HEADER TRANSPORT PROTEIN 27-APR-04 1T3S
TITLE STRUCTURAL ANALYSIS OF THE VOLTAGE-DEPENDENT CALCIUM CHANNEL BETA
TITLE 2 SUBUNIT FUNCTIONAL CORE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: DIHYDROPYRIDINE-SENSITIVE L-TYPE, CALCIUM CHANNEL BETA-2
COMPND 3 SUBUNIT;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: FUNCTIONAL CORE (RESIDUES 25-422);
COMPND 6 SYNONYM: VOLTAGE-DEPENDENT CALCIUM CHANNEL BETA-2 SUBUNIT, CAB2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS;
SOURCE 3 ORGANISM_COMMON: RABBIT;
SOURCE 4 ORGANISM_TAXID: 9986;
SOURCE 5 GENE: CACNB2, CACNLB2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET21
KEYWDS SH3 DOMAIN, GUANYLATE KINASE DOMAIN, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.OPATOWSKY,C.-C.CHEN,K.P.CAMPBELL,J.A.HIRSCH
REVDAT 7 03-APR-24 1T3S 1 REMARK
REVDAT 6 14-FEB-24 1T3S 1 REMARK
REVDAT 5 27-OCT-21 1T3S 1 REMARK SEQADV
REVDAT 4 23-AUG-17 1T3S 1 SOURCE
REVDAT 3 12-FEB-14 1T3S 1 JRNL VERSN
REVDAT 2 24-FEB-09 1T3S 1 VERSN
REVDAT 1 25-MAY-04 1T3S 0
JRNL AUTH Y.OPATOWSKY,C.C.CHEN,K.P.CAMPBELL,J.A.HIRSCH
JRNL TITL STRUCTURAL ANALYSIS OF THE VOLTAGE-DEPENDENT CALCIUM CHANNEL
JRNL TITL 2 BETA SUBUNIT FUNCTIONAL CORE AND ITS COMPLEX WITH THE ALPHA
JRNL TITL 3 1 INTERACTION DOMAIN.
JRNL REF NEURON V. 42 387 2004
JRNL REFN ISSN 0896-6273
JRNL PMID 15134636
JRNL DOI 10.1093/HMG/DDH162
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.OPATOWSKY,O.CHOMSKY-HECHT,J.A.HIRSCH
REMARK 1 TITL EXPRESSION, PURIFICATION AND CRYSTALLIZATION OF A FUNCTIONAL
REMARK 1 TITL 2 CORE OF THE VOLTAGE-DEPENDENT CALCIUM CHANNEL BETA SUBUNIT
REMARK 1 REF TO BE PUBLISHED
REMARK 1 REFN
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 81.65
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.8
REMARK 3 NUMBER OF REFLECTIONS : 17294
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) : 0.262
REMARK 3 R VALUE (WORKING SET) : 0.261
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 935
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) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1168
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.3770
REMARK 3 BIN FREE R VALUE SET COUNT : 70
REMARK 3 BIN FREE R VALUE : 0.3430
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2282
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 87
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 57.76
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -3.86000
REMARK 3 B22 (A**2) : 5.23000
REMARK 3 B33 (A**2) : -1.37000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.346
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.246
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.926
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.912
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2327 ; 0.008 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2148 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3159 ; 1.536 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4994 ; 3.506 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 291 ; 1.213 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 365 ; 0.108 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2580 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 449 ; 0.006 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 652 ; 0.241 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2542 ; 0.302 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1174 ; 0.109 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 78 ; 0.161 ; 0.200
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): 9 ; 0.167 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 35 ; 0.267 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 2 ; 0.039 ; 0.200
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): 1476 ; 1.559 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2377 ; 2.705 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 851 ; 2.323 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 782 ; 3.492 ; 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 : NULL
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 : 1.40
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 1T3S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-04.
