HEADER METAL BINDING PROTEIN 22-NOV-18 6N5W
TITLE CRYSTAL STRUCTURE OF THE CA2+/CAM COMPLEX WITH INDEPENDENT PEPTIDES OF
TITLE 2 KV7.4 (KCNQ4) A & B DOMAINS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY KQT MEMBER 4;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: KQT-LIKE 4,POTASSIUM CHANNEL SUBUNIT ALPHA KVLQT4,VOLTAGE-
COMPND 5 GATED POTASSIUM CHANNEL SUBUNIT KV7.4;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY KQT MEMBER 4;
COMPND 9 CHAIN: B;
COMPND 10 SYNONYM: KQT-LIKE 4,POTASSIUM CHANNEL SUBUNIT ALPHA KVLQT4,VOLTAGE-
COMPND 11 GATED POTASSIUM CHANNEL SUBUNIT KV7.4;
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: CALMODULIN-1;
COMPND 15 CHAIN: C;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 4 ORGANISM_COMMON: HUMAN;
SOURCE 5 ORGANISM_TAXID: 9606;
SOURCE 6 MOL_ID: 2;
SOURCE 7 SYNTHETIC: YES;
SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 9 ORGANISM_COMMON: HUMAN;
SOURCE 10 ORGANISM_TAXID: 9606;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: CALM1, CALM, CAM, CAM1;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 19 EXPRESSION_SYSTEM_PLASMID: PETGQ.HCAM
KEYWDS ION CHANNEL, CALMODULIN, KCNQ4 PEPTIDES, COMPLEX, METAL BINDING
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR A.B.TAYLOR,C.R.ARCHER,M.S.SHAPIRO
REVDAT 4 11-OCT-23 6N5W 1 REMARK
REVDAT 3 04-DEC-19 6N5W 1 REMARK
REVDAT 2 24-APR-19 6N5W 1 JRNL
REVDAT 1 13-MAR-19 6N5W 0
JRNL AUTH C.R.ARCHER,B.T.ENSLOW,A.B.TAYLOR,V.DE LA ROSA,
JRNL AUTH 2 A.BHATTACHARYA,M.S.SHAPIRO
JRNL TITL A MUTUALLY INDUCED CONFORMATIONAL FIT UNDERLIES
JRNL TITL 2 CA2+-DIRECTED INTERACTIONS BETWEEN CALMODULIN AND THE
JRNL TITL 3 PROXIMAL C TERMINUS OF KCNQ4 K+CHANNELS.
JRNL REF J. BIOL. CHEM. V. 294 6094 2019
JRNL REFN ESSN 1083-351X
JRNL PMID 30808708
JRNL DOI 10.1074/JBC.RA118.006857
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.13_2998: ???)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.28
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 11810
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.237
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.980
REMARK 3 FREE R VALUE TEST SET COUNT : 1179
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 41.2861 - 4.2986 0.99 1416 176 0.1965 0.2035
REMARK 3 2 4.2986 - 3.4124 1.00 1386 118 0.1943 0.2694
REMARK 3 3 3.4124 - 2.9812 1.00 1281 177 0.2612 0.3274
REMARK 3 4 2.9812 - 2.7087 1.00 1360 118 0.2710 0.3411
REMARK 3 5 2.7087 - 2.5146 1.00 1284 177 0.2796 0.3513
REMARK 3 6 2.5146 - 2.3664 1.00 1319 118 0.2990 0.2985
REMARK 3 7 2.3664 - 2.2479 1.00 1259 177 0.3181 0.3433
REMARK 3 8 2.2479 - 2.1500 1.00 1326 118 0.3425 0.3921
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.340
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.300
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.60
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 59.90
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 : 0.010 1514
REMARK 3 ANGLE : 1.127 2032
REMARK 3 CHIRALITY : 0.077 227
REMARK 3 PLANARITY : 0.005 269
REMARK 3 DIHEDRAL : 23.281 581
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 338 THROUGH 356 )
REMARK 3 ORIGIN FOR THE GROUP (A): -18.6051 20.8231 -5.8396
REMARK 3 T TENSOR
REMARK 3 T11: 0.5073 T22: 0.3210
REMARK 3 T33: 0.2434 T12: 0.1133
