HEADER METAL TRANSPORT 09-OCT-17 6B8L
TITLE CRYSTAL STRUCTURE OF THE APO/CAM:KV7.4 (KCNQ4) AB DOMAIN COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY KQT MEMBER 4;
COMPND 3 CHAIN: A, C, E, G;
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: CALMODULIN-1;
COMPND 9 CHAIN: B, D, F, H;
COMPND 10 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: KCNQ4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28;
SOURCE 11 MOL_ID: 2;
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;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: ROSETTA;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PEGST
KEYWDS ION CHANNEL, COMPLEX, METAL TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR A.CHANG,F.ABDEREMANE-ALI,D.L.MINOR
REVDAT 3 13-MAR-24 6B8L 1 REMARK
REVDAT 2 18-DEC-19 6B8L 1 REMARK
REVDAT 1 14-MAR-18 6B8L 0
JRNL AUTH A.CHANG,F.ABDEREMANE-ALI,G.L.HURA,N.D.ROSSEN,R.E.GATE,
JRNL AUTH 2 D.L.MINOR
JRNL TITL A CALMODULIN C-LOBE CA2+-DEPENDENT SWITCH GOVERNS KV7
JRNL TITL 2 CHANNEL FUNCTION
JRNL REF NEURON V. 97 836 2018
JRNL REFN ISSN 1097-4199
JRNL PMID 29429937
JRNL DOI 10.1016/J.NEURON.2018.01.035
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1_2575
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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.89
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 54987
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.198
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.960
REMARK 3 FREE R VALUE TEST SET COUNT : 5475
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 48.8996 - 7.0852 0.99 1859 207 0.1708 0.1846
REMARK 3 2 7.0852 - 5.6264 1.00 1801 201 0.2109 0.2411
REMARK 3 3 5.6264 - 4.9159 1.00 1768 195 0.1840 0.2285
REMARK 3 4 4.9159 - 4.4668 1.00 1762 196 0.1618 0.1906
REMARK 3 5 4.4668 - 4.1468 1.00 1762 197 0.1531 0.2039
REMARK 3 6 4.1468 - 3.9025 0.99 1711 191 0.1701 0.2187
REMARK 3 7 3.9025 - 3.7071 0.99 1731 196 0.1800 0.2262
REMARK 3 8 3.7071 - 3.5458 0.98 1709 189 0.2196 0.2603
REMARK 3 9 3.5458 - 3.4093 0.99 1728 193 0.1992 0.2632
REMARK 3 10 3.4093 - 3.2917 0.99 1708 190 0.2149 0.2607
REMARK 3 11 3.2917 - 3.1888 0.99 1722 193 0.2194 0.2653
REMARK 3 12 3.1888 - 3.0976 0.99 1720 190 0.2280 0.2601
REMARK 3 13 3.0976 - 3.0161 0.99 1715 191 0.2200 0.2818
REMARK 3 14 3.0161 - 2.9425 0.98 1723 191 0.2259 0.2634
REMARK 3 15 2.9425 - 2.8756 0.97 1679 186 0.2227 0.2899
REMARK 3 16 2.8756 - 2.8145 0.97 1678 186 0.2151 0.3154
REMARK 3 17 2.8145 - 2.7582 0.96 1646 181 0.2223 0.2612
REMARK 3 18 2.7582 - 2.7061 0.95 1642 190 0.2330 0.2864
REMARK 3 19 2.7061 - 2.6578 0.95 1665 183 0.2231 0.2565
REMARK 3 20 2.6578 - 2.6127 0.95 1631 177 0.2143 0.2579
REMARK 3 21 2.6127 - 2.5706 0.94 1610 181 0.2015 0.3178
REMARK 3 22 2.5706 - 2.5310 0.93 1573 172 0.2194 0.2689
REMARK 3 23 2.5310 - 2.4938 0.94 1635 178 0.2118 0.3143
REMARK 3 24 2.4938 - 2.4587 0.92 1585 175 0.2280 0.2887
REMARK 3 25 2.4587 - 2.4255 0.90 1554 167 0.2268 0.3202
REMARK 3 26 2.4255 - 2.3940 0.91 1585 172 0.2311 0.2873
REMARK 3 27 2.3940 - 2.3641 0.90 1539 168 0.2131 0.2843
REMARK 3 28 2.3641 - 2.3356 0.90 1529 168 0.2109 0.2939
REMARK 3 29 2.3356 - 2.3084 0.88 1528 158 0.2286 0.3058
REMARK 3 30 2.3084 - 2.2825 0.59 1014 113 0.2108 0.2842
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) : 0.270
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.500
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.47
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.03
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 : 0.007 7074
REMARK 3 ANGLE : 0.840 9505
REMARK 3 CHIRALITY : 0.047 1042
REMARK 3 PLANARITY : 0.005 1239
REMARK 3 DIHEDRAL : 21.646 2713
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 6B8L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-OCT-17.