REMARK 100 THE DEPOSITION ID IS D_1000022275.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-JUL-02
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9333
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18271
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : NULL
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.04800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.31000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: MODEL BUILT FROM EARLIER MAD DATA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 20K, BICINE, SODIUM CHLORIDE, BETA
REMARK 280 -MERCAPTOETHANOL, MPD, PH 9, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+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 37.03300
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 81.92050
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.03300
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 81.92050
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: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 SER A 25
REMARK 465 ARG A 26
REMARK 465 PRO A 27
REMARK 465 SER A 28
REMARK 465 ASP A 29
REMARK 465 SER A 30
REMARK 465 ASP A 31
REMARK 465 VAL A 32
REMARK 465 SER A 33
REMARK 465 LEU A 34
REMARK 465 HIS A 203
REMARK 465 SER A 204
REMARK 465 LYS A 205
REMARK 465 GLU A 206
REMARK 465 LYS A 207
REMARK 465 ARG A 208
REMARK 465 MET A 209
REMARK 465 PRO A 210
REMARK 465 PHE A 211
REMARK 465 PHE A 212
REMARK 465 LYS A 213
REMARK 465 LYS A 214
REMARK 465 THR A 215
REMARK 465 GLU A 216
REMARK 465 HIS A 217
REMARK 465 PRO A 282
REMARK 465 SER A 283
REMARK 465 LYS A 284
REMARK 465 HIS A 285
REMARK 465 ALA A 286
REMARK 465 ILE A 287
REMARK 465 ILE A 288
REMARK 465 GLU A 289
REMARK 465 ARG A 290
REMARK 465 SER A 291
REMARK 465 ASN A 292
REMARK 465 ASN A 416
REMARK 465 LEU A 417
REMARK 465 PRO A 418
REMARK 465 ASN A 419
REMARK 465 PRO A 420
REMARK 465 LEU A 421
REMARK 465 LEU A 422
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 ASP A 37 CG OD1 OD2
REMARK 470 ARG A 38 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 39 CG CD OE1 OE2
REMARK 470 VAL A 41 CG1 CG2
REMARK 470 ARG A 43 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 55 CG CD CE NZ
REMARK 470 ASP A 77 CG OD1 OD2
REMARK 470 ASP A 78 CG OD1 OD2
REMARK 470 LYS A 111 CG CD CE NZ
REMARK 470 LYS A 137 CD CE NZ
REMARK 470 LYS A 140 CG CD CE NZ
REMARK 470 LYS A 332 CD CE NZ
REMARK 470 LYS A 348 CG CD CE NZ
REMARK 470 ARG A 352 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 359 CG CD CE NZ
REMARK 470 LYS A 363 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 412 C - N - CA ANGL. DEV. = 9.2 DEGREES
REMARK 500 PRO A 412 C - N - CD ANGL. DEV. = -15.7 DEGREES
REMARK 500 PRO A 413 C - N - CA ANGL. DEV. = 9.9 DEGREES
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 ASP A 77 -154.47 -106.77
REMARK 500 PRO A 82 125.56 -36.70
REMARK 500 SER A 236 -147.59 -135.89
REMARK 500 TYR A 240 -131.21 -94.51
REMARK 500 GLU A 241 -47.73 -132.41
REMARK 500 ARG A 261 21.42 -145.26
REMARK 500 ALA A 274 36.42 -75.19
REMARK 500 ARG A 294 -93.27 -63.50
REMARK 500 SER A 356 20.09 -66.45
REMARK 500 GLN A 361 -28.45 -151.30
REMARK 500 VAL A 367 3.64 -65.25
REMARK 500 ASP A 388 58.80 -118.74
REMARK 500 HIS A 411 -96.18 -122.33
REMARK 500 PRO A 412 159.69 32.38
REMARK 500 PRO A 413 128.55 -2.49
REMARK 500 SER A 414 41.78 76.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HG A 1
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1T3L RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE OF THE PROTEIN IS FROM
REMARK 999 SWISSPROT P54288, ISOFORM 2A.
REMARK 999 RESIDUES 138-141 IN THE COORDINATES WERE
