HEADER CALCIUM BINDING PROTEIN/MEMBRANE PROTEIN01-MAY-18 6DAE
TITLE 2.0 ANGSTROM CRYSTAL STRUCTURE OF THE D95V CA/CAM:CAV1.2 IQ DOMAIN
TITLE 2 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN-1;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: VOLTAGE-DEPENDENT L-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1C;
COMPND 8 CHAIN: D, C;
COMPND 9 FRAGMENT: UNP RESIDUES 1611-1644;
COMPND 10 SYNONYM: CALCIUM CHANNEL, L TYPE,ALPHA-1 POLYPEPTIDE, ISOFORM 1,
COMPND 11 CARDIAC MUSCLE, VOLTAGE-GATED CALCIUM CHANNEL SUBUNIT ALPHA CAV1.2;
COMPND 12 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: CACNA1C, CACH2, CACN2, CACNL1A1, CCHL1A1;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS CALMODULIN, MUTANT, COMPLEX, CALCIUM BINDING PROTEIN-MEMBRANE PROTEIN
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR K.WANG,J.LU,F.VAN PETEGEM
REVDAT 5 04-OCT-23 6DAE 1 LINK
REVDAT 4 17-APR-19 6DAE 1 REMARK
REVDAT 3 21-NOV-18 6DAE 1 JRNL
REVDAT 2 31-OCT-18 6DAE 1 JRNL
REVDAT 1 17-OCT-18 6DAE 0
JRNL AUTH K.WANG,C.HOLT,J.LU,M.BROHUS,K.T.LARSEN,M.T.OVERGAARD,
JRNL AUTH 2 R.WIMMER,F.VAN PETEGEM
JRNL TITL ARRHYTHMIA MUTATIONS IN CALMODULIN CAUSE CONFORMATIONAL
JRNL TITL 2 CHANGES THAT AFFECT INTERACTIONS WITH THE CARDIAC
JRNL TITL 3 VOLTAGE-GATED CALCIUM CHANNEL.
JRNL REF PROC. NATL. ACAD. SCI. V. 115 10556 2018
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 30348784
JRNL DOI 10.1073/PNAS.1808733115
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.13_2998
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.04
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 51054
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.179
REMARK 3 R VALUE (WORKING SET) : 0.176
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2555
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 43.0489 - 5.2386 1.00 2704 144 0.1718 0.1764
REMARK 3 2 5.2386 - 4.1591 1.00 2680 138 0.1386 0.2024
REMARK 3 3 4.1591 - 3.6337 1.00 2706 140 0.1387 0.2016
REMARK 3 4 3.6337 - 3.3016 1.00 2681 141 0.1784 0.2089
REMARK 3 5 3.3016 - 3.0650 1.00 2687 141 0.1863 0.2296
REMARK 3 6 3.0650 - 2.8844 1.00 2723 138 0.1985 0.2478
REMARK 3 7 2.8844 - 2.7399 1.00 2678 139 0.1977 0.2445
REMARK 3 8 2.7399 - 2.6207 1.00 2688 144 0.1815 0.2557
REMARK 3 9 2.6207 - 2.5198 1.00 2667 145 0.1817 0.2346
REMARK 3 10 2.5198 - 2.4329 1.00 2741 146 0.1730 0.2314
REMARK 3 11 2.4329 - 2.3568 1.00 2701 142 0.1746 0.2302
REMARK 3 12 2.3568 - 2.2894 1.00 2684 141 0.1742 0.2029
REMARK 3 13 2.2894 - 2.2292 1.00 2675 142 0.1914 0.2418
REMARK 3 14 2.2292 - 2.1748 1.00 2668 143 0.1839 0.2741
REMARK 3 15 2.1748 - 2.1253 1.00 2734 147 0.1895 0.2681
REMARK 3 16 2.1253 - 2.0801 1.00 2683 138 0.2111 0.2829
REMARK 3 17 2.0801 - 2.0385 1.00 2671 143 0.2270 0.2677
REMARK 3 18 2.0385 - 2.0000 1.00 2728 143 0.2379 0.3127
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.230
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.120
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.11
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 : NULL NULL
REMARK 3 ANGLE : NULL NULL
REMARK 3 CHIRALITY : NULL NULL
