HEADER TRANSPORT PROTEIN 19-MAR-13 4JPZ
TITLE VOLTAGE-GATED SODIUM CHANNEL 1.2 C-TERMINAL DOMAIN IN COMPLEX WITH
TITLE 2 FGF13U AND CA2+/CALMODULIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FIBROBLAST GROWTH FACTOR 13;
COMPND 3 CHAIN: A, E;
COMPND 4 SYNONYM: FGF-13, FIBROBLAST GROWTH FACTOR HOMOLOGOUS FACTOR 2, FHF-2;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: SODIUM CHANNEL PROTEIN TYPE 2 SUBUNIT ALPHA;
COMPND 8 CHAIN: B, H;
COMPND 9 SYNONYM: HBSC II, SODIUM CHANNEL PROTEIN BRAIN II SUBUNIT ALPHA,
COMPND 10 SODIUM CHANNEL PROTEIN TYPE II SUBUNIT ALPHA, VOLTAGE-GATED SODIUM
COMPND 11 CHANNEL SUBUNIT ALPHA NAV1.2;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: CALMODULIN;
COMPND 15 CHAIN: C, I;
COMPND 16 SYNONYM: CAM;
COMPND 17 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: FGF13, FHF2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: SCN2A, NAC2, SCN2A1, SCN2A2;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 17 ORGANISM_COMMON: HUMAN;
SOURCE 18 ORGANISM_TAXID: 9606;
SOURCE 19 GENE: CALM1, CALM, CAM, CAM1, CALM2, CAM2, CAMB, CALM3, CALML2,
SOURCE 20 CAM3, CAMC, CAMIII;
SOURCE 21 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 22 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS EF HAND AND IQ MOTIF, ION CHANNEL, MEMBRANE, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR C.WANG,B.C.CHUNG,H.YAN,H.G.WANG,S.Y.LEE,G.S.PITT
REVDAT 5 28-FEB-24 4JPZ 1 REMARK SEQADV LINK
REVDAT 4 15-NOV-17 4JPZ 1 REMARK
REVDAT 3 03-DEC-14 4JPZ 1 AUTHOR
REVDAT 2 22-OCT-14 4JPZ 1 JRNL
REVDAT 1 16-APR-14 4JPZ 0
JRNL AUTH C.WANG,B.C.CHUNG,H.YAN,H.G.WANG,S.Y.LEE,G.S.PITT
JRNL TITL STRUCTURAL ANALYSES OF CA(2+)/CAM INTERACTION WITH NAV
JRNL TITL 2 CHANNEL C-TERMINI REVEAL MECHANISMS OF CALCIUM-DEPENDENT
JRNL TITL 3 REGULATION.
JRNL REF NAT COMMUN V. 5 4896 2014
JRNL REFN ESSN 2041-1723
JRNL PMID 25232683
JRNL DOI 10.1038/NCOMMS5896
REMARK 2
REMARK 2 RESOLUTION. 3.02 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.1_1168)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.02
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.23
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.400
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.8
REMARK 3 NUMBER OF REFLECTIONS : 49449
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.240
REMARK 3 FREE R VALUE TEST SET COUNT : 3581
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 48.2365 - 6.5016 1.00 4992 394 0.1756 0.1827
REMARK 3 2 6.5016 - 5.1625 1.00 4937 391 0.1886 0.2295
REMARK 3 3 5.1625 - 4.5104 1.00 4995 390 0.1828 0.2186
REMARK 3 4 4.5104 - 4.0983 0.99 4978 393 0.2100 0.2725
REMARK 3 5 4.0983 - 3.8047 0.99 4910 384 0.2274 0.2766
REMARK 3 6 3.8047 - 3.5804 0.97 4854 372 0.2415 0.2732
REMARK 3 7 3.5804 - 3.4012 0.96 4766 381 0.2681 0.3356
REMARK 3 8 3.4012 - 3.2531 0.89 4478 340 0.2910 0.3282
REMARK 3 9 3.2531 - 3.1279 0.79 3926 288 0.3037 0.3252
REMARK 3 10 3.1279 - 3.0200 0.60 3032 248 0.3191 0.3668
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.440
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.430
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.011 7122
REMARK 3 ANGLE : 1.041 9621
REMARK 3 CHIRALITY : 0.071 1036
REMARK 3 PLANARITY : 0.004 1242
REMARK 3 DIHEDRAL : 14.966 2708
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4JPZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-MAR-13.