REMARK 3 T13: -0.0137 T23: 0.0996
REMARK 3 L TENSOR
REMARK 3 L11: 1.0106 L22: 1.3045
REMARK 3 L33: 0.4599 L12: 0.8776
REMARK 3 L13: -0.4319 L23: -0.4832
REMARK 3 S TENSOR
REMARK 3 S11: -0.2658 S12: 0.0964 S13: -0.1637
REMARK 3 S21: -0.3948 S22: 0.6325 S23: -0.0231
REMARK 3 S31: -0.3436 S32: -0.5646 S33: 0.1366
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 525 THROUGH 549 )
REMARK 3 ORIGIN FOR THE GROUP (A): -14.0423 10.4558 -9.6824
REMARK 3 T TENSOR
REMARK 3 T11: 0.3744 T22: 0.3747
REMARK 3 T33: 0.3050 T12: -0.0352
REMARK 3 T13: 0.0123 T23: 0.0293
REMARK 3 L TENSOR
REMARK 3 L11: 0.2397 L22: 0.1502
REMARK 3 L33: 0.3399 L12: -0.1532
REMARK 3 L13: -0.2043 L23: 0.2242
REMARK 3 S TENSOR
REMARK 3 S11: 0.1014 S12: 0.0503 S13: 0.0095
REMARK 3 S21: 0.5764 S22: -0.3538 S23: -0.4282
REMARK 3 S31: -0.1181 S32: -0.0542 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 4 THROUGH 78 )
REMARK 3 ORIGIN FOR THE GROUP (A): -9.1494 6.1267 -15.8142
REMARK 3 T TENSOR
REMARK 3 T11: 0.2917 T22: 0.3491
REMARK 3 T33: 0.3907 T12: -0.0269
REMARK 3 T13: 0.0384 T23: 0.0595
REMARK 3 L TENSOR
REMARK 3 L11: 1.7814 L22: 1.0201
REMARK 3 L33: 0.7380 L12: -0.1787
REMARK 3 L13: -0.5766 L23: 0.4042
REMARK 3 S TENSOR
REMARK 3 S11: 0.0631 S12: 0.2590 S13: 0.0710
REMARK 3 S21: 0.1034 S22: -0.0651 S23: -0.2743
REMARK 3 S31: -0.0882 S32: 0.0030 S33: -0.0000
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 79 THROUGH 147 )
REMARK 3 ORIGIN FOR THE GROUP (A): -19.6985 25.8706 1.7816
REMARK 3 T TENSOR
REMARK 3 T11: 0.6673 T22: 0.4170
REMARK 3 T33: 0.5055 T12: 0.1321
REMARK 3 T13: 0.1625 T23: 0.2392
REMARK 3 L TENSOR
REMARK 3 L11: 1.6641 L22: 0.5847
REMARK 3 L33: 4.5717 L12: -0.2153
REMARK 3 L13: -0.5771 L23: 0.9296
REMARK 3 S TENSOR
REMARK 3 S11: 0.4137 S12: -0.1814 S13: 0.1446
REMARK 3 S21: 0.2120 S22: 0.2725 S23: 0.1581
REMARK 3 S31: -1.3472 S32: -0.2506 S33: 2.0627
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 6N5W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-NOV-18.
REMARK 100 THE DEPOSITION ID IS D_1000238239.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-MAR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
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-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97918
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11851
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 43.520
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.900
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.15700
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.90
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 1.07300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
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: 4UMO
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.3 M SODIUM CITRATE, 0.1 M HEPES PH
REMARK 280 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K
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 21.75500
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 65.28500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.75500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 65.28500
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10080 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 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 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 GLU A 336
