 OE1 106.6 133.7 150.3 74.2 55.0
REMARK 620 7 HOH R 317 O 158.3 106.8 76.4 90.6 103.0 87.7
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA R 203 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP R 56 OD1
REMARK 620 2 ASP R 58 OD2 106.1
REMARK 620 3 ASN R 60 OD1 95.0 68.5
REMARK 620 4 THR R 62 O 98.9 135.2 72.9
REMARK 620 5 GLU R 67 OE2 104.5 82.2 148.4 126.6
REMARK 620 6 GLU R 67 OE2 104.2 82.8 149.0 126.3 0.6
REMARK 620 7 GLU R 67 OE1 122.2 118.2 133.9 75.0 51.9 51.7
REMARK 620 8 GLU R 67 OE1 122.4 116.9 134.8 76.6 50.3 50.1 1.7
REMARK 620 9 HOH R 301 O 148.6 74.3 55.3 65.3 106.6 107.0 81.5 81.9
REMARK 620 N 1 2 3 4 5 6 7 8
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1KP R 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA R 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA R 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 R 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 R 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL R 206
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1G4Y RELATED DB: PDB
REMARK 900 RELATED ID: 4G27 RELATED DB: PDB
REMARK 900 RELATED ID: 4G28 RELATED DB: PDB
REMARK 900 RELATED ID: 3SJQ RELATED DB: PDB
REMARK 900 RELATED ID: 4J9Y RELATED DB: PDB
DBREF 4J9Z B 396 487 UNP P70604 KCNN2_RAT 396 487
DBREF 4J9Z R 0 148 UNP P62161 CALM_RAT 1 149
SEQADV 4J9Z MET B 394 UNP P70604 EXPRESSION TAG
SEQADV 4J9Z GLY B 395 UNP P70604 EXPRESSION TAG
SEQADV 4J9Z LEU B 488 UNP P70604 EXPRESSION TAG
SEQADV 4J9Z GLU B 489 UNP P70604 EXPRESSION TAG
SEQADV 4J9Z HIS B 490 UNP P70604 EXPRESSION TAG
SEQADV 4J9Z HIS B 491 UNP P70604 EXPRESSION TAG
SEQADV 4J9Z HIS B 492 UNP P70604 EXPRESSION TAG
SEQADV 4J9Z HIS B 493 UNP P70604 EXPRESSION TAG
SEQADV 4J9Z HIS B 494 UNP P70604 EXPRESSION TAG
SEQADV 4J9Z HIS B 495 UNP P70604 EXPRESSION TAG
SEQRES 1 B 102 MET GLY ARG LYS LEU GLU LEU THR LYS ALA GLU LYS HIS
SEQRES 2 B 102 VAL HIS ASN PHE MET MET ASP THR GLN LEU THR LYS ARG
SEQRES 3 B 102 VAL LYS ASN ALA ALA ALA ASN VAL LEU ARG GLU THR TRP
SEQRES 4 B 102 LEU ILE TYR LYS ASN THR LYS LEU VAL LYS LYS ILE ASP
SEQRES 5 B 102 HIS ALA LYS VAL ARG LYS HIS GLN ARG LYS PHE LEU GLN
SEQRES 6 B 102 ALA ILE HIS GLN LEU ARG SER VAL LYS MET GLU GLN ARG
SEQRES 7 B 102 LYS LEU ASN ASP GLN ALA ASN THR LEU VAL ASP LEU ALA
SEQRES 8 B 102 LYS THR GLN LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 R 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 R 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 R 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 R 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 R 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 R 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 R 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 R 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 R 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 R 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 R 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 R 149 GLN MET MET THR ALA LYS