REMARK 100 THE DEPOSITION ID IS D_1000078357.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-AUG-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-C
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : DOUBLE 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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53782
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.020
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
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) : 3.02
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.17
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.8
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: SAD
REMARK 200 SOFTWARE USED: PHASER, SHELX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG3350, 300 MM SODIUM ACETATE,50
REMARK 280 MM TRIS PH 7.5, AND 2 MM CACL2, EVAPORATION, TEMPERATURE 290K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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 76.56650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 43.05300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 76.56650
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 43.05300
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5810 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, H, I
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 MET A 1
REMARK 465 ALA A 2
REMARK 465 LEU A 3
REMARK 465 LEU A 4
REMARK 465 ARG A 5
REMARK 465 LYS A 6
REMARK 465 SER A 7
REMARK 465 TYR A 8
REMARK 465 SER A 9
REMARK 465 GLU A 10
REMARK 465 LEU A 159
REMARK 465 THR A 160
REMARK 465 GLU A 161
REMARK 465 PHE A 162
REMARK 465 SER A 163
REMARK 465 ARG A 164
REMARK 465 SER A 165
REMARK 465 GLY A 166
REMARK 465 SER A 167
REMARK 465 GLY A 168
REMARK 465 THR A 169
REMARK 465 PRO A 170
REMARK 465 THR A 171
REMARK 465 LYS A 172
REMARK 465 SER A 173
REMARK 465 ARG A 174
REMARK 465 SER A 175
REMARK 465 VAL A 176
REMARK 465 SER A 177
REMARK 465 GLY A 178
REMARK 465 VAL A 179
REMARK 465 LEU A 180
REMARK 465 ASN A 181
REMARK 465 GLY A 182
REMARK 465 GLY A 183
REMARK 465 LYS A 184
REMARK 465 SER A 185
REMARK 465 MET A 186
REMARK 465 SER A 187
REMARK 465 HIS A 188
REMARK 465 ASN A 189
REMARK 465 GLU A 190
REMARK 465 SER A 191
REMARK 465 THR A 192
REMARK 465 MET B 1754
REMARK 465 GLY B 1755
REMARK 465 SER B 1756
REMARK 465 SER B 1757
REMARK 465 HIS B 1758
REMARK 465 HIS B 1759
REMARK 465 HIS B 1760
REMARK 465 HIS B 1761
REMARK 465 HIS B 1762
REMARK 465 HIS B 1763
REMARK 465 SER B 1764
REMARK 465 SER B 1765
REMARK 465 GLY B 1766
REMARK 465 LEU B 1767
REMARK 465 VAL B 1768
REMARK 465 PRO B 1769
REMARK 465 ARG B 1770
REMARK 465 GLY B 1771
REMARK 465 SER B 1772
REMARK 465 HIS B 1773
REMARK 465 MET B 1774
REMARK 465 ALA B 1775
REMARK 465 SER B 1776
REMARK 465 GLU B 1777
REMARK 465 ASN B 1778
REMARK 465 PHE B 1779
REMARK 465 SER B 1780
REMARK 465 VAL B 1781
REMARK 465 ALA B 1782
REMARK 465 THR B 1783
REMARK 465 GLU B 1784
REMARK 465 GLU B 1785
REMARK 465 SER B 1786
REMARK 465 ALA B 1787
REMARK 465 SER B 1930
REMARK 465 ILE B 1931
REMARK 465 TYR B 1932
REMARK 465 LYS B 1933
REMARK 465 LYS B 1934
REMARK 465 ASP B 1935
REMARK 465 LYS B 1936
REMARK 465 GLY B 1937
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 ASP C 3
REMARK 465 GLN C 4
REMARK 465 LEU C 5
REMARK 465 THR C 6
