HEADER CALCIUM-BINDING PROTEIN 01-FEB-12 4DJC
TITLE 1.35 A CRYSTAL STRUCTURE OF THE NAV1.5 DIII-IV-CA/CAM 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: SODIUM CHANNEL PROTEIN TYPE 5 SUBUNIT ALPHA;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: HH1, SODIUM CHANNEL PROTEIN CARDIAC MUSCLE SUBUNIT ALPHA,
COMPND 10 SODIUM CHANNEL PROTEIN TYPE V SUBUNIT ALPHA, VOLTAGE-GATED SODIUM
COMPND 11 CHANNEL SUBUNIT ALPHA NAV1.5;
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, CALM2, CAM2, CAMB, CALM3, CALML2,
SOURCE 6 CAM3, CAMC, CAMIII;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: SCN5A;
SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS EF-HAND, CALCIUM-BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR M.F.SARHAN,C.-C.TUNG,F.VAN PETEGEM,C.A.AHERN
REVDAT 4 28-FEB-24 4DJC 1 REMARK SEQADV LINK
REVDAT 3 24-JAN-18 4DJC 1 AUTHOR
REVDAT 2 21-MAR-12 4DJC 1 JRNL
REVDAT 1 22-FEB-12 4DJC 0
JRNL AUTH M.F.SARHAN,C.C.TUNG,F.VAN PETEGEM,C.A.AHERN
JRNL TITL CRYSTALLOGRAPHIC BASIS FOR CALCIUM REGULATION OF SODIUM
JRNL TITL 2 CHANNELS.
JRNL REF PROC.NATL.ACAD.SCI.USA V. 109 3558 2012
JRNL REFN ISSN 0027-8424
JRNL PMID 22331908
JRNL DOI 10.1073/PNAS.1114748109
REMARK 2
REMARK 2 RESOLUTION. 1.35 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 1.35
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.55
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 42422
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) : 0.154
REMARK 3 R VALUE (WORKING SET) : 0.153
REMARK 3 FREE R VALUE : 0.176
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2234
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) : 1.35
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.39
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2834
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.2660
REMARK 3 BIN FREE R VALUE SET COUNT : 150
REMARK 3 BIN FREE R VALUE : 0.2830
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1256
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 161
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.79
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.67000
REMARK 3 B22 (A**2) : 2.25000
REMARK 3 B33 (A**2) : -0.58000
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): 0.049
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.046
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.032
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.787
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.973
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.966
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1402 ; 0.018 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 923 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1901 ; 1.620 ; 1.979
REMARK 3 BOND ANGLES OTHERS (DEGREES): 2288 ; 1.097 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 193 ; 4.532 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 72 ;30.039 ;26.806
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 261 ;11.330 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 5 ; 9.713 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 212 ; 0.111 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1597 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 256 ; 0.002 ; 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): 863 ; 1.960 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 353 ; 1.271 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1392 ; 2.925 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 539 ; 4.244 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 495 ; 6.280 ; 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): 2325 ; 1.997 ; 3.000
REMARK 3 SPHERICITY; FREE ATOMS (A**2): 165 ;10.290 ; 3.000
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 2305 ; 7.621 ; 3.000
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 4DJC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-FEB-12.
