HEADER TRANSPORT PROTEIN 06-MAR-17 5V2P
TITLE CAV BETA2A SUBUNIT: CAV1.2 AID-CAP COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: VOLTAGE-DEPENDENT L-TYPE CALCIUM CHANNEL SUBUNIT BETA-2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: BETA2A SUBUNIT (UNP RESIDUES 24-145,254-476);
COMPND 5 SYNONYM: CAB2, CALCIUM CHANNEL VOLTAGE-DEPENDENT SUBUNIT BETA 2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: VOLTAGE-DEPENDENT L-TYPE CALCIUM CHANNEL SUBUNIT ALPHA-1C;
COMPND 9 CHAIN: B;
COMPND 10 FRAGMENT: AID-CAP (UNP RESIDUES 427-445);
COMPND 11 SYNONYM: CALCIUM CHANNEL, L TYPE,ALPHA-1 POLYPEPTIDE, ISOFORM 1,
COMPND 12 CARDIAC MUSCLE, VOLTAGE-GATED CALCIUM CHANNEL SUBUNIT ALPHA CAV1.2;
COMPND 13 ENGINEERED: YES;
COMPND 14 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;
SOURCE 3 ORGANISM_COMMON: RAT;
SOURCE 4 ORGANISM_TAXID: 10116;
SOURCE 5 GENE: CACNB2, CACNLB2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606
KEYWDS ION CHANNEL, SIGNALING, CALCIUM, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR F.FINDEISEN,M.CAMPIGLIO,H.JO,C.H.RUMPF,L.POPE,B.FLUCHER,W.F.DEGRADO,
AUTHOR 2 D.L.MINOR
REVDAT 5 04-OCT-23 5V2P 1 LINK
REVDAT 4 04-DEC-19 5V2P 1 REMARK
REVDAT 3 13-SEP-17 5V2P 1 REMARK
REVDAT 2 23-AUG-17 5V2P 1 REMARK
REVDAT 1 19-JUL-17 5V2P 0
JRNL AUTH F.FINDEISEN,M.CAMPIGLIO,H.JO,F.ABDEREMANE-ALI,C.H.RUMPF,
JRNL AUTH 2 L.POPE,N.D.ROSSEN,B.E.FLUCHER,W.F.DEGRADO,D.L.MINOR
JRNL TITL STAPLED VOLTAGE-GATED CALCIUM CHANNEL (CAV)
JRNL TITL 2 ALPHA-INTERACTION DOMAIN (AID) PEPTIDES ACT AS SELECTIVE
JRNL TITL 3 PROTEIN-PROTEIN INTERACTION INHIBITORS OF CAV FUNCTION.
JRNL REF ACS CHEM NEUROSCI V. 8 1313 2017
JRNL REFN ESSN 1948-7193
JRNL PMID 28278376
JRNL DOI 10.1021/ACSCHEMNEURO.6B00454
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0049
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
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) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 25636
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.230
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1388
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1812
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 95.65
REMARK 3 BIN R VALUE (WORKING SET) : 0.3600
REMARK 3 BIN FREE R VALUE SET COUNT : 99
REMARK 3 BIN FREE R VALUE : 0.3800
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2366
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 41
REMARK 3 SOLVENT ATOMS : 374
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.38
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.03000
REMARK 3 B22 (A**2) : -1.03000
REMARK 3 B33 (A**2) : 3.35000
REMARK 3 B12 (A**2) : -0.52000
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): 0.165
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.155
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 : 0.970
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.949
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2454 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2377 ; 0.000 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3315 ; 1.193 ; 1.976
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5458 ; 3.947 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 302 ; 5.798 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 107 ;36.246 ;24.393
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 405 ;14.206 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;13.461 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 376 ; 0.064 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2728 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 530 ; 0.022 ; 0.020
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): 1220 ; 1.927 ; 4.139
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1219 ; 1.925 ; 4.138
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1518 ; 3.151 ; 6.182
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1519 ; 3.151 ; 6.183
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1234 ; 2.320 ; 4.366
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1234 ; 2.320 ; 4.366
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1797 ; 3.811 ; 6.416
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2845 ; 6.550 ;34.013
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2719 ; 6.324 ;32.862
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 : NULL
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 5V2P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1000225260.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-NOV-12
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 6.3
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 : SI(111) DOUBLE CRYSTAL KHOZU
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 S 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM 7.0.4
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.20
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 23913
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 53.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 86.6
REMARK 200 DATA REDUNDANCY : 1.300
REMARK 200 R MERGE (I) : 0.10900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.9000
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) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.1
REMARK 200 DATA REDUNDANCY IN SHELL : 1.40
REMARK 200 R MERGE FOR SHELL (I) : 1.93700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.1
REMARK 200 STARTING MODEL: PDB ENTRY 1T3S
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 34-37% PEG400, 0.1 M MAGNESIUM
REMARK 280 CHLORIDE, 0.1 M MES, PH 6.3, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.90250
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 23.61507
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 54.42367
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 40.90250
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 23.61507
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 54.42367
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 40.90250
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 23.61507
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 54.42367
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 47.23014
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 108.84733
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 47.23014
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 108.84733
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 47.23014
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 108.84733
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: 2230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 16260 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 NI NI A 501 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 789 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 623 LIES ON A SPECIAL POSITION.