HET SO4 B 501 5
HET SO4 B 502 5
HET 1KP R 201 14
HET CA R 202 1
HET CA R 203 1
HET SO4 R 204 5
HET SO4 R 205 5
HET GOL R 206 6
HETNAM SO4 SULFATE ION
HETNAM 1KP (3E)-6,7-DICHLORO-3-(HYDROXYIMINO)-1,3-DIHYDRO-2H-
HETNAM 2 1KP INDOL-2-ONE
HETNAM CA CALCIUM ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 SO4 4(O4 S 2-)
FORMUL 5 1KP C8 H4 CL2 N2 O2
FORMUL 6 CA 2(CA 2+)
FORMUL 10 GOL C3 H8 O3
FORMUL 11 HOH *156(H2 O)
HELIX 1 1 ASP B 413 LEU B 440 1 28
HELIX 2 2 ASP B 445 THR B 486 1 42
HELIX 3 3 GLN B 487 GLU B 489 5 3
HELIX 4 4 GLU R 6 ASP R 20 1 15
HELIX 5 5 THR R 28 LEU R 39 1 12
HELIX 6 6 THR R 44 VAL R 55 1 12
HELIX 7 7 ASP R 64 LYS R 75 1 12
HELIX 8 8 SER R 81 VAL R 91 1 11
HELIX 9 9 ALA R 102 LEU R 112 1 11
HELIX 10 10 THR R 117 ASP R 129 1 13
HELIX 11 11 TYR R 138 ALA R 147 1 10
SHEET 1 A 2 LEU B 400 THR B 401 0
SHEET 2 A 2 ASP R 78 THR R 79 -1 O THR R 79 N LEU B 400
SHEET 1 B 2 TYR R 99 SER R 101 0
SHEET 2 B 2 GLN R 135 ASN R 137 -1 O VAL R 136 N ILE R 100
LINK OD1 ASP R 20 CA CA R 202 1555 1555 2.39
LINK OD1 ASP R 22 CA CA R 202 1555 1555 2.27
LINK OD1 ASP R 24 CA CA R 202 1555 1555 2.27
LINK O THR R 26 CA CA R 202 1555 1555 2.23
LINK OE2 GLU R 31 CA CA R 202 1555 1555 2.35
LINK OE1 GLU R 31 CA CA R 202 1555 1555 2.41
LINK OD1 ASP R 56 CA CA R 203 1555 1555 2.13
LINK OD2 ASP R 58 CA CA R 203 1555 1555 2.32
LINK OD1 ASN R 60 CA CA R 203 1555 1555 2.66
LINK O THR R 62 CA CA R 203 1555 1555 2.55
LINK OE2BGLU R 67 CA CA R 203 1555 1555 2.45
LINK OE2AGLU R 67 CA CA R 203 1555 1555 2.54
LINK OE1BGLU R 67 CA CA R 203 1555 1555 2.56
LINK OE1AGLU R 67 CA CA R 203 1555 1555 2.64
LINK CA CA R 202 O HOH R 317 1555 1555 2.38
LINK CA CA R 203 O HOH R 301 1555 1555 1.98
CISPEP 1 HIS B 490 HIS B 491 0 7.61
SITE 1 AC1 4 ARG B 429 LYS B 451 HIS B 452 LYS B 455
SITE 1 AC2 2 ARG B 450 ARG B 454
SITE 1 AC3 10 PHE B 410 ALA B 477 LEU B 480 VAL B 481
SITE 2 AC3 10 LEU R 32 MET R 51 ILE R 63 MET R 71
SITE 3 AC3 10 MET R 72 LYS R 75
SITE 1 AC4 6 ASP R 20 ASP R 22 ASP R 24 THR R 26
SITE 2 AC4 6 GLU R 31 HOH R 317
SITE 1 AC5 6 ASP R 56 ASP R 58 ASN R 60 THR R 62
SITE 2 AC5 6 GLU R 67 HOH R 301
SITE 1 AC6 4 LYS B 402 ASP R 78 THR R 79 HOH R 338
SITE 1 AC7 2 LYS R 30 ARG R 126
SITE 1 AC8 6 ILE R 100 SER R 101 GLU R 104 HOH R 329
SITE 2 AC8 6 HOH R 332 HOH R 342
CRYST1 77.200 66.850 64.830 90.00 93.81 90.00 C 1 2 1 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 0.012953 0.000000 0.000863 0.00000
SCALE2 0.000000 0.014959 0.000000 0.00000
SCALE3 0.000000 0.000000 0.015459 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