REMARK 465 MET E 1
REMARK 465 ALA E 2
REMARK 465 LEU E 3
REMARK 465 LEU E 4
REMARK 465 ARG E 5
REMARK 465 LYS E 6
REMARK 465 SER E 7
REMARK 465 TYR E 8
REMARK 465 SER E 9
REMARK 465 GLU E 10
REMARK 465 LEU E 159
REMARK 465 THR E 160
REMARK 465 GLU E 161
REMARK 465 PHE E 162
REMARK 465 SER E 163
REMARK 465 ARG E 164
REMARK 465 SER E 165
REMARK 465 GLY E 166
REMARK 465 SER E 167
REMARK 465 GLY E 168
REMARK 465 THR E 169
REMARK 465 PRO E 170
REMARK 465 THR E 171
REMARK 465 LYS E 172
REMARK 465 SER E 173
REMARK 465 ARG E 174
REMARK 465 SER E 175
REMARK 465 VAL E 176
REMARK 465 SER E 177
REMARK 465 GLY E 178
REMARK 465 VAL E 179
REMARK 465 LEU E 180
REMARK 465 ASN E 181
REMARK 465 GLY E 182
REMARK 465 GLY E 183
REMARK 465 LYS E 184
REMARK 465 SER E 185
REMARK 465 MET E 186
REMARK 465 SER E 187
REMARK 465 HIS E 188
REMARK 465 ASN E 189
REMARK 465 GLU E 190
REMARK 465 SER E 191
REMARK 465 THR E 192
REMARK 465 MET H 1754
REMARK 465 GLY H 1755
REMARK 465 SER H 1756
REMARK 465 SER H 1757
REMARK 465 HIS H 1758
REMARK 465 HIS H 1759
REMARK 465 HIS H 1760
REMARK 465 HIS H 1761
REMARK 465 HIS H 1762
REMARK 465 HIS H 1763
REMARK 465 SER H 1764
REMARK 465 SER H 1765
REMARK 465 GLY H 1766
REMARK 465 LEU H 1767
REMARK 465 VAL H 1768
REMARK 465 PRO H 1769
REMARK 465 ARG H 1770
REMARK 465 GLY H 1771
REMARK 465 SER H 1772
REMARK 465 HIS H 1773
REMARK 465 MET H 1774
REMARK 465 ALA H 1775
REMARK 465 SER H 1776
REMARK 465 GLU H 1777
REMARK 465 ASN H 1778
REMARK 465 PHE H 1779
REMARK 465 SER H 1780
REMARK 465 VAL H 1781
REMARK 465 ALA H 1782
REMARK 465 THR H 1783
REMARK 465 GLU H 1784
REMARK 465 GLU H 1785
REMARK 465 SER H 1786
REMARK 465 ALA H 1787
REMARK 465 SER H 1930
REMARK 465 ILE H 1931
REMARK 465 TYR H 1932
REMARK 465 LYS H 1933
REMARK 465 LYS H 1934
REMARK 465 ASP H 1935
REMARK 465 LYS H 1936
REMARK 465 GLY H 1937
REMARK 465 MET I 1
REMARK 465 ALA I 2
REMARK 465 ASP I 3
REMARK 465 GLN I 4
REMARK 465 LEU I 5
REMARK 465 THR I 6
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 LYS C 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 NH2 ARG I 107 OD1 ASP I 123 2.16
REMARK 500 O GLU I 83 N GLU I 85 2.16
REMARK 500 O SER I 82 N GLU I 84 2.16
REMARK 500 O VAL C 36 OG SER C 39 2.18
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 PRO A 53 96.27 -68.06
REMARK 500 TYR A 98 -31.37 -146.13
REMARK 500 GLN A 110 -37.93 64.43
REMARK 500 GLN A 111 -61.00 -90.07
REMARK 500 HIS A 157 -151.07 -134.68
REMARK 500 PRO B1789 -156.94 -61.11
REMARK 500 SER B1869 -163.53 -168.66
REMARK 500 ALA B1885 -71.72 -79.17
REMARK 500 ASP C 81 72.56 -101.51
REMARK 500 GLU C 115 70.43 -69.44
REMARK 500 PRO E 53 96.72 -66.94
REMARK 500 TYR E 98 -32.10 -147.50
REMARK 500 HIS E 157 -153.12 -133.20
REMARK 500 PRO H1789 -174.18 -60.83
REMARK 500 SER H1869 -162.82 -166.93
REMARK 500 ALA H1885 -70.83 -76.61
REMARK 500 THR H1898 -159.21 -146.54
REMARK 500 GLU I 83 45.52 -2.45
REMARK 500 GLU I 84 -55.15 52.08
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 C 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 21 OD1
REMARK 620 2 ASP C 23 OD1 95.4
REMARK 620 3 ASP C 25 OD1 85.2 89.8
REMARK 620 4 THR C 27 O 81.9 156.1 66.3
REMARK 620 5 GLU C 32 OE2 110.4 75.3 159.1 128.0
REMARK 620 6 GLU C 32 OE1 91.9 125.4 144.8 78.5 51.7