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 GLY A 67
REMARK 465 SER A 68
REMARK 465 ALA A 69
REMARK 465 ASP A 70
REMARK 465 SER A 71
REMARK 465 TYR A 72
REMARK 465 THR A 73
REMARK 465 SER A 74
REMARK 465 ARG A 75
REMARK 465 PRO A 76
REMARK 465 SER A 77
REMARK 465 ASP A 78
REMARK 465 SER A 79
REMARK 465 ASP A 80
REMARK 465 VAL A 81
REMARK 465 GLY A 252
REMARK 465 SER A 253
REMARK 465 SER A 254
REMARK 465 LYS A 255
REMARK 465 GLU A 256
REMARK 465 LYS A 257
REMARK 465 ARG A 258
REMARK 465 MET A 259
REMARK 465 PRO A 260
REMARK 465 PHE A 261
REMARK 465 PHE A 262
REMARK 465 LYS A 263
REMARK 465 LYS A 264
REMARK 465 THR A 265
REMARK 465 GLU A 266
REMARK 465 ARG A 326
REMARK 465 SER A 327
REMARK 465 VAL A 328
REMARK 465 LEU A 329
REMARK 465 ASN A 330
REMARK 465 ASN A 331
REMARK 465 PRO A 332
REMARK 465 SER A 333
REMARK 465 LYS A 334
REMARK 465 HIS A 335
REMARK 465 ALA A 336
REMARK 465 ILE A 337
REMARK 465 ILE A 338
REMARK 465 GLU A 339
REMARK 465 ARG A 340
REMARK 465 SER A 341
REMARK 465 ASN A 342
REMARK 465 THR A 343
REMARK 465 ARG A 344
REMARK 465 SER A 466
REMARK 465 ASN A 467
REMARK 465 LEU A 468
REMARK 465 PRO A 469
REMARK 465 ASN A 470
REMARK 465 PRO A 471
REMARK 465 LEU A 472
REMARK 465 LEU A 473
REMARK 465 SER A 474
REMARK 465 ARG A 475
REMARK 465 THR A 476
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 SER A 82 CB OG
REMARK 470 SER A 83 OG
REMARK 470 GLU A 85 CG CD OE1 OE2
REMARK 470 GLU A 86 CG CD OE1 OE2
REMARK 470 GLN A 125 CG CD OE1 NE2
REMARK 470 GLU A 176 CG CD OE1 OE2
REMARK 470 ARG A 179 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 187 CG CD CE NZ
REMARK 470 HIS A 267 CG ND1 CD2 CE1 NE2
REMARK 470 THR A 268 OG1 CG2
REMARK 470 LYS A 325 CG CD CE NZ
REMARK 470 SER A 345 OG
REMARK 470 SER A 346 OG
REMARK 470 LEU A 347 CG CD1 CD2
REMARK 470 SER A 381 OG
REMARK 470 LYS A 382 CG CD CE NZ
REMARK 470 LYS A 405 CG CD CE NZ
REMARK 470 LYS A 409 CG CD CE NZ
REMARK 470 LYS A 413 CE NZ
REMARK 470 GLU A 432 CG CD OE1 OE2
REMARK 470 GLU B 445 CG CD OE1 OE2
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 HOH A 782 O HOH A 827 1.67
REMARK 500 O HOH A 810 O HOH A 895 2.09
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 128 70.26 62.61
REMARK 500 SER A 286 -139.82 -136.24