REMARK 3 PLANARITY : NULL NULL
REMARK 3 DIHEDRAL : NULL NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND ((RESID 2 THROUGH 78 ) OR (RESID 501
REMARK 3 THROUGH 502))
REMARK 3 ORIGIN FOR THE GROUP (A): 7.4310 2.1967 0.1329
REMARK 3 T TENSOR
REMARK 3 T11: 0.1185 T22: 0.1319
REMARK 3 T33: 0.1551 T12: 0.0053
REMARK 3 T13: -0.0064 T23: -0.0041
REMARK 3 L TENSOR
REMARK 3 L11: 1.6347 L22: 1.5531
REMARK 3 L33: 3.0079 L12: 0.3061
REMARK 3 L13: -0.9684 L23: 0.2780
REMARK 3 S TENSOR
REMARK 3 S11: 0.0015 S12: 0.1796 S13: -0.0183
REMARK 3 S21: -0.0961 S22: -0.0476 S23: -0.0332
REMARK 3 S31: -0.0125 S32: -0.0736 S33: 0.0462
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND ((RESID 79 THROUGH 146 ) OR (RESID
REMARK 3 504))
REMARK 3 ORIGIN FOR THE GROUP (A): 2.8246 23.2398 -1.6610
REMARK 3 T TENSOR
REMARK 3 T11: 0.2144 T22: 0.2473
REMARK 3 T33: 0.2119 T12: 0.0726
REMARK 3 T13: 0.0157 T23: 0.0221
REMARK 3 L TENSOR
REMARK 3 L11: 2.6641 L22: 3.1019
REMARK 3 L33: 2.9850 L12: -0.4930
REMARK 3 L13: 1.0502 L23: 0.9031
REMARK 3 S TENSOR
REMARK 3 S11: 0.0876 S12: 0.2925 S13: 0.2336
REMARK 3 S21: -0.2890 S22: -0.2370 S23: 0.1062
REMARK 3 S31: -0.3558 S32: -0.2936 S33: 0.1445
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND ((RESID 3 THROUGH 78) OR (RESID 501
REMARK 3 THROUGH 502))
REMARK 3 ORIGIN FOR THE GROUP (A): 16.8494 -10.1487 -17.6982
REMARK 3 T TENSOR
REMARK 3 T11: 0.1512 T22: 0.1242
REMARK 3 T33: 0.1446 T12: 0.0012
REMARK 3 T13: 0.0122 T23: 0.0133
REMARK 3 L TENSOR
REMARK 3 L11: 2.4535 L22: 1.5221
REMARK 3 L33: 4.0248 L12: -0.4677
REMARK 3 L13: -0.5118 L23: 1.7894
REMARK 3 S TENSOR
REMARK 3 S11: -0.0697 S12: -0.0455 S13: -0.0329
REMARK 3 S21: -0.0278 S22: 0.0422 S23: -0.0493
REMARK 3 S31: -0.0253 S32: -0.1430 S33: 0.0347
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND ((RESID 79 THROUGH 146 ) OR (RESID
REMARK 3 504))
REMARK 3 ORIGIN FOR THE GROUP (A): 35.7140 -19.5707 -17.1639
REMARK 3 T TENSOR
REMARK 3 T11: 0.1729 T22: 0.1493
REMARK 3 T33: 0.1349 T12: 0.0469
REMARK 3 T13: -0.0041 T23: -0.0189
REMARK 3 L TENSOR
REMARK 3 L11: 2.2941 L22: 4.2590
REMARK 3 L33: 2.4245 L12: -0.0590
REMARK 3 L13: 0.0130 L23: -2.2232
REMARK 3 S TENSOR
REMARK 3 S11: -0.0344 S12: -0.0163 S13: 0.0080
REMARK 3 S21: -0.0154 S22: -0.0302 S23: -0.0987
REMARK 3 S31: 0.1311 S32: 0.1650 S33: 0.0682
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'D' AND (RESID 1612 THROUGH 1635 )
REMARK 3 ORIGIN FOR THE GROUP (A): 30.0685 -11.5666 -13.5852
REMARK 3 T TENSOR
REMARK 3 T11: 0.2220 T22: 0.1556
REMARK 3 T33: 0.1789 T12: 0.0784
REMARK 3 T13: -0.0091 T23: -0.0172
REMARK 3 L TENSOR
REMARK 3 L11: 6.8581 L22: 6.0307
REMARK 3 L33: 4.5545 L12: 3.3673
REMARK 3 L13: -1.0382 L23: 0.4363
REMARK 3 S TENSOR
REMARK 3 S11: 0.0503 S12: -0.1271 S13: 0.3055
REMARK 3 S21: 0.2313 S22: 0.0769 S23: -0.1628
REMARK 3 S31: -0.2163 S32: 0.1314 S33: -0.1351
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 1612 THROUGH 1634 )
REMARK 3 ORIGIN FOR THE GROUP (A): 8.3033 14.8819 -4.9423
REMARK 3 T TENSOR
REMARK 3 T11: 0.2321 T22: 0.2346
REMARK 3 T33: 0.2473 T12: 0.0557
REMARK 3 T13: 0.0306 T23: 0.0186
REMARK 3 L TENSOR