REMARK 620 7 HOH C 301 O 168.7 86.3 105.9 101.0 59.2 78.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 57 OD1
REMARK 620 2 ASN C 61 OD1 114.7
REMARK 620 3 THR C 63 O 101.9 75.9
REMARK 620 4 GLU C 68 OE1 94.3 141.2 73.3
REMARK 620 5 GLU C 68 OE2 67.8 169.3 114.3 45.5
REMARK 620 6 HOH C 302 O 149.6 92.5 70.7 55.3 88.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 203 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 94 OD1
REMARK 620 2 ASP C 96 OD1 97.5
REMARK 620 3 ASN C 98 OD1 80.5 96.0
REMARK 620 4 TYR C 100 O 78.1 175.2 85.3
REMARK 620 5 HOH C 303 O 172.8 85.8 105.6 98.3
REMARK 620 6 HOH C 304 O 78.0 78.3 156.8 98.7 96.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 204 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP C 130 OD1
REMARK 620 2 ASP C 132 OD1 89.2
REMARK 620 3 ASP C 134 OD1 77.6 72.6
REMARK 620 4 GLN C 136 O 74.1 149.9 79.3
REMARK 620 5 HOH C 305 O 161.8 85.8 84.2 102.2
REMARK 620 6 HOH C 306 O 111.7 107.8 170.6 101.7 86.4
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA I 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP I 21 OD1
REMARK 620 2 ASP I 23 OD1 113.9
REMARK 620 3 ASP I 25 OD1 73.8 83.5
REMARK 620 4 THR I 27 O 72.7 145.6 65.5
REMARK 620 5 GLU I 32 OE2 131.1 82.2 154.8 120.0
REMARK 620 6 GLU I 32 OE1 103.7 128.0 142.9 78.3 45.8
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA I 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP I 57 OD1
REMARK 620 2 ASN I 61 OD1 97.0
REMARK 620 3 THR I 63 O 86.3 77.1
REMARK 620 4 GLU I 68 OE1 109.8 140.9 76.8
REMARK 620 5 GLU I 68 OE2 96.6 151.6 128.5 53.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA I 203 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP I 94 OD1
REMARK 620 2 ASP I 96 OD1 91.3
REMARK 620 3 ASN I 98 OD1 68.2 91.4
REMARK 620 4 TYR I 100 O 82.8 173.9 88.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA I 204 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP I 130 OD1
REMARK 620 2 ASP I 132 OD1 64.4
REMARK 620 3 ASP I 132 OD2 116.0 53.4
REMARK 620 4 ASP I 134 OD1 75.7 78.9 79.4
REMARK 620 5 GLN I 136 O 66.8 130.9 162.0 84.5
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA I 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA I 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA I 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA I 204
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4JQ0 RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE RESIDUES RRRP AT POSITIONS 59-62 ARE ISOFORM 2 NATURAL VARIANTS,
REMARK 999 UNP CODE Q92913-2
DBREF 4JPZ A 5 192 UNP Q92913 FGF13_HUMAN 58 245
DBREF 4JPZ B 1777 1937 UNP Q99250 SCN2A_HUMAN 1777 1937
DBREF 4JPZ C 1 149 UNP P62158 CALM_HUMAN 1 149
DBREF 4JPZ E 5 192 UNP Q92913 FGF13_HUMAN 58 245
DBREF 4JPZ H 1777 1937 UNP Q99250 SCN2A_HUMAN 1777 1937
DBREF 4JPZ I 1 149 UNP P62158 CALM_HUMAN 1 149
SEQADV 4JPZ MET A 1 UNP Q92913 EXPRESSION TAG
SEQADV 4JPZ ALA A 2 UNP Q92913 EXPRESSION TAG
SEQADV 4JPZ LEU A 3 UNP Q92913 EXPRESSION TAG
SEQADV 4JPZ LEU A 4 UNP Q92913 EXPRESSION TAG
SEQADV 4JPZ LYS A 6 UNP Q92913 ARG 59 SEE REMARK 999
SEQADV 4JPZ SER A 7 UNP Q92913 ARG 60 SEE REMARK 999
SEQADV 4JPZ TYR A 8 UNP Q92913 ARG 61 SEE REMARK 999
SEQADV 4JPZ SER A 9 UNP Q92913 PRO 62 SEE REMARK 999