REMARK 100 THE DEPOSITION ID IS D_1000070401.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-SEP-10
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 : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9749
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX300HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS, XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44657
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.350
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.35
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.38
REMARK 200 COMPLETENESS FOR SHELL (%) : 92.6
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 : 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 (%): 47.79
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, 60% ISOPROPANOL, PH 6.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 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 14.19000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 48.50500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.36000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 48.50500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 14.19000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.36000
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1450 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9980 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 SER A -2
REMARK 465 SER B 1488
REMARK 465 GLY B 1502
REMARK 465 SER B 1503
REMARK 465 LYS B 1504
REMARK 465 LYS B 1505
REMARK 465 PRO B 1506
REMARK 465 GLN B 1507
REMARK 465 LYS B 1508
REMARK 465 PRO B 1509
REMARK 465 ILE B 1510
REMARK 465 PRO B 1511
REMARK 465 ARG B 1512
REMARK 465 PRO B 1513
REMARK 465 LEU B 1514
REMARK 465 ASN B 1515
REMARK 465 LYS B 1516
REMARK 465 TYR B 1517
REMARK 465 GLN B 1518
REMARK 465 GLY B 1519
REMARK 465 PHE B 1520
REMARK 465 ILE B 1521
REMARK 465 PHE B 1522
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 ASN A -1 CG OD1 ND2
REMARK 470 MET A 1 CG SD CE
REMARK 470 ASP A 3 CG OD1 OD2
REMARK 470 THR A 6 OG1 CG2
REMARK 470 GLU A 7 CG CD OE1 OE2
REMARK 470 GLU A 8 CG CD OE1 OE2
REMARK 470 GLU A 12 CG CD OE1 OE2
REMARK 470 GLU A 15 CG CD OE1 OE2
REMARK 470 ARG A 75 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 78 CG CD CE NZ
REMARK 470 LYS A 149 CG CD CE NZ
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 418 O HOH A 450 1.90
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O ASP A 59 O HOH A 418 4445 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 140 CG GLU A 140 CD 0.092
REMARK 500
REMARK 500 REMARK: NULL
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 ASP A 25 CB - CG - OD2 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ARG A 127 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG A 127 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
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 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 21 OD1
REMARK 620 2 ASP A 23 OD1 77.9
REMARK 620 3 ASP A 25 OD2 86.0 80.2
REMARK 620 4 THR A 27 O 83.1 155.4 83.1
REMARK 620 5 GLU A 32 OE2 97.4 75.5 154.1 122.8