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 918 DISTANCE = 5.91 ANGSTROMS
REMARK 525 HOH A 919 DISTANCE = 5.94 ANGSTROMS
REMARK 525 HOH A 920 DISTANCE = 5.98 ANGSTROMS
REMARK 525 HOH A 921 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH A 922 DISTANCE = 6.03 ANGSTROMS
REMARK 525 HOH A 923 DISTANCE = 6.23 ANGSTROMS
REMARK 525 HOH A 924 DISTANCE = 6.38 ANGSTROMS
REMARK 525 HOH A 925 DISTANCE = 6.39 ANGSTROMS
REMARK 525 HOH A 926 DISTANCE = 6.39 ANGSTROMS
REMARK 525 HOH A 927 DISTANCE = 6.59 ANGSTROMS
REMARK 525 HOH A 928 DISTANCE = 6.75 ANGSTROMS
REMARK 525 HOH A 929 DISTANCE = 6.79 ANGSTROMS
REMARK 525 HOH A 930 DISTANCE = 6.86 ANGSTROMS
REMARK 525 HOH A 931 DISTANCE = 6.86 ANGSTROMS
REMARK 525 HOH A 932 DISTANCE = 6.90 ANGSTROMS
REMARK 525 HOH A 933 DISTANCE = 6.95 ANGSTROMS
REMARK 525 HOH A 934 DISTANCE = 7.49 ANGSTROMS
REMARK 525 HOH A 935 DISTANCE = 7.49 ANGSTROMS
REMARK 525 HOH A 936 DISTANCE = 7.53 ANGSTROMS
REMARK 525 HOH A 937 DISTANCE = 7.65 ANGSTROMS
REMARK 525 HOH A 938 DISTANCE = 7.76 ANGSTROMS
REMARK 525 HOH A 939 DISTANCE = 7.82 ANGSTROMS
REMARK 525 HOH A 940 DISTANCE = 8.62 ANGSTROMS
REMARK 525 HOH A 941 DISTANCE = 8.73 ANGSTROMS
REMARK 525 HOH A 942 DISTANCE = 9.12 ANGSTROMS
REMARK 525 HOH A 943 DISTANCE = 9.44 ANGSTROMS
REMARK 525 HOH A 944 DISTANCE = 9.48 ANGSTROMS
REMARK 525 HOH A 945 DISTANCE = 9.55 ANGSTROMS
REMARK 525 HOH A 946 DISTANCE = 10.08 ANGSTROMS
REMARK 525 HOH A 947 DISTANCE = 10.86 ANGSTROMS
REMARK 525 HOH A 948 DISTANCE = 10.99 ANGSTROMS
REMARK 525 HOH A 949 DISTANCE = 11.30 ANGSTROMS
REMARK 525 HOH B 621 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH B 622 DISTANCE = 6.57 ANGSTROMS
REMARK 525 HOH B 623 DISTANCE = 7.88 ANGSTROMS
REMARK 525 HOH B 624 DISTANCE = 8.01 ANGSTROMS
REMARK 525 HOH B 625 DISTANCE = 10.03 ANGSTROMS
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 NI A 501 NI
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 306 NE2
REMARK 620 2 HIS A 306 NE2 0.0
REMARK 620 3 HOH A 703 O 88.9 88.9
REMARK 620 4 HOH A 703 O 168.9 168.9 80.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NI A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8VY B 501
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5V2Q RELATED DB: PDB
DBREF 5V2P A 67 252 UNP Q8VGC3 CACB2_RAT 24 145