SEQADV 4JPZ MET B 1754 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ GLY B 1755 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ SER B 1756 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ SER B 1757 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ HIS B 1758 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ HIS B 1759 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ HIS B 1760 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ HIS B 1761 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ HIS B 1762 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ HIS B 1763 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ SER B 1764 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ SER B 1765 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ GLY B 1766 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ LEU B 1767 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ VAL B 1768 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ PRO B 1769 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ ARG B 1770 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ GLY B 1771 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ SER B 1772 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ HIS B 1773 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ MET B 1774 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ ALA B 1775 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ SER B 1776 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ MET E 1 UNP Q92913 EXPRESSION TAG
SEQADV 4JPZ ALA E 2 UNP Q92913 EXPRESSION TAG
SEQADV 4JPZ LEU E 3 UNP Q92913 EXPRESSION TAG
SEQADV 4JPZ LEU E 4 UNP Q92913 EXPRESSION TAG
SEQADV 4JPZ LYS E 6 UNP Q92913 ARG 59 SEE REMARK 999
SEQADV 4JPZ SER E 7 UNP Q92913 ARG 60 SEE REMARK 999
SEQADV 4JPZ TYR E 8 UNP Q92913 ARG 61 SEE REMARK 999
SEQADV 4JPZ SER E 9 UNP Q92913 PRO 62 SEE REMARK 999
SEQADV 4JPZ MET H 1754 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ GLY H 1755 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ SER H 1756 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ SER H 1757 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ HIS H 1758 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ HIS H 1759 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ HIS H 1760 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ HIS H 1761 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ HIS H 1762 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ HIS H 1763 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ SER H 1764 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ SER H 1765 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ GLY H 1766 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ LEU H 1767 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ VAL H 1768 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ PRO H 1769 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ ARG H 1770 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ GLY H 1771 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ SER H 1772 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ HIS H 1773 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ MET H 1774 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ ALA H 1775 UNP Q99250 EXPRESSION TAG
SEQADV 4JPZ SER H 1776 UNP Q99250 EXPRESSION TAG