REMARK 3 L11: 7.1644 L22: 3.6470
REMARK 3 L33: 3.0447 L12: 4.8333
REMARK 3 L13: -0.2977 L23: 0.8296
REMARK 3 S TENSOR
REMARK 3 S11: -0.0087 S12: 0.3214 S13: 0.2335
REMARK 3 S21: -0.2368 S22: 0.1179 S23: -0.1605
REMARK 3 S31: -0.2386 S32: 0.2090 S33: -0.1203
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 6DAE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-18.
REMARK 100 THE DEPOSITION ID IS D_1000234209.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-DEC-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 10.3
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-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.033
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL CRYO-COOLED
REMARK 200 SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51221
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 43.039
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.880
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.8400
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
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 : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRIES 2BE6 & 4CDK
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.01
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 M LITHIUM CHLORIDE, 30% PEG6000,
REMARK 280 0.1M BICINE, PH 10.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 277K
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 32.57400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 43.03900
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 34.80750
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 43.03900
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.57400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 34.80750
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: 2810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9010 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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
REMARK 350 BIOMOLECULE: 2
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: 2780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9100 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 ALA A 1
REMARK 465 ALA A 147
REMARK 465 LYS A 148
REMARK 465 ALA B 1
REMARK 465 ASP B 2
REMARK 465 ALA B 147
REMARK 465 LYS B 148
REMARK 465 SER D 1608
REMARK 465 ASN D 1609
REMARK 465 ALA D 1610
REMARK 465 ASP D 1611
REMARK 465 GLU D 1636
REMARK 465 GLN D 1637
REMARK 465 GLY D 1638
REMARK 465 LEU D 1639
REMARK 465 VAL D 1640
REMARK 465 GLY D 1641
REMARK 465 LYS D 1642
REMARK 465 PRO D 1643
REMARK 465 SER D 1644
REMARK 465 SER C 1608
REMARK 465 ASN C 1609
REMARK 465 ALA C 1610
REMARK 465 ASP C 1611
REMARK 465 LYS C 1635
REMARK 465 GLU C 1636
REMARK 465 GLN C 1637
REMARK 465 GLY C 1638
REMARK 465 LEU C 1639
REMARK 465 VAL C 1640
REMARK 465 GLY C 1641
REMARK 465 LYS C 1642
REMARK 465 PRO C 1643
REMARK 465 SER C 1644
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 GLU A 6 CG CD OE1 OE2
REMARK 470 ASP A 80 CG OD1 OD2
REMARK 470 GLU A 82 CG CD OE1 OE2
REMARK 470 GLU A 83 CG CD OE1 OE2
REMARK 470 ARG A 90 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 94 CG CD CE NZ