REMARK 465 LYS A 337
REMARK 465 MET A 357
REMARK 465 SER A 358
REMARK 465 ARG A 359
REMARK 465 ALA A 360
REMARK 465 TYR A 361
REMARK 465 LEU A 362
REMARK 465 ASP B 524
REMARK 465 MET C 0
REMARK 465 ALA C 1
REMARK 465 ASP C 2
REMARK 465 GLN C 3
REMARK 465 LYS C 148
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 LYS C 75 -124.87 52.33
REMARK 500 ARG C 90 -37.45 -37.36
REMARK 500 ASN C 137 93.38 -68.59
REMARK 500 THR C 146 54.44 -91.67
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 20 OD1
REMARK 620 2 ASP C 22 OD1 71.6
REMARK 620 3 ASP C 24 OD1 77.5 74.8
REMARK 620 4 THR C 26 O 87.8 152.0 82.5
REMARK 620 5 GLU C 31 OE1 96.8 81.9 156.7 120.2
REMARK 620 6 GLU C 31 OE2 117.9 132.1 150.9 74.1 51.3
REMARK 620 7 HOH C 307 O 154.0 84.5 86.8 110.7 89.5 85.6
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 56 OD1
REMARK 620 2 ASP C 58 OD1 72.2
REMARK 620 3 ASN C 60 OD1 81.6 76.4
REMARK 620 4 THR C 62 O 80.5 149.2 86.0
REMARK 620 5 GLU C 67 OE1 99.8 115.0 168.5 83.0
REMARK 620 6 GLU C 67 OE2 88.3 66.6 142.9 127.5 48.5
REMARK 620 N 1 2 3 4 5
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
DBREF 6N5W A 336 362 UNP P56696 KCNQ4_HUMAN 336 362
DBREF 6N5W B 524 549 UNP P56696 KCNQ4_HUMAN 470 495
DBREF 6N5W C 0 148 UNP P0DP23 CALM1_HUMAN 1 149
SEQRES 1 A 27 GLU LYS ARG ARG MET PRO ALA ALA ASN LEU ILE GLN ALA
SEQRES 2 A 27 ALA TRP ARG LEU TYR SER THR ASP MET SER ARG ALA TYR
SEQRES 3 A 27 LEU
SEQRES 1 B 26 ASP ASP ILE MET PRO ALA VAL LYS THR VAL ILE ARG SER
SEQRES 2 B 26 ILE ARG ILE LEU LYS PHE LEU VAL ALA LYS ARG LYS PHE
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
HET CA C 201 1
HET CA C 202 1
HETNAM CA CALCIUM ION
FORMUL 4 CA 2(CA 2+)
FORMUL 6 HOH *23(H2 O)
HELIX 1 AA1 ARG A 338 SER A 354 1 17
HELIX 2 AA2 ILE B 526 PHE B 549 1 24
HELIX 3 AA3 THR C 5 ASP C 20 1 16
HELIX 4 AA4 THR C 28 LEU C 39 1 12
HELIX 5 AA5 THR C 44 ASP C 56 1 13
HELIX 6 AA6 PHE C 65 LYS C 75 1 11
HELIX 7 AA7 ASP C 80 VAL C 91 1 12
HELIX 8 AA8 ALA C 102 LEU C 112 1 11
HELIX 9 AA9 THR C 117 ASP C 129 1 13
HELIX 10 AB1 TYR C 138 THR C 146 1 9
SHEET 1 AA1 2 THR C 26 ILE C 27 0
SHEET 2 AA1 2 ILE C 63 ASP C 64 -1 O ILE C 63 N ILE C 27
SHEET 1 AA2 2 TYR C 99 SER C 101 0
SHEET 2 AA2 2 GLN C 135 ASN C 137 -1 O VAL C 136 N ILE C 100
LINK OD1 ASP C 20 CA CA C 201 1555 1555 2.44
LINK OD1 ASP C 22 CA CA C 201 1555 1555 2.16
LINK OD1 ASP C 24 CA CA C 201 1555 1555 2.55
LINK O THR C 26 CA CA C 201 1555 1555 2.30
LINK OE1 GLU C 31 CA CA C 201 1555 1555 2.68
LINK OE2 GLU C 31 CA CA C 201 1555 1555 2.35
LINK OD1 ASP C 56 CA CA C 202 1555 1555 2.42
LINK OD1 ASP C 58 CA CA C 202 1555 1555 2.48
LINK OD1 ASN C 60 CA CA C 202 1555 1555 2.50
LINK O THR C 62 CA CA C 202 1555 1555 2.48
LINK OE1 GLU C 67 CA CA C 202 1555 1555 2.63
LINK OE2 GLU C 67 CA CA C 202 1555 1555 2.70
LINK CA CA C 201 O HOH C 307 1555 1555 2.70
SITE 1 AC1 6 ASP C 20 ASP C 22 ASP C 24 THR C 26
SITE 2 AC1 6 GLU C 31 HOH C 307
SITE 1 AC2 5 ASP C 56 ASP C 58 ASN C 60 THR C 62
SITE 2 AC2 5 GLU C 67
CRYST1 43.510 130.570 36.160 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 0.022983 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007659 0.000000 0.00000
SCALE3 0.000000 0.000000 0.027655 0.00000
(ATOM LINES ARE NOT SHOWN.)
END