SEQRES 1 A 192 MET ALA LEU LEU ARG LYS SER TYR SER GLU PRO GLN LEU
SEQRES 2 A 192 LYS GLY ILE VAL THR LYS LEU TYR SER ARG GLN GLY TYR
SEQRES 3 A 192 HIS LEU GLN LEU GLN ALA ASP GLY THR ILE ASP GLY THR
SEQRES 4 A 192 LYS ASP GLU ASP SER THR TYR THR LEU PHE ASN LEU ILE
SEQRES 5 A 192 PRO VAL GLY LEU ARG VAL VAL ALA ILE GLN GLY VAL GLN
SEQRES 6 A 192 THR LYS LEU TYR LEU ALA MET ASN SER GLU GLY TYR LEU
SEQRES 7 A 192 TYR THR SER GLU LEU PHE THR PRO GLU CYS LYS PHE LYS
SEQRES 8 A 192 GLU SER VAL PHE GLU ASN TYR TYR VAL THR TYR SER SER
SEQRES 9 A 192 MET ILE TYR ARG GLN GLN GLN SER GLY ARG GLY TRP TYR
SEQRES 10 A 192 LEU GLY LEU ASN LYS GLU GLY GLU ILE MET LYS GLY ASN
SEQRES 11 A 192 HIS VAL LYS LYS ASN LYS PRO ALA ALA HIS PHE LEU PRO
SEQRES 12 A 192 LYS PRO LEU LYS VAL ALA MET TYR LYS GLU PRO SER LEU
SEQRES 13 A 192 HIS ASP LEU THR GLU PHE SER ARG SER GLY SER GLY THR
SEQRES 14 A 192 PRO THR LYS SER ARG SER VAL SER GLY VAL LEU ASN GLY
SEQRES 15 A 192 GLY LYS SER MET SER HIS ASN GLU SER THR
SEQRES 1 B 184 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 184 LEU VAL PRO ARG GLY SER HIS MET ALA SER GLU ASN PHE
SEQRES 3 B 184 SER VAL ALA THR GLU GLU SER ALA GLU PRO LEU SER GLU
SEQRES 4 B 184 ASP ASP PHE GLU MET PHE TYR GLU VAL TRP GLU LYS PHE
SEQRES 5 B 184 ASP PRO ASP ALA THR GLN PHE ILE GLU PHE ALA LYS LEU
SEQRES 6 B 184 SER ASP PHE ALA ASP ALA LEU ASP PRO PRO LEU LEU ILE
SEQRES 7 B 184 ALA LYS PRO ASN LYS VAL GLN LEU ILE ALA MET ASP LEU
SEQRES 8 B 184 PRO MET VAL SER GLY ASP ARG ILE HIS CYS LEU ASP ILE
SEQRES 9 B 184 LEU PHE ALA PHE THR LYS ARG VAL LEU GLY GLU SER GLY
SEQRES 10 B 184 GLU MET ASP ALA LEU ARG ILE GLN MET GLU GLU ARG PHE
SEQRES 11 B 184 MET ALA SER ASN PRO SER LYS VAL SER TYR GLU PRO ILE
SEQRES 12 B 184 THR THR THR LEU LYS ARG LYS GLN GLU GLU VAL SER ALA
SEQRES 13 B 184 ILE ILE ILE GLN ARG ALA TYR ARG ARG TYR LEU LEU LYS
SEQRES 14 B 184 GLN LYS VAL LYS LYS VAL SER SER ILE TYR LYS LYS ASP
SEQRES 15 B 184 LYS GLY
SEQRES 1 C 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 C 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 C 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 C 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 C 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 C 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 C 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 C 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 C 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 C 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 C 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 C 149 GLN MET MET THR ALA LYS
SEQRES 1 E 192 MET ALA LEU LEU ARG LYS SER TYR SER GLU PRO GLN LEU
SEQRES 2 E 192 LYS GLY ILE VAL THR LYS LEU TYR SER ARG GLN GLY TYR
SEQRES 3 E 192 HIS LEU GLN LEU GLN ALA ASP GLY THR ILE ASP GLY THR
SEQRES 4 E 192 LYS ASP GLU ASP SER THR TYR THR LEU PHE ASN LEU ILE
SEQRES 5 E 192 PRO VAL GLY LEU ARG VAL VAL ALA ILE GLN GLY VAL GLN
SEQRES 6 E 192 THR LYS LEU TYR LEU ALA MET ASN SER GLU GLY TYR LEU
SEQRES 7 E 192 TYR THR SER GLU LEU PHE THR PRO GLU CYS LYS PHE LYS
SEQRES 8 E 192 GLU SER VAL PHE GLU ASN TYR TYR VAL THR TYR SER SER
SEQRES 9 E 192 MET ILE TYR ARG GLN GLN GLN SER GLY ARG GLY TRP TYR
SEQRES 10 E 192 LEU GLY LEU ASN LYS GLU GLY GLU ILE MET LYS GLY ASN