DBREF 5V2P A 254 476 UNP Q8VGC3 CACB2_RAT 254 476
DBREF 5V2P B 427 445 UNP Q13936 CAC1C_HUMAN 427 445
SEQADV 5V2P SER A 82 UNP Q8VGC3 INSERTION
SEQADV 5V2P SER A 253 UNP Q8VGC3 LINKER
SEQADV 5V2P CYS B 427 UNP Q13936 LYS 427 ENGINEERED MUTATION
SEQADV 5V2P SER B 428 UNP Q13936 GLN 428 ENGINEERED MUTATION
SEQADV 5V2P PRO B 429 UNP Q13936 GLN 429 ENGINEERED MUTATION
SEQADV 5V2P CYS B 432 UNP Q13936 GLU 432 ENGINEERED MUTATION
SEQRES 1 A 347 GLY SER ALA ASP SER TYR THR SER ARG PRO SER ASP SER
SEQRES 2 A 347 ASP VAL SER SER LEU GLU GLU ASP ARG GLU ALA VAL ARG
SEQRES 3 A 347 ARG GLU ALA GLU ARG GLN ALA GLN ALA GLN LEU GLU LYS
SEQRES 4 A 347 ALA LYS THR LYS PRO VAL ALA PHE ALA VAL ARG THR ASN
SEQRES 5 A 347 VAL ARG TYR SER ALA ALA GLN GLU ASP ASP VAL PRO VAL
SEQRES 6 A 347 PRO GLY MET ALA ILE SER PHE GLU ALA LYS ASP PHE LEU
SEQRES 7 A 347 HIS VAL LYS GLU LYS PHE ASN ASN ASP TRP TRP ILE GLY
SEQRES 8 A 347 ARG LEU VAL LYS GLU GLY CYS GLU ILE GLY PHE ILE PRO
SEQRES 9 A 347 SER PRO VAL LYS LEU GLU ASN MET ARG LEU GLN HIS GLU
SEQRES 10 A 347 GLN ARG ALA LYS GLN GLY SER SER LYS GLU LYS ARG MET
SEQRES 11 A 347 PRO PHE PHE LYS LYS THR GLU HIS THR PRO PRO TYR ASP
SEQRES 12 A 347 VAL VAL PRO SER MET ARG PRO VAL VAL LEU VAL GLY PRO
SEQRES 13 A 347 SER LEU LYS GLY TYR GLU VAL THR ASP MET MET GLN LYS
SEQRES 14 A 347 ALA LEU PHE ASP PHE LEU LYS HIS ARG PHE GLU GLY ARG
SEQRES 15 A 347 ILE SER ILE THR ARG VAL THR ALA ASP ILE SER LEU ALA
SEQRES 16 A 347 LYS ARG SER VAL LEU ASN ASN PRO SER LYS HIS ALA ILE
SEQRES 17 A 347 ILE GLU ARG SER ASN THR ARG SER SER LEU ALA GLU VAL
SEQRES 18 A 347 GLN SER GLU ILE GLU ARG ILE PHE GLU LEU ALA ARG THR
SEQRES 19 A 347 LEU GLN LEU VAL VAL LEU ASP ALA ASP THR ILE ASN HIS
SEQRES 20 A 347 PRO ALA GLN LEU SER LYS THR SER LEU ALA PRO ILE ILE
SEQRES 21 A 347 VAL TYR VAL LYS ILE SER SER PRO LYS VAL LEU GLN ARG
SEQRES 22 A 347 LEU ILE LYS SER ARG GLY LYS SER GLN ALA LYS HIS LEU
SEQRES 23 A 347 ASN VAL GLN MET VAL ALA ALA ASP LYS LEU ALA GLN CYS
SEQRES 24 A 347 PRO PRO GLN GLU SER PHE ASP VAL ILE LEU ASP GLU ASN
SEQRES 25 A 347 GLN LEU GLU ASP ALA CYS GLU HIS LEU ALA ASP TYR LEU
SEQRES 26 A 347 GLU ALA TYR TRP LYS ALA THR HIS PRO PRO SER SER ASN
SEQRES 27 A 347 LEU PRO ASN PRO LEU LEU SER ARG THR
SEQRES 1 B 19 CYS SER PRO LEU GLU CYS ASP LEU LYS GLY TYR LEU ASP