REMARK 999 INTRODUCED INTO THE PROTEIN. THEY REPLACE
REMARK 999 RESIDUES 138-202 FROM THE NATIVE SEQUENCE.
DBREF 1T3S A 25 137 UNP P54288 CACB2_RABIT 25 137
DBREF 1T3S A 203 422 UNP P54288 CACB2_RABIT 203 422
SEQADV 1T3S ARG A 122 UNP P54288 PRO 122 ENGINEERED MUTATION
SEQADV 1T3S GLU A 138 UNP P54288 SEE REMARK 999
SEQADV 1T3S PHE A 139 UNP P54288 SEE REMARK 999
SEQADV 1T3S LYS A 140 UNP P54288 SEE REMARK 999
SEQADV 1T3S LEU A 141 UNP P54288 SEE REMARK 999
SEQRES 1 A 337 SER ARG PRO SER ASP SER ASP VAL SER LEU GLU GLU ASP
SEQRES 2 A 337 ARG GLU ALA VAL ARG ARG GLU ALA GLU ARG GLN ALA GLN
SEQRES 3 A 337 ALA GLN LEU GLU LYS ALA LYS THR LYS PRO VAL ALA PHE
SEQRES 4 A 337 ALA VAL ARG THR ASN VAL SER TYR SER ALA ALA HIS GLU
SEQRES 5 A 337 ASP ASP VAL PRO VAL PRO GLY MET ALA ILE SER PHE GLU
SEQRES 6 A 337 ALA LYS ASP PHE LEU HIS VAL LYS GLU LYS PHE ASN ASN
SEQRES 7 A 337 ASP TRP TRP ILE GLY ARG LEU VAL LYS GLU GLY CYS GLU
SEQRES 8 A 337 ILE GLY PHE ILE PRO SER ARG VAL LYS LEU GLU ASN MET
SEQRES 9 A 337 ARG LEU GLN HIS GLU GLN ARG ALA LYS GLU PHE LYS LEU
SEQRES 10 A 337 HIS SER LYS GLU LYS ARG MET PRO PHE PHE LYS LYS THR
SEQRES 11 A 337 GLU HIS THR PRO PRO TYR ASP VAL VAL PRO SER MET ARG
SEQRES 12 A 337 PRO VAL VAL LEU VAL GLY PRO SER LEU LYS GLY TYR GLU
SEQRES 13 A 337 VAL THR ASP MET MET GLN LYS ALA LEU PHE ASP PHE LEU
SEQRES 14 A 337 LYS HIS ARG PHE GLU GLY ARG ILE SER ILE THR ARG VAL
SEQRES 15 A 337 THR ALA ASP ILE SER LEU ALA LYS ARG SER VAL LEU ASN
SEQRES 16 A 337 ASN PRO SER LYS HIS ALA ILE ILE GLU ARG SER ASN THR
SEQRES 17 A 337 ARG SER SER LEU ALA GLU VAL GLN SER GLU ILE GLU ARG
SEQRES 18 A 337 ILE PHE GLU LEU ALA ARG THR LEU GLN LEU VAL VAL LEU
SEQRES 19 A 337 ASP ALA ASP THR ILE ASN HIS PRO ALA GLN LEU SER LYS
SEQRES 20 A 337 THR SER LEU ALA PRO ILE VAL VAL TYR VAL LYS ILE SER
SEQRES 21 A 337 SER PRO LYS VAL LEU GLN ARG LEU ILE LYS SER ARG GLY
SEQRES 22 A 337 LYS SER GLN ALA LYS HIS LEU ASN VAL GLN MET VAL ALA
SEQRES 23 A 337 ALA ASP LYS LEU ALA GLN CYS PRO PRO GLU LEU PHE ASP
SEQRES 24 A 337 VAL ILE LEU ASP GLU ASN GLN LEU GLU ASP ALA CYS GLU
SEQRES 25 A 337 HIS LEU ALA ASP TYR LEU GLU ALA TYR TRP LYS ALA THR
SEQRES 26 A 337 HIS PRO PRO SER SER ASN LEU PRO ASN PRO LEU LEU
HET HG A 1 1
HETNAM HG MERCURY (II) ION
FORMUL 2 HG HG 2+
FORMUL 3 HOH *87(H2 O)
HELIX 1 1 ASP A 37 ALA A 56 1 20
HELIX 2 2 SER A 121 PHE A 139 1 19
HELIX 3 3 GLU A 241 PHE A 258 1 18
HELIX 4 4 ASP A 270 ALA A 274 5 5
HELIX 5 5 LYS A 275 ASN A 280 1 6
HELIX 6 6 SER A 296 ARG A 312 1 17
HELIX 7 7 HIS A 326 SER A 331 5 6
HELIX 8 8 SER A 346 SER A 356 1 11
HELIX 9 9 GLY A 358 LYS A 363 1 6
HELIX 10 10 LEU A 365 CYS A 378 1 14
HELIX 11 11 PRO A 379 PHE A 383 5 5
HELIX 12 12 GLN A 391 HIS A 411 1 21
SHEET 1 A 5 GLY A 117 PRO A 120 0
SHEET 2 A 5 TRP A 104 LEU A 109 -1 N TRP A 105 O ILE A 119
SHEET 3 A 5 PHE A 93 LYS A 99 -1 N GLU A 98 O ILE A 106
SHEET 4 A 5 PHE A 63 THR A 67 -1 N PHE A 63 O VAL A 96
SHEET 5 A 5 TYR A 221 VAL A 224 -1 O VAL A 224 N ALA A 64
SHEET 1 B 5 ILE A 262 VAL A 267 0
SHEET 2 B 5 LEU A 316 ALA A 321 1 O ASP A 320 N VAL A 267
SHEET 3 B 5 VAL A 230 VAL A 233 1 N VAL A 230 O LEU A 319
SHEET 4 B 5 ILE A 338 VAL A 342 1 O VAL A 340 N VAL A 231
SHEET 5 B 5 VAL A 385 LEU A 387 1 O LEU A 387 N TYR A 341
LINK HG HG A 1 SG CYS A 114 1555 1555 2.75
CISPEP 1 THR A 218 PRO A 219 0 -0.76
CISPEP 2 GLY A 234 PRO A 235 0 -1.20
SITE 1 AC1 1 CYS A 114
CRYST1 74.066 163.841 34.761 90.00 90.00 90.00 P 21 21 2 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 0.013501 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006103 0.000000 0.00000
SCALE3 0.000000 0.000000 0.028768 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