REMARK 620 6 GLU A 32 OE1 113.2 127.4 147.9 74.6 52.6
REMARK 620 7 HOH A 346 O 158.1 81.4 83.6 114.5 84.1 85.1
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 57 OD2
REMARK 620 2 ASP A 59 OD1 81.8
REMARK 620 3 ASN A 61 OD1 90.9 76.8
REMARK 620 4 THR A 63 O 87.1 153.0 78.9
REMARK 620 5 GLU A 68 OE1 103.2 126.3 154.0 80.1
REMARK 620 6 GLU A 68 OE2 90.8 74.6 150.8 130.3 52.2
REMARK 620 7 HOH A 344 O 166.0 84.6 89.2 106.6 82.3 82.4
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 203 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 94 OD1
REMARK 620 2 ASP A 96 OD1 86.1
REMARK 620 3 ASN A 98 OD1 86.5 76.9
REMARK 620 4 TYR A 100 O 83.6 156.3 81.2
REMARK 620 5 GLU A 105 OE1 100.2 126.9 155.3 76.1
REMARK 620 6 GLU A 105 OE2 106.5 74.8 147.8 128.7 52.7
REMARK 620 7 HOH A 316 O 170.7 94.4 84.6 92.4 86.9 82.5
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 204 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 130 OD1
REMARK 620 2 ASP A 132 OD1 82.2
REMARK 620 3 ASP A 134 OD1 85.6 79.5
REMARK 620 4 GLN A 136 O 88.5 153.4 74.9
REMARK 620 5 GLN A 136 O 81.1 152.8 77.9 8.1
REMARK 620 6 GLU A 141 OE1 112.2 125.5 149.8 81.1 81.0
REMARK 620 7 GLU A 141 OE2 91.7 76.5 156.0 128.9 125.3 51.9
REMARK 620 8 HOH A 348 O 164.0 87.1 80.9 96.0 104.0 83.7 97.3
REMARK 620 N 1 2 3 4 5 6 7
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 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 208
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 209
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 210
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 212
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IPA A 213
DBREF 4DJC A 1 149 UNP P62158 CALM_HUMAN 1 149
DBREF 4DJC B 1491 1522 UNP Q14524 SCN5A_HUMAN 1491 1522
SEQADV 4DJC SER A -2 UNP P62158 EXPRESSION TAG
SEQADV 4DJC ASN A -1 UNP P62158 EXPRESSION TAG
SEQADV 4DJC ALA A 0 UNP P62158 EXPRESSION TAG
SEQADV 4DJC SER B 1488 UNP Q14524 EXPRESSION TAG
SEQADV 4DJC ASN B 1489 UNP Q14524 EXPRESSION TAG
SEQADV 4DJC ALA B 1490 UNP Q14524 EXPRESSION TAG
SEQRES 1 A 152 SER ASN ALA MET ALA ASP GLN LEU THR GLU GLU GLN ILE
SEQRES 2 A 152 ALA GLU PHE LYS GLU ALA PHE SER LEU PHE ASP LYS ASP
SEQRES 3 A 152 GLY ASP GLY THR ILE THR THR LYS GLU LEU GLY THR VAL
SEQRES 4 A 152 MET ARG SER LEU GLY GLN ASN PRO THR GLU ALA GLU LEU
SEQRES 5 A 152 GLN ASP MET ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY
SEQRES 6 A 152 THR ILE ASP PHE PRO GLU PHE LEU THR MET MET ALA ARG
SEQRES 7 A 152 LYS MET LYS ASP THR ASP SER GLU GLU GLU ILE ARG GLU
SEQRES 8 A 152 ALA PHE ARG VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE
SEQRES 9 A 152 SER ALA ALA GLU LEU ARG HIS VAL MET THR ASN LEU GLY
SEQRES 10 A 152 GLU LYS LEU THR ASP GLU GLU VAL ASP GLU MET ILE ARG
SEQRES 11 A 152 GLU ALA ASP ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU
SEQRES 12 A 152 GLU PHE VAL GLN MET MET THR ALA LYS
SEQRES 1 B 35 SER ASN ALA GLN LYS LYS TYR TYR ASN ALA MET LYS LYS
SEQRES 2 B 35 LEU GLY SER LYS LYS PRO GLN LYS PRO ILE PRO ARG PRO
SEQRES 3 B 35 LEU ASN LYS TYR GLN GLY PHE ILE PHE
HET CA A 201 1
HET CA A 202 1