SEQRES 2 B 19 TRP ILE THR GLN ALA GLU
HET NI A 501 1
HET 1PE A 502 16
HET 1PE A 503 16
HET 8VY B 501 8
HETNAM NI NICKEL (II) ION
HETNAM 1PE PENTAETHYLENE GLYCOL
HETNAM 8VY 1,3-BIS(BROMOMETHYL)BENZENE
HETSYN 1PE PEG400
HETSYN 8VY ALPHA,ALPHA'-DIBROMO-M-XYLENE
FORMUL 3 NI NI 2+
FORMUL 4 1PE 2(C10 H22 O6)
FORMUL 6 8VY C8 H8 BR2
FORMUL 7 HOH *374(H2 O)
HELIX 1 AA1 LEU A 84 LYS A 107 1 24
HELIX 2 AA2 ALA A 124 ASP A 128 5 5
HELIX 3 AA3 SER A 171 GLN A 188 1 18
HELIX 4 AA4 TYR A 290 PHE A 308 1 19
HELIX 5 AA5 ASP A 320 ALA A 324 5 5
HELIX 6 AA6 SER A 346 ARG A 362 1 17
HELIX 7 AA7 HIS A 376 SER A 381 5 6
HELIX 8 AA8 SER A 396 ARG A 407 1 12
HELIX 9 AA9 GLY A 408 LYS A 413 1 6
HELIX 10 AB1 HIS A 414 GLN A 427 1 14
HELIX 11 AB2 PRO A 429 PHE A 434 1 6
HELIX 12 AB3 GLN A 442 HIS A 462 1 21
HELIX 13 AB4 SER B 428 GLU B 445 1 18
SHEET 1 AA1 5 GLY A 167 PRO A 170 0
SHEET 2 AA1 5 TRP A 154 LEU A 159 -1 N TRP A 155 O ILE A 169
SHEET 3 AA1 5 PHE A 143 LYS A 149 -1 N GLU A 148 O ILE A 156
SHEET 4 AA1 5 PHE A 113 THR A 117 -1 N PHE A 113 O VAL A 146
SHEET 5 AA1 5 TYR A 271 VAL A 274 -1 O ASP A 272 N ARG A 116
SHEET 1 AA2 5 ILE A 312 VAL A 317 0
SHEET 2 AA2 5 LEU A 366 ALA A 371 1 O LEU A 366 N SER A 313
SHEET 3 AA2 5 VAL A 280 VAL A 283 1 N VAL A 280 O LEU A 369
SHEET 4 AA2 5 ILE A 388 VAL A 392 1 O VAL A 390 N VAL A 283
SHEET 5 AA2 5 VAL A 436 LEU A 438 1 O VAL A 436 N TYR A 391
LINK SG CYS B 427 C1' 8VY B 501 1555 1555 1.82
LINK SG CYS B 432 C3' 8VY B 501 1555 1555 1.82
LINK NE2 HIS A 306 NI NI A 501 1555 1555 2.18
LINK NE2 HIS A 306 NI NI A 501 1555 2655 2.18
LINK NI NI A 501 O HOH A 703 1555 1555 2.10
LINK NI NI A 501 O HOH A 703 1555 2655 2.10
CISPEP 1 GLY A 284 PRO A 285 0 -0.65
SITE 1 AC1 2 HIS A 306 HOH A 703
SITE 1 AC2 9 PHE A 113 LYS A 147 GLU A 148 LYS A 149
SITE 2 AC2 9 ASN A 152 ASP A 153 TRP A 155 VAL A 173
SITE 3 AC2 9 HOH A 670
SITE 1 AC3 4 ALA A 299 ASP A 302 LYS A 305 HIS A 306
SITE 1 AC4 4 SER A 352 GLU A 359 CYS B 427 CYS B 432
CRYST1 81.805 81.805 163.271 90.00 90.00 120.00 H 3 9
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 0.012224 0.007058 0.000000 0.00000
SCALE2 0.000000 0.014115 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006125 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