SEQRES 11 E 192 HIS VAL LYS LYS ASN LYS PRO ALA ALA HIS PHE LEU PRO
SEQRES 12 E 192 LYS PRO LEU LYS VAL ALA MET TYR LYS GLU PRO SER LEU
SEQRES 13 E 192 HIS ASP LEU THR GLU PHE SER ARG SER GLY SER GLY THR
SEQRES 14 E 192 PRO THR LYS SER ARG SER VAL SER GLY VAL LEU ASN GLY
SEQRES 15 E 192 GLY LYS SER MET SER HIS ASN GLU SER THR
SEQRES 1 H 184 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 H 184 LEU VAL PRO ARG GLY SER HIS MET ALA SER GLU ASN PHE
SEQRES 3 H 184 SER VAL ALA THR GLU GLU SER ALA GLU PRO LEU SER GLU
SEQRES 4 H 184 ASP ASP PHE GLU MET PHE TYR GLU VAL TRP GLU LYS PHE
SEQRES 5 H 184 ASP PRO ASP ALA THR GLN PHE ILE GLU PHE ALA LYS LEU
SEQRES 6 H 184 SER ASP PHE ALA ASP ALA LEU ASP PRO PRO LEU LEU ILE
SEQRES 7 H 184 ALA LYS PRO ASN LYS VAL GLN LEU ILE ALA MET ASP LEU
SEQRES 8 H 184 PRO MET VAL SER GLY ASP ARG ILE HIS CYS LEU ASP ILE
SEQRES 9 H 184 LEU PHE ALA PHE THR LYS ARG VAL LEU GLY GLU SER GLY
SEQRES 10 H 184 GLU MET ASP ALA LEU ARG ILE GLN MET GLU GLU ARG PHE
SEQRES 11 H 184 MET ALA SER ASN PRO SER LYS VAL SER TYR GLU PRO ILE
SEQRES 12 H 184 THR THR THR LEU LYS ARG LYS GLN GLU GLU VAL SER ALA
SEQRES 13 H 184 ILE ILE ILE GLN ARG ALA TYR ARG ARG TYR LEU LEU LYS
SEQRES 14 H 184 GLN LYS VAL LYS LYS VAL SER SER ILE TYR LYS LYS ASP
SEQRES 15 H 184 LYS GLY
SEQRES 1 I 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 I 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 I 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 I 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 I 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 I 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 I 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 I 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 I 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 I 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 I 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 I 149 GLN MET MET THR ALA LYS
HET CA C 201 1
HET CA C 202 1
HET CA C 203 1
HET CA C 204 1
HET CA I 201 1
HET CA I 202 1
HET CA I 203 1
HET CA I 204 1
HETNAM CA CALCIUM ION
FORMUL 7 CA 8(CA 2+)
FORMUL 15 HOH *31(H2 O)
HELIX 1 1 SER A 44 THR A 47 5 4
HELIX 2 2 THR A 85 CYS A 88 5 4
HELIX 3 3 LYS A 128 VAL A 132 5 5
HELIX 4 4 LYS A 136 ALA A 139 5 4
HELIX 5 5 SER B 1791 ASP B 1806 1 16
HELIX 6 6 LYS B 1817 ALA B 1824 1 8
HELIX 7 7 ASN B 1835 ILE B 1840 1 6
HELIX 8 8 CYS B 1854 GLY B 1867 1 14
HELIX 9 9 SER B 1869 ASN B 1887 1 19
HELIX 10 10 LEU B 1900 LYS B 1927 1 28
HELIX 11 11 GLN C 9 ASP C 21 1 13
HELIX 12 12 THR C 29 GLY C 41 1 13
HELIX 13 13 THR C 45 GLU C 55 1 11
HELIX 14 14 ASP C 65 LYS C 78 1 14
HELIX 15 15 ILE C 86 VAL C 92 1 7
HELIX 16 16 ALA C 103 LEU C 113 1 11
HELIX 17 17 THR C 118 ASP C 130 1 13
HELIX 18 18 TYR C 139 THR C 147 1 9
HELIX 19 19 SER E 44 THR E 47 5 4
HELIX 20 20 THR E 85 GLU E 87 5 3
HELIX 21 21 LYS E 128 VAL E 132 5 5
HELIX 22 22 LYS E 136 ALA E 139 5 4
HELIX 23 23 SER H 1791 ASP H 1806 1 16
HELIX 24 24 LYS H 1817 ALA H 1824 1 8
HELIX 25 25 ASN H 1835 ILE H 1840 1 6
HELIX 26 26 CYS H 1854 GLY H 1867 1 14
HELIX 27 27 SER H 1869 ASN H 1887 1 19
HELIX 28 28 LEU H 1900 VAL H 1928 1 29
HELIX 29 29 GLU I 8 ASP I 21 1 14
HELIX 30 30 THR I 29 GLY I 41 1 13
HELIX 31 31 THR I 45 GLU I 55 1 11
HELIX 32 32 ASP I 65 LYS I 78 1 14