HET CA A 203 1
HET CA A 204 1
HET IPA A 205 4
HET IPA A 206 4
HET IPA A 207 4
HET IPA A 208 4
HET IPA A 209 4
HET IPA A 210 4
HET IPA A 211 4
HET IPA A 212 4
HET IPA A 213 4
HETNAM CA CALCIUM ION
HETNAM IPA ISOPROPYL ALCOHOL
HETSYN IPA 2-PROPANOL
FORMUL 3 CA 4(CA 2+)
FORMUL 7 IPA 9(C3 H8 O)
FORMUL 16 HOH *161(H2 O)
HELIX 1 1 MET A 1 LEU A 5 5 5
HELIX 2 2 THR A 6 ASP A 21 1 16
HELIX 3 3 THR A 29 LEU A 40 1 12
HELIX 4 4 THR A 45 ASP A 57 1 13
HELIX 5 5 PHE A 66 ASP A 94 1 29
HELIX 6 6 SER A 102 LEU A 113 1 12
HELIX 7 7 THR A 118 ASP A 130 1 13
HELIX 8 8 TYR A 139 THR A 147 1 9
HELIX 9 9 ALA B 1490 LEU B 1501 1 12
SHEET 1 A 2 THR A 27 ILE A 28 0
SHEET 2 A 2 ILE A 64 ASP A 65 -1 O ILE A 64 N ILE A 28
SHEET 1 B 2 TYR A 100 ILE A 101 0
SHEET 2 B 2 VAL A 137 ASN A 138 -1 O VAL A 137 N ILE A 101
LINK OD1 ASP A 21 CA CA A 201 1555 1555 2.21
LINK OD1 ASP A 23 CA CA A 201 1555 1555 2.42
LINK OD2 ASP A 25 CA CA A 201 1555 1555 2.42
LINK O THR A 27 CA CA A 201 1555 1555 2.29
LINK OE2 GLU A 32 CA CA A 201 1555 1555 2.45
LINK OE1 GLU A 32 CA CA A 201 1555 1555 2.46
LINK OD2 ASP A 57 CA CA A 202 1555 1555 2.22
LINK OD1 ASP A 59 CA CA A 202 1555 1555 2.41
LINK OD1 ASN A 61 CA CA A 202 1555 1555 2.37
LINK O THR A 63 CA CA A 202 1555 1555 2.34
LINK OE1 GLU A 68 CA CA A 202 1555 1555 2.45
LINK OE2 GLU A 68 CA CA A 202 1555 1555 2.49
LINK OD1 ASP A 94 CA CA A 203 1555 1555 2.29
LINK OD1 ASP A 96 CA CA A 203 1555 1555 2.34
LINK OD1 ASN A 98 CA CA A 203 1555 1555 2.39
LINK O TYR A 100 CA CA A 203 1555 1555 2.28
LINK OE1 GLU A 105 CA CA A 203 1555 1555 2.45
LINK OE2 GLU A 105 CA CA A 203 1555 1555 2.49
LINK OD1 ASP A 130 CA CA A 204 1555 1555 2.28
LINK OD1 ASP A 132 CA CA A 204 1555 1555 2.34
LINK OD1 ASP A 134 CA CA A 204 1555 1555 2.37
LINK O BGLN A 136 CA CA A 204 1555 1555 2.23
LINK O AGLN A 136 CA CA A 204 1555 1555 2.40
LINK OE1 GLU A 141 CA CA A 204 1555 1555 2.45
LINK OE2 GLU A 141 CA CA A 204 1555 1555 2.48
LINK CA CA A 201 O HOH A 346 1555 1555 2.48
LINK CA CA A 202 O HOH A 344 1555 1555 2.26
LINK CA CA A 203 O HOH A 316 1555 1555 2.42
LINK CA CA A 204 O HOH A 348 1555 1555 2.41
SITE 1 AC1 6 ASP A 21 ASP A 23 ASP A 25 THR A 27
SITE 2 AC1 6 GLU A 32 HOH A 346
SITE 1 AC2 6 ASP A 57 ASP A 59 ASN A 61 THR A 63
SITE 2 AC2 6 GLU A 68 HOH A 344
SITE 1 AC3 6 ASP A 94 ASP A 96 ASN A 98 TYR A 100
SITE 2 AC3 6 GLU A 105 HOH A 316
SITE 1 AC4 6 ASP A 130 ASP A 132 ASP A 134 GLN A 136
SITE 2 AC4 6 GLU A 141 HOH A 348
SITE 1 AC5 3 LYS A 14 PHE A 66 ASP A 134
SITE 1 AC6 3 ALA A 47 ASP A 123 HOH A 383
SITE 1 AC7 2 TYR A 100 HOH A 302
SITE 1 AC8 6 THR A 30 LYS A 31 ASP A 59 GLY A 60
SITE 2 AC8 6 ASP A 96 ASN A 98
SITE 1 AC9 2 ILE A 64 MET A 72
SITE 1 BC1 3 GLY A 24 ARG A 127 GLY A 135
SITE 1 BC2 5 THR A 30 GLN A 50 ALA A 58 HOH A 364
SITE 2 BC2 5 HOH A 450
SITE 1 BC3 3 MET A 37 GLN A 42 GLU A 48
CRYST1 28.380 72.720 97.010 90.00 90.00 90.00 P 21 21 21 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 0.035236 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013751 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010308 0.00000
(ATOM LINES ARE NOT SHOWN.)
END