REMARK 470 LYS A 115 CG CD CE NZ
REMARK 470 GLU A 119 CG CD OE1 OE2
REMARK 470 ASP A 122 CG OD1 OD2
REMARK 470 GLU A 139 CG CD OE1 OE2
REMARK 470 ASP B 80 CG OD1 OD2
REMARK 470 LYS B 94 CG CD CE NZ
REMARK 470 GLU B 119 CG CD OE1 OE2
REMARK 470 GLU B 123 CG CD OE1 OE2
REMARK 470 GLU B 127 CG CD OE1 OE2
REMARK 470 GLU D1612 CG CD OE1 OE2
REMARK 470 LYS D1630 CG CD CE NZ
REMARK 470 LYS D1633 CG CD CE NZ
REMARK 470 GLU C1612 CG CD OE1 OE2
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 B 56 90.72 -63.85
REMARK 500 ARG D1634 93.50 -67.63
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 20 OD1
REMARK 620 2 ASP A 22 OD1 74.0
REMARK 620 3 ASP A 24 OD1 82.0 83.4
REMARK 620 4 THR A 26 O 81.0 152.2 81.3
REMARK 620 5 GLU A 31 OE1 96.8 74.5 157.2 121.2
REMARK 620 6 GLU A 31 OE2 117.6 126.4 146.7 76.2 52.9
REMARK 620 7 HOH A 650 O 158.7 86.1 88.6 116.5 84.5 80.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 56 OD1
REMARK 620 2 ASP A 58 OD1 74.2
REMARK 620 3 ASN A 60 OD1 82.9 78.3
REMARK 620 4 THR A 62 O 75.3 144.3 80.0
REMARK 620 5 GLU A 67 OE1 96.9 120.6 160.5 81.0
REMARK 620 6 GLU A 67 OE2 83.4 69.7 147.5 124.2 50.9
REMARK 620 7 HOH A 618 O 148.3 75.0 98.1 136.3 92.3 79.1
REMARK 620 8 HOH A 653 O 144.8 130.6 79.8 71.7 89.8 125.7 65.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 129 OD1
REMARK 620 2 ASP A 131 OD1 80.6
REMARK 620 3 ASP A 133 OD1 79.8 76.7
REMARK 620 4 GLN A 135 O 78.6 150.5 79.2
REMARK 620 5 GLU A 140 OE1 112.5 126.9 153.8 80.9
REMARK 620 6 GLU A 140 OE2 98.0 75.3 151.9 128.3 52.5
REMARK 620 7 HOH A 664 O 163.8 96.3 84.0 97.8 82.1 96.6
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 501 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 20 OD1
REMARK 620 2 ASP B 22 OD1 79.3
REMARK 620 3 ASP B 24 OD1 87.4 80.7
REMARK 620 4 THR B 26 O 81.1 156.0 84.6
REMARK 620 5 GLU B 31 OE1 95.4 71.6 151.0 124.3
REMARK 620 6 GLU B 31 OE2 110.1 123.6 151.5 76.4 52.5
REMARK 620 7 HOH B 634 O 165.8 86.9 87.0 111.3 83.3 80.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 56 OD1
REMARK 620 2 ASP B 58 OD1 70.3
REMARK 620 3 ASN B 60 OD1 81.7 77.8
REMARK 620 4 THR B 62 O 78.7 144.3 80.5
REMARK 620 5 GLU B 67 OE1 99.1 121.0 160.5 80.6
REMARK 620 6 GLU B 67 OE2 81.0 69.3 146.4 123.6 51.7
REMARK 620 7 HOH B 608 O 140.0 138.2 80.2 63.3 87.1 129.8
REMARK 620 8 HOH B 627 O 149.9 79.7 95.2 130.5 93.5 85.8 67.4
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 503 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 129 OD1
REMARK 620 2 ASP B 131 OD1 79.5
REMARK 620 3 ASP B 133 OD1 84.8 83.2
REMARK 620 4 GLN B 135 O 82.5 156.1 79.7
REMARK 620 5 GLU B 140 OE1 106.9 121.6 153.7 78.6
REMARK 620 6 GLU B 140 OE2 95.5 70.9 153.5 126.6 50.8
REMARK 620 7 HOH B 621 O 164.9 94.8 80.7 98.7 88.0 95.8
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 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 503
DBREF 6DAE A 1 148 UNP P0DP23 CALM1_HUMAN 2 149
DBREF 6DAE B 1 148 UNP P0DP23 CALM1_HUMAN 2 149
DBREF 6DAE D 1611 1644 UNP Q13936 CAC1C_HUMAN 1611 1644
DBREF 6DAE C 1611 1644 UNP Q13936 CAC1C_HUMAN 1611 1644
SEQADV 6DAE VAL A 95 UNP P0DP23 ASP 96 ENGINEERED MUTATION
SEQADV 6DAE VAL B 95 UNP P0DP23 ASP 96 ENGINEERED MUTATION
SEQADV 6DAE SER D 1608 UNP Q13936 EXPRESSION TAG
SEQADV 6DAE ASN D 1609 UNP Q13936 EXPRESSION TAG
SEQADV 6DAE ALA D 1610 UNP Q13936 EXPRESSION TAG
SEQADV 6DAE SER C 1608 UNP Q13936 EXPRESSION TAG
SEQADV 6DAE ASN C 1609 UNP Q13936 EXPRESSION TAG
SEQADV 6DAE ALA C 1610 UNP Q13936 EXPRESSION TAG
SEQRES 1 A 148 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES 2 A 148 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR
SEQRES 3 A 148 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU
SEQRES 4 A 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE
SEQRES 5 A 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE
SEQRES 6 A 148 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP
SEQRES 7 A 148 THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL
SEQRES 8 A 148 PHE ASP LYS VAL GLY ASN GLY TYR ILE SER ALA ALA GLU
SEQRES 9 A 148 LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR
SEQRES 10 A 148 ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE
SEQRES 11 A 148 ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN
SEQRES 12 A 148 MET MET THR ALA LYS
SEQRES 1 B 148 ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS
SEQRES 2 B 148 GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR
SEQRES 3 B 148 ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER LEU
SEQRES 4 B 148 GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE
SEQRES 5 B 148 ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE
SEQRES 6 B 148 PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS ASP
SEQRES 7 B 148 THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL
SEQRES 8 B 148 PHE ASP LYS VAL GLY ASN GLY TYR ILE SER ALA ALA GLU
SEQRES 9 B 148 LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR
SEQRES 10 B 148 ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE
SEQRES 11 B 148 ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN
SEQRES 12 B 148 MET MET THR ALA LYS
SEQRES 1 D 37 SER ASN ALA ASP GLU VAL THR VAL GLY LYS PHE TYR ALA
SEQRES 2 D 37 THR PHE LEU ILE GLN GLU TYR PHE ARG LYS PHE LYS LYS
SEQRES 3 D 37 ARG LYS GLU GLN GLY LEU VAL GLY LYS PRO SER
SEQRES 1 C 37 SER ASN ALA ASP GLU VAL THR VAL GLY LYS PHE TYR ALA
SEQRES 2 C 37 THR PHE LEU ILE GLN GLU TYR PHE ARG LYS PHE LYS LYS
SEQRES 3 C 37 ARG LYS GLU GLN GLY LEU VAL GLY LYS PRO SER
HET CA A 501 1
HET CA A 502 1
HET CA A 503 1
HET CA B 501 1
HET CA B 502 1
HET CA B 503 1
HETNAM CA CALCIUM ION
FORMUL 5 CA 6(CA 2+)
FORMUL 11 HOH *219(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 THR A 79 1 15
HELIX 5 AA5 ASP A 80 ASP A 93 1 14
HELIX 6 AA6 ALA A 102 GLY A 113 1 12
HELIX 7 AA7 THR A 117 ASP A 129 1 13
HELIX 8 AA8 TYR A 138 THR A 146 1 9
HELIX 9 AA9 THR B 5 ASP B 20 1 16
HELIX 10 AB1 THR B 28 LEU B 39 1 12
HELIX 11 AB2 THR B 44 ASP B 56 1 13
HELIX 12 AB3 PHE B 65 THR B 79 1 15
HELIX 13 AB4 ASP B 80 ASP B 93 1 14
HELIX 14 AB5 ALA B 102 GLY B 113 1 12
HELIX 15 AB6 THR B 117 ASP B 129 1 13
HELIX 16 AB7 TYR B 138 THR B 146 1 9
HELIX 17 AB8 VAL D 1613 ARG D 1634 1 22
HELIX 18 AB9 VAL C 1613 ARG C 1634 1 22
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 TYR A 99 SER A 101 0
SHEET 2 AA2 2 GLN A 135 ASN A 137 -1 O VAL A 136 N ILE A 100
SHEET 1 AA3 2 THR B 26 ILE B 27 0
SHEET 2 AA3 2 ILE B 63 ASP B 64 -1 O ILE B 63 N ILE B 27
SHEET 1 AA4 2 TYR B 99 SER B 101 0
SHEET 2 AA4 2 GLN B 135 ASN B 137 -1 O VAL B 136 N ILE B 100
LINK OD1 ASP A 20 CA CA A 501 1555 1555 2.30
LINK OD1 ASP A 22 CA CA A 501 1555 1555 2.36
LINK OD1 ASP A 24 CA CA A 501 1555 1555 2.40
LINK O THR A 26 CA CA A 501 1555 1555 2.33
LINK OE1 GLU A 31 CA CA A 501 1555 1555 2.46
LINK OE2 GLU A 31 CA CA A 501 1555 1555 2.49
LINK OD1 ASP A 56 CA CA A 502 1555 1555 2.38
LINK OD1 ASP A 58 CA CA A 502 1555 1555 2.42
LINK OD1 ASN A 60 CA CA A 502 1555 1555 2.47
LINK O THR A 62 CA CA A 502 1555 1555 2.50
LINK OE1 GLU A 67 CA CA A 502 1555 1555 2.53
LINK OE2 GLU A 67 CA CA A 502 1555 1555 2.59
LINK OD1 ASP A 129 CA CA A 503 1555 1555 2.32
LINK OD1 ASP A 131 CA CA A 503 1555 1555 2.27
LINK OD1 ASP A 133 CA CA A 503 1555 1555 2.36
LINK O GLN A 135 CA CA A 503 1555 1555 2.35
LINK OE1 GLU A 140 CA CA A 503 1555 1555 2.46
LINK OE2 GLU A 140 CA CA A 503 1555 1555 2.53
LINK CA CA A 501 O HOH A 650 1555 1555 2.43
LINK CA CA A 502 O HOH A 618 1555 1555 2.47
LINK CA CA A 502 O HOH A 653 1555 1555 2.45
LINK CA CA A 503 O HOH A 664 1555 1555 2.37
LINK OD1 ASP B 20 CA CA B 501 1555 1555 2.29
LINK OD1 ASP B 22 CA CA B 501 1555 1555 2.27
LINK OD1 ASP B 24 CA CA B 501 1555 1555 2.38
LINK O THR B 26 CA CA B 501 1555 1555 2.28
LINK OE1 GLU B 31 CA CA B 501 1555 1555 2.48
LINK OE2 GLU B 31 CA CA B 501 1555 1555 2.48
LINK OD1 ASP B 56 CA CA B 502 1555 1555 2.32
LINK OD1 ASP B 58 CA CA B 502 1555 1555 2.45
LINK OD1 ASN B 60 CA CA B 502 1555 1555 2.34
LINK O THR B 62 CA CA B 502 1555 1555 2.42
LINK OE1 GLU B 67 CA CA B 502 1555 1555 2.47
LINK OE2 GLU B 67 CA CA B 502 1555 1555 2.58
LINK OD1 ASP B 129 CA CA B 503 1555 1555 2.35
LINK OD1 ASP B 131 CA CA B 503 1555 1555 2.38
LINK OD1 ASP B 133 CA CA B 503 1555 1555 2.37
LINK O GLN B 135 CA CA B 503 1555 1555 2.27
LINK OE1 GLU B 140 CA CA B 503 1555 1555 2.53
LINK OE2 GLU B 140 CA CA B 503 1555 1555 2.58
LINK CA CA B 501 O HOH B 634 1555 1555 2.42
LINK CA CA B 502 O HOH B 608 1555 1555 2.54
LINK CA CA B 502 O HOH B 627 1555 1555 2.46
LINK CA CA B 503 O HOH B 621 1555 1555 2.50
SITE 1 AC1 6 ASP A 20 ASP A 22 ASP A 24 THR A 26
SITE 2 AC1 6 GLU A 31 HOH A 650
SITE 1 AC2 7 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 AC2 7 GLU A 67 HOH A 618 HOH A 653
SITE 1 AC3 6 ASP A 129 ASP A 131 ASP A 133 GLN A 135
SITE 2 AC3 6 GLU A 140 HOH A 664
SITE 1 AC4 6 ASP B 20 ASP B 22 ASP B 24 THR B 26
SITE 2 AC4 6 GLU B 31 HOH B 634
SITE 1 AC5 7 ASP B 56 ASP B 58 ASN B 60 THR B 62
SITE 2 AC5 7 GLU B 67 HOH B 608 HOH B 627
SITE 1 AC6 6 ASP B 129 ASP B 131 ASP B 133 GLN B 135
SITE 2 AC6 6 GLU B 140 HOH B 621
CRYST1 65.148 69.615 86.078 90.00 90.00 90.00 P 21 21 21 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 0.015350 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014365 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011617 0.00000
(ATOM LINES ARE NOT SHOWN.)
END