HELIX 33 33 ILE I 86 VAL I 92 1 7
HELIX 34 34 ALA I 103 LEU I 113 1 11
HELIX 35 35 THR I 118 ASP I 130 1 13
HELIX 36 36 TYR I 139 ALA I 148 1 10
LINK OD1 ASP C 21 CA CA C 201 1555 1555 2.19
LINK OD1 ASP C 23 CA CA C 201 1555 1555 2.34
LINK OD1 ASP C 25 CA CA C 201 1555 1555 2.29
LINK O THR C 27 CA CA C 201 1555 1555 2.57
LINK OE2 GLU C 32 CA CA C 201 1555 1555 2.40
LINK OE1 GLU C 32 CA CA C 201 1555 1555 2.59
LINK OD1 ASP C 57 CA CA C 202 1555 1555 2.40
LINK OD1 ASN C 61 CA CA C 202 1555 1555 2.31
LINK O THR C 63 CA CA C 202 1555 1555 2.54
LINK OE1 GLU C 68 CA CA C 202 1555 1555 2.58
LINK OE2 GLU C 68 CA CA C 202 1555 1555 3.00
LINK OD1 ASP C 94 CA CA C 203 1555 1555 2.39
LINK OD1 ASP C 96 CA CA C 203 1555 1555 2.39
LINK OD1 ASN C 98 CA CA C 203 1555 1555 2.28
LINK O TYR C 100 CA CA C 203 1555 1555 2.43
LINK OD1 ASP C 130 CA CA C 204 1555 1555 2.46
LINK OD1 ASP C 132 CA CA C 204 1555 1555 2.26
LINK OD1 ASP C 134 CA CA C 204 1555 1555 2.46
LINK O GLN C 136 CA CA C 204 1555 1555 2.28
LINK CA CA C 201 O HOH C 301 1555 1555 2.90
LINK CA CA C 202 O HOH C 302 1555 1555 2.52
LINK CA CA C 203 O HOH C 303 1555 1555 2.34
LINK CA CA C 203 O HOH C 304 1555 1555 2.50
LINK CA CA C 204 O HOH C 305 1555 1555 2.26
LINK CA CA C 204 O HOH C 306 1555 1555 2.28
LINK OD1 ASP I 21 CA CA I 201 1555 1555 2.25
LINK OD1 ASP I 23 CA CA I 201 1555 1555 2.28
LINK OD1 ASP I 25 CA CA I 201 1555 1555 2.36
LINK O THR I 27 CA CA I 201 1555 1555 2.56
LINK OE2 GLU I 32 CA CA I 201 1555 1555 2.36
LINK OE1 GLU I 32 CA CA I 201 1555 1555 3.04
LINK OD1 ASP I 57 CA CA I 202 1555 1555 2.35
LINK OD1 ASN I 61 CA CA I 202 1555 1555 2.32
LINK O THR I 63 CA CA I 202 1555 1555 2.50
LINK OE1 GLU I 68 CA CA I 202 1555 1555 2.42
LINK OE2 GLU I 68 CA CA I 202 1555 1555 2.43
LINK OD1 ASP I 94 CA CA I 203 1555 1555 2.63
LINK OD1 ASP I 96 CA CA I 203 1555 1555 2.34
LINK OD1 ASN I 98 CA CA I 203 1555 1555 2.37
LINK O TYR I 100 CA CA I 203 1555 1555 2.23
LINK OD1 ASP I 130 CA CA I 204 1555 1555 2.52
LINK OD1 ASP I 132 CA CA I 204 1555 1555 2.30
LINK OD2 ASP I 132 CA CA I 204 1555 1555 2.54
LINK OD1 ASP I 134 CA CA I 204 1555 1555 2.45
LINK O GLN I 136 CA CA I 204 1555 1555 2.41
CISPEP 1 PRO B 1827 PRO B 1828 0 3.28
CISPEP 2 LYS B 1833 PRO B 1834 0 -1.60
CISPEP 3 SER B 1848 GLY B 1849 0 -0.92
CISPEP 4 LEU B 1866 GLY B 1867 0 -13.38
CISPEP 5 PRO H 1827 PRO H 1828 0 3.86
CISPEP 6 LYS H 1833 PRO H 1834 0 -1.52
CISPEP 7 SER H 1848 GLY H 1849 0 -0.56
SITE 1 AC1 6 ASP C 21 ASP C 23 ASP C 25 THR C 27
SITE 2 AC1 6 GLU C 32 HOH C 301
SITE 1 AC2 6 ASP C 57 ASP C 59 ASN C 61 THR C 63
SITE 2 AC2 6 GLU C 68 HOH C 302
SITE 1 AC3 6 ASP C 94 ASP C 96 ASN C 98 TYR C 100
SITE 2 AC3 6 HOH C 303 HOH C 304
SITE 1 AC4 6 ASP C 130 ASP C 132 ASP C 134 GLN C 136
SITE 2 AC4 6 HOH C 305 HOH C 306
SITE 1 AC5 5 ASP I 21 ASP I 23 ASP I 25 THR I 27
SITE 2 AC5 5 GLU I 32
SITE 1 AC6 5 ASP I 57 ASP I 59 ASN I 61 THR I 63
SITE 2 AC6 5 GLU I 68
SITE 1 AC7 4 ASP I 94 ASP I 96 ASN I 98 TYR I 100
SITE 1 AC8 4 ASP I 130 ASP I 132 ASP I 134 GLN I 136
CRYST1 153.133 86.106 109.399 90.00 100.90 90.00 C 1 2 1 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.006530 0.000000 0.001258 0.00000
SCALE2 0.000000 0.011614 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009309 0.00000
(ATOM LINES ARE NOT SHOWN.)
END