REMARK 100 THE DEPOSITION ID IS D_1000230454.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-MAR-15; 20-AUG-16
REMARK 200 TEMPERATURE (KELVIN) : 80; 80
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : ALS; APS
REMARK 200 BEAMLINE : 8.3.1; 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9797; 1.072
REMARK 200 MONOCHROMATOR : DOUBLE FLAT CRYSTAL, SI(111);
REMARK 200 SI(111) DOUBLE CRYSTAL KHOZU
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; PIXEL
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R; DECTRIS
REMARK 200 PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 57501
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.300
REMARK 200 R MERGE (I) : 0.11900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.40
REMARK 200 R MERGE FOR SHELL (I) : 0.92800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.96
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULFATE, 0.1M BISTRIS PH
REMARK 280 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 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,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 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 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 54.21750
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 71.22650
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 82.15650
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 54.21750
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 71.22650
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 82.15650
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 54.21750
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 71.22650
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 82.15650
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 54.21750
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 71.22650
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 82.15650
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: 3940 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11890 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 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 350
REMARK 350 BIOMOLECULE: 2
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: 4050 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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: 3
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: 4020 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F
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: 4
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: 4520 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12200 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H
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 GLY A 322
REMARK 465 HIS A 323
REMARK 465 MET A 324
REMARK 465 LYS A 325
REMARK 465 VAL A 326
REMARK 465 GLN A 327
REMARK 465 GLU A 328
REMARK 465 GLN A 329
REMARK 465 HIS A 330
REMARK 465 ARG A 331
REMARK 465 ARG A 554
REMARK 465 PRO A 555
REMARK 465 TYR A 556
REMARK 465 ASP A 557
REMARK 465 MET B 0
REMARK 465 ALA B 1
REMARK 465 ASP B 2
REMARK 465 LYS B 148
REMARK 465 GLY C 322
REMARK 465 HIS C 323
REMARK 465 MET C 324
REMARK 465 LYS C 325
REMARK 465 VAL C 326
REMARK 465 GLN C 327
REMARK 465 GLU C 328
REMARK 465 GLN C 329
REMARK 465 ARG C 554
REMARK 465 PRO C 555
REMARK 465 TYR C 556
REMARK 465 ASP C 557
REMARK 465 MET D 0
REMARK 465 ALA D 1
REMARK 465 ASP D 2
REMARK 465 LYS D 148
REMARK 465 GLY E 322
REMARK 465 HIS E 323
REMARK 465 MET E 324
REMARK 465 LYS E 325
REMARK 465 VAL E 326
REMARK 465 GLN E 327
REMARK 465 GLU E 328
REMARK 465 GLN E 329
REMARK 465 HIS E 330
REMARK 465 ARG E 331
REMARK 465 ARG E 554
REMARK 465 PRO E 555
REMARK 465 TYR E 556
REMARK 465 ASP E 557
REMARK 465 MET F 0
REMARK 465 ALA F 1
REMARK 465 ASP F 2
REMARK 465 LYS F 148
REMARK 465 GLY G 322
REMARK 465 HIS G 323
REMARK 465 MET G 324
REMARK 465 LYS G 325
REMARK 465 VAL G 326
REMARK 465 GLN G 327
REMARK 465 GLU G 328
REMARK 465 GLN G 329
REMARK 465 PRO G 555
REMARK 465 TYR G 556
REMARK 465 ASP G 557
REMARK 465 MET H 0
REMARK 465 ALA H 1
REMARK 465 LYS H 148
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU B 14 CD
REMARK 480 GLU B 114 CD
REMARK 480 GLU D 11 CD
REMARK 480 GLU F 6 CD
REMARK 480 GLU F 104 CD
REMARK 480 GLU H 7 CD
REMARK 480 ASP H 58 CG
REMARK 480 GLU H 104 CD
REMARK 480 GLU H 123 CD
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 ALA F 10 OE2 GLU F 14 1.68
REMARK 500 O HOH E 613 O HOH E 631 2.02
REMARK 500 OE1 GLN H 3 O HOH H 301 2.07
REMARK 500 O HOH D 311 O HOH E 617 2.12
REMARK 500 OD2 ASP H 58 O HOH H 302 2.13
REMARK 500 O HOH D 336 O HOH F 218 2.15
REMARK 500 OE2 GLU H 54 O HOH H 303 2.15
REMARK 500 OE1 GLU E 336 O HOH E 601 2.16
REMARK 500 OD1 ASP B 78 O HOH B 201 2.19
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 LEU A 362 56.47 -94.83
REMARK 500 LYS B 75 -119.32 54.35
REMARK 500 LYS B 77 47.55 -88.71
REMARK 500 THR B 146 38.67 -95.59
REMARK 500 LYS D 75 -113.28 39.35
REMARK 500 LYS F 75 -125.01 52.57
REMARK 500 MET G 357 -1.34 -143.05
REMARK 500 LEU G 362 64.29 -100.52
REMARK 500 LYS H 75 -116.37 48.68
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 202
DBREF 6B8L A 325 367 UNP P56696 KCNQ4_HUMAN 325 367
DBREF 6B8L A 524 557 UNP P56696 KCNQ4_HUMAN 524 557
DBREF 6B8L B 0 148 UNP P0DP23 CALM1_HUMAN 1 149
DBREF 6B8L C 325 367 UNP P56696 KCNQ4_HUMAN 325 367
DBREF 6B8L C 524 557 UNP P56696 KCNQ4_HUMAN 524 557
DBREF 6B8L D 0 148 UNP P0DP23 CALM1_HUMAN 1 149
DBREF 6B8L E 325 367 UNP P56696 KCNQ4_HUMAN 325 367
DBREF 6B8L E 524 557 UNP P56696 KCNQ4_HUMAN 524 557
DBREF 6B8L F 0 148 UNP P0DP23 CALM1_HUMAN 1 149
DBREF 6B8L G 325 367 UNP P56696 KCNQ4_HUMAN 325 367
DBREF 6B8L G 524 557 UNP P56696 KCNQ4_HUMAN 524 557
DBREF 6B8L H 0 148 UNP P0DP23 CALM1_HUMAN 1 149
SEQADV 6B8L GLY A 322 UNP P56696 EXPRESSION TAG
SEQADV 6B8L HIS A 323 UNP P56696 EXPRESSION TAG
SEQADV 6B8L MET A 324 UNP P56696 EXPRESSION TAG
SEQADV 6B8L LYS A 368 UNP P56696 LINKER
SEQADV 6B8L LEU A 369 UNP P56696 LINKER
SEQADV 6B8L GLY C 322 UNP P56696 EXPRESSION TAG
SEQADV 6B8L HIS C 323 UNP P56696 EXPRESSION TAG
SEQADV 6B8L MET C 324 UNP P56696 EXPRESSION TAG
SEQADV 6B8L LYS C 368 UNP P56696 LINKER
SEQADV 6B8L LEU C 369 UNP P56696 LINKER
SEQADV 6B8L GLY E 322 UNP P56696 EXPRESSION TAG
SEQADV 6B8L HIS E 323 UNP P56696 EXPRESSION TAG
SEQADV 6B8L MET E 324 UNP P56696 EXPRESSION TAG
SEQADV 6B8L LYS E 368 UNP P56696 LINKER
SEQADV 6B8L LEU E 369 UNP P56696 LINKER
SEQADV 6B8L GLY G 322 UNP P56696 EXPRESSION TAG
SEQADV 6B8L HIS G 323 UNP P56696 EXPRESSION TAG
SEQADV 6B8L MET G 324 UNP P56696 EXPRESSION TAG
SEQADV 6B8L LYS G 368 UNP P56696 LINKER
SEQADV 6B8L LEU G 369 UNP P56696 LINKER
SEQRES 1 A 82 GLY HIS MET LYS VAL GLN GLU GLN HIS ARG GLN LYS HIS
SEQRES 2 A 82 PHE GLU LYS ARG ARG MET PRO ALA ALA ASN LEU ILE GLN
SEQRES 3 A 82 ALA ALA TRP ARG LEU TYR SER THR ASP MET SER ARG ALA
SEQRES 4 A 82 TYR LEU THR ALA THR TRP TYR LYS LEU ASP ASP ILE MET
SEQRES 5 A 82 PRO ALA VAL LYS THR VAL ILE ARG SER ILE ARG ILE LEU
SEQRES 6 A 82 LYS PHE LEU VAL ALA LYS ARG LYS PHE LYS GLU THR LEU
SEQRES 7 A 82 ARG PRO TYR ASP
SEQRES 1 B 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 B 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 B 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 B 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 B 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 B 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 B 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 B 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 B 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 B 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 B 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 B 149 GLN MET MET THR ALA LYS
SEQRES 1 C 82 GLY HIS MET LYS VAL GLN GLU GLN HIS ARG GLN LYS HIS
SEQRES 2 C 82 PHE GLU LYS ARG ARG MET PRO ALA ALA ASN LEU ILE GLN
SEQRES 3 C 82 ALA ALA TRP ARG LEU TYR SER THR ASP MET SER ARG ALA
SEQRES 4 C 82 TYR LEU THR ALA THR TRP TYR LYS LEU ASP ASP ILE MET
SEQRES 5 C 82 PRO ALA VAL LYS THR VAL ILE ARG SER ILE ARG ILE LEU
SEQRES 6 C 82 LYS PHE LEU VAL ALA LYS ARG LYS PHE LYS GLU THR LEU
SEQRES 7 C 82 ARG PRO TYR ASP
SEQRES 1 D 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 D 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 D 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 D 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 D 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 D 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 D 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 D 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 D 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 D 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 D 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 D 149 GLN MET MET THR ALA LYS
SEQRES 1 E 82 GLY HIS MET LYS VAL GLN GLU GLN HIS