HEADER MEMBRANE PROTEIN 18-JUL-08 3DVE
TITLE CRYSTAL STRUCTURE OF CA2+/CAM-CAV2.2 IQ DOMAIN COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: CAM;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: VOLTAGE-DEPENDENT N-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1B;
COMPND 8 CHAIN: B;
COMPND 9 FRAGMENT: UNP RESIDUES 1855-1875;
COMPND 10 SYNONYM: VOLTAGE-GATED CALCIUM CHANNEL SUBUNIT ALPHA CAV2.2, CALCIUM
COMPND 11 CHANNEL, L TYPE, ALPHA-1 POLYPEPTIDE ISOFORM 5, BRAIN CALCIUM CHANNEL
COMPND 12 III, BIII;
COMPND 13 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, CALM2, CAM2, CAMB, CALM3, CALML2,
SOURCE 6 CAM3, CAMC, CAMIII;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-PLYSS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PEGST;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 14 ORGANISM_COMMON: RABBIT;
SOURCE 15 ORGANISM_TAXID: 9986;
SOURCE 16 GENE: CACNA1B, CACH5, CACNL1A5;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 19 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-PLYSS;
SOURCE 20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 21 EXPRESSION_SYSTEM_PLASMID: PET28B-HMT
KEYWDS CALMODULIN, CALCIUM CHANNEL, IQ DOMAIN, INACTIVATION, FACILITATION,
KEYWDS 2 CALCIUM-DEPENDENT, VOLTAGE-GATED, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR E.Y.KIM,C.H.RUMPF,Y.FUJIWARA,E.S.COOLEY,F.VAN PETEGEM,D.L.MINOR
REVDAT 5 21-FEB-24 3DVE 1 REMARK SEQADV
REVDAT 4 25-OCT-17 3DVE 1 REMARK
REVDAT 3 13-JUL-11 3DVE 1 VERSN
REVDAT 2 24-FEB-09 3DVE 1 VERSN
REVDAT 1 04-NOV-08 3DVE 0
JRNL AUTH E.Y.KIM,C.H.RUMPF,Y.FUJIWARA,E.S.COOLEY,F.VAN PETEGEM,
JRNL AUTH 2 D.L.MINOR
JRNL TITL STRUCTURES OF CA(V)2 CA(2+)/CAM-IQ DOMAIN COMPLEXES REVEAL
JRNL TITL 2 BINDING MODES THAT UNDERLIE CALCIUM-DEPENDENT INACTIVATION
JRNL TITL 3 AND FACILITATION.
JRNL REF STRUCTURE V. 16 1455 2008
JRNL REFN ISSN 0969-2126
JRNL PMID 18940602
JRNL DOI 10.1016/J.STR.2008.07.010
REMARK 2
REMARK 2 RESOLUTION. 2.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 7757
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) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.271
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 358
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) : 2.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.41
REMARK 3 REFLECTION IN BIN (WORKING SET) : 483
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.05
REMARK 3 BIN R VALUE (WORKING SET) : 0.2040
REMARK 3 BIN FREE R VALUE SET COUNT : 26
REMARK 3 BIN FREE R VALUE : 0.3240
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1254
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 78
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.34
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.54000
REMARK 3 B22 (A**2) : -0.54000
REMARK 3 B33 (A**2) : 0.81000
REMARK 3 B12 (A**2) : -0.27000
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): 0.419
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.279
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.179
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.012
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.903
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1308 ; 0.015 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1764 ; 1.379 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 171 ; 5.544 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 71 ;30.037 ;25.915
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 239 ;15.972 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;19.382 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 194 ; 0.086 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1007 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 814 ; 0.746 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1300 ; 1.482 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 494 ; 2.455 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 458 ; 4.176 ; 4.500
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 : 5
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 5 A 39
REMARK 3 ORIGIN FOR THE GROUP (A): -1.7196 20.6417 17.3410
REMARK 3 T TENSOR
REMARK 3 T11: 0.0186 T22: -0.0055
REMARK 3 T33: 0.0019 T12: 0.0086
REMARK 3 T13: -0.0125 T23: 0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 0.3889 L22: 1.7307
REMARK 3 L33: 5.4858 L12: 0.7706
REMARK 3 L13: -0.1603 L23: -1.3689
REMARK 3 S TENSOR
REMARK 3 S11: 0.0257 S12: 0.0292 S13: -0.0141
REMARK 3 S21: 0.0594 S22: 0.0574 S23: -0.1817
REMARK 3 S31: 0.3461 S32: -0.0803 S33: -0.0831
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 45 A 75
REMARK 3 ORIGIN FOR THE GROUP (A): -8.0867 30.0799 20.6052
REMARK 3 T TENSOR
REMARK 3 T11: -0.0033 T22: 0.0377
REMARK 3 T33: -0.0067 T12: 0.0283
REMARK 3 T13: 0.0490 T23: 0.0163
REMARK 3 L TENSOR
REMARK 3 L11: 0.5289 L22: 0.2334
REMARK 3 L33: 4.4454 L12: 0.1978
REMARK 3 L13: -0.2142 L23: -0.9137
REMARK 3 S TENSOR
REMARK 3 S11: 0.0728 S12: -0.0671 S13: 0.1195
REMARK 3 S21: 0.1980 S22: 0.0981 S23: 0.1884
REMARK 3 S31: -0.2667 S32: -0.2962 S33: -0.1709
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 : A 82 A 112
REMARK 3 ORIGIN FOR THE GROUP (A): -11.0742 13.0818 2.6398
REMARK 3 T TENSOR
REMARK 3 T11: -0.0223 T22: -0.0606
REMARK 3 T33: 0.0109 T12: 0.0023
REMARK 3 T13: -0.0084 T23: 0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 4.7570 L22: 2.7359
REMARK 3 L33: 2.5546 L12: 0.5765
REMARK 3 L13: 0.0939 L23: -0.9576
REMARK 3 S TENSOR
REMARK 3 S11: -0.1330 S12: 0.1703 S13: 0.4022
REMARK 3 S21: -0.0066 S22: 0.0311 S23: 0.0091
REMARK 3 S31: -0.1615 S32: -0.0157 S33: 0.1019
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 : A 118 A 146
REMARK 3 ORIGIN FOR THE GROUP (A): -14.0353 5.2078 9.4638
REMARK 3 T TENSOR
REMARK 3 T11: 0.0006 T22: -0.0263
REMARK 3 T33: -0.0077 T12: 0.0134
REMARK 3 T13: -0.0129 T23: 0.0007
REMARK 3 L TENSOR
REMARK 3 L11: 3.0619 L22: 0.7985
REMARK 3 L33: 2.9551 L12: 0.8654
REMARK 3 L13: 0.8152 L23: -0.8785
REMARK 3 S TENSOR
REMARK 3 S11: -0.0224 S12: -0.1132 S13: 0.0316
REMARK 3 S21: 0.1962 S22: -0.0598 S23: -0.0653
REMARK 3 S31: -0.0692 S32: -0.0629 S33: 0.0823
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 1853 B 1875
REMARK 3 ORIGIN FOR THE GROUP (A): -11.9883 23.6503 11.7206
REMARK 3 T TENSOR
REMARK 3 T11: -0.0515 T22: -0.0023
REMARK 3 T33: -0.0010 T12: -0.0037
REMARK 3 T13: 0.0123 T23: -0.0001
REMARK 3 L TENSOR
REMARK 3 L11: 0.8540 L22: 9.6907
REMARK 3 L33: 1.1267 L12: -1.9378
REMARK 3 L13: 0.9517 L23: -2.3508
REMARK 3 S TENSOR
REMARK 3 S11: 0.0455 S12: 0.0571 S13: 0.0884
REMARK 3 S21: 0.0072 S22: -0.0618 S23: -0.0355
REMARK 3 S31: 0.0564 S32: -0.0038 S33: 0.0163
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
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
REMARK 4
REMARK 4 3DVE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUL-08.
REMARK 100 THE DEPOSITION ID IS D_1000048536.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-NOV-07
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.11587
REMARK 200 MONOCHROMATOR : DOUBLE FLAT CRYSTAL, SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7844
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.350
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 15.00
REMARK 200 R MERGE (I) : 0.13400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.8000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.43
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.50
REMARK 200 R MERGE FOR SHELL (I) : 0.42500
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: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.50
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, 25-30 % PEG 2000 MME,
REMARK 280 PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2
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 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+5/6
REMARK 290 6555 X-Y,X,Z+1/6
REMARK 290 7555 Y,X,-Z+1/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+2/3
REMARK 290 10555 -Y,-X,-Z+5/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+1/6
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 114.88400
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 229.76800
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 172.32600
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 287.21000
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 57.44200
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 114.88400
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 229.76800
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 287.21000
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 172.32600
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 57.44200
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: 3430 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 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 ALA A 1
REMARK 465 ASP A 2
REMARK 465 GLN A 3
REMARK 465 ASP A 78
REMARK 465 THR A 79
REMARK 465 ASP A 80
REMARK 465 SER A 81
REMARK 465 ALA A 147
REMARK 465 LYS A 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 LEU A 4 CG CD1 CD2
REMARK 470 GLU A 45 CG CD OE1 OE2
REMARK 470 LYS A 77 CG CD CE NZ
REMARK 470 GLU A 82 CG CD OE1 OE2
REMARK 470 LYS A 115 CB CG CD CE NZ
REMARK 470 GLU A 119 CG CD OE1 OE2
REMARK 470 HIS B1853 CG ND1 CD2 CE1 NE2
REMARK 470 SER B1873 OG
REMARK 470 ARG B1874 CG CD NE CZ NH1 NH2
REMARK 470 ASP B1875 CG OD1 OD2
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 56 74.92 -69.21
REMARK 500 GLU A 83 -33.58 -38.84
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 83.1
REMARK 620 3 ASP A 24 OD2 89.4 76.8
REMARK 620 4 THR A 26 O 91.0 152.3 76.1
REMARK 620 5 GLU A 31 OE1 105.2 129.3 150.7 78.3
REMARK 620 6 GLU A 31 OE2 93.8 79.2 155.1 128.3 50.8
REMARK 620 7 HOH A 524 O 166.2 83.1 86.7 100.9 84.3 84.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 502 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 56 OD2
REMARK 620 2 ASP A 58 OD2 76.9
REMARK 620 3 ASN A 60 OD1 91.3 79.3
REMARK 620 4 THR A 62 O 92.8 157.3 80.8
REMARK 620 5 GLU A 67 OE1 109.9 127.3 148.4 75.1
REMARK 620 6 GLU A 67 OE2 86.7 78.5 157.6 121.5 51.0
REMARK 620 7 HOH A 543 O 162.0 85.5 81.9 102.4 83.6 93.3
REMARK 620 N 1 2 3 4 5 6
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 93 OD2
REMARK 620 2 ASP A 95 OD1 87.4
REMARK 620 3 ASN A 97 OD1 88.8 83.7
REMARK 620 4 TYR A 99 O 86.7 161.3 78.5
REMARK 620 5 GLU A 104 OE1 97.7 80.5 162.6 117.9
REMARK 620 6 GLU A 104 OE2 101.8 130.2 144.2 68.4 50.0
REMARK 620 7 HOH A 535 O 170.1 85.9 83.2 97.4 88.5 88.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 504 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 129 OD2
REMARK 620 2 ASP A 131 OD1 80.2
REMARK 620 3 ASP A 133 OD2 96.7 80.4
REMARK 620 4 GLN A 135 O 90.4 158.8 81.9
REMARK 620 5 GLU A 140 OE1 112.7 123.2 144.1 77.9
REMARK 620 6 GLU A 140 OE2 82.9 76.7 156.8 121.2 52.6
REMARK 620 7 HOH A 509 O 167.7 87.5 80.5 101.0 74.6 94.9
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 A 504
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3DVJ RELATED DB: PDB
REMARK 900 RELATED ID: 3DVK RELATED DB: PDB
REMARK 900 RELATED ID: 3DVM RELATED DB: PDB
DBREF 3DVE A 1 148 UNP P62158 CALM_HUMAN 2 149
DBREF 3DVE B 1855 1875 UNP Q05152 CAC1B_RABIT 1855 1875
SEQADV 3DVE HIS B 1853 UNP Q05152 EXPRESSION TAG
SEQADV 3DVE MET B 1854 UNP Q05152 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 ASP 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 23 HIS MET GLY LYS VAL TYR ALA ALA LEU MET ILE PHE ASP
SEQRES 2 B 23 PHE TYR LYS GLN ASN LYS THR SER ARG ASP
HET CA A 501 1
HET CA A 502 1
HET CA A 503 1
HET CA A 504 1
HET NI A 505 1
HETNAM CA CALCIUM ION
HETNAM NI NICKEL (II) ION
FORMUL 3 CA 4(CA 2+)
FORMUL 7 NI NI 2+
FORMUL 8 HOH *78(H2 O)
HELIX 1 1 THR A 5 ASP A 20 1 16
HELIX 2 2 THR A 28 LEU A 39 1 12
HELIX 3 3 THR A 44 ASP A 56 1 13
HELIX 4 4 ASP A 64 LYS A 77 1 14
HELIX 5 5 GLU A 82 ASP A 93 1 12
HELIX 6 6 SER A 101 LEU A 112 1 12
HELIX 7 7 THR A 117 ASP A 129 1 13
HELIX 8 8 TYR A 138 MET A 145 1 8
HELIX 9 9 MET B 1854 ASN B 1870 1 17
SHEET 1 A 2 TYR A 99 ILE A 100 0
SHEET 2 A 2 VAL A 136 ASN A 137 -1 O VAL A 136 N ILE A 100
LINK OD1 ASP A 20 CA CA A 501 1555 1555 2.22
LINK OD1 ASP A 22 CA CA A 501 1555 1555 2.42
LINK OD2 ASP A 24 CA CA A 501 1555 1555 2.44
LINK O THR A 26 CA CA A 501 1555 1555 2.26
LINK OE1 GLU A 31 CA CA A 501 1555 1555 2.59
LINK OE2 GLU A 31 CA CA A 501 1555 1555 2.49
LINK OD2 ASP A 56 CA CA A 502 1555 1555 2.23
LINK OD2 ASP A 58 CA CA A 502 1555 1555 2.42
LINK OD1 ASN A 60 CA CA A 502 1555 1555 2.33
LINK O THR A 62 CA CA A 502 1555 1555 2.52
LINK OE1 GLU A 67 CA CA A 502 1555 1555 2.46
LINK OE2 GLU A 67 CA CA A 502 1555 1555 2.55
LINK OD2 ASP A 93 CA CA A 503 1555 1555 2.11
LINK OD1 ASP A 95 CA CA A 503 1555 1555 2.35
LINK OD1 ASN A 97 CA CA A 503 1555 1555 2.39
LINK O TYR A 99 CA CA A 503 1555 1555 2.32
LINK OE1 GLU A 104 CA CA A 503 1555 1555 2.44
LINK OE2 GLU A 104 CA CA A 503 1555 1555 2.69
LINK OD2 ASP A 129 CA CA A 504 1555 1555 2.39
LINK OD1 ASP A 131 CA CA A 504 1555 1555 2.38
LINK OD2 ASP A 133 CA CA A 504 1555 1555 2.37
LINK O GLN A 135 CA CA A 504 1555 1555 2.44
LINK OE1 GLU A 140 CA CA A 504 1555 1555 2.50
LINK OE2 GLU A 140 CA CA A 504 1555 1555 2.47
LINK CA CA A 501 O HOH A 524 1555 1555 2.40
LINK CA CA A 502 O HOH A 543 1555 1555 2.25
LINK CA CA A 503 O HOH A 535 1555 1555 2.51
LINK CA CA A 504 O HOH A 509 1555 1555 2.41
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 524
SITE 1 AC2 6 ASP A 56 ASP A 58 ASN A 60 THR A 62
SITE 2 AC2 6 GLU A 67 HOH A 543
SITE 1 AC3 6 ASP A 93 ASP A 95 ASN A 97 TYR A 99
SITE 2 AC3 6 GLU A 104 HOH A 535
SITE 1 AC4 6 ASP A 129 ASP A 131 ASP A 133 GLN A 135
SITE 2 AC4 6 GLU A 140 HOH A 509
CRYST1 40.303 40.303 344.652 90.00 90.00 120.00 P 61 2 2 12
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 0.024812 0.014325 0.000000 0.00000
SCALE2 0.000000 0.028650 0.000000 0.00000
SCALE3 0.000000 0.000000 0.002901 0.00000
(ATOM LINES ARE NOT SHOWN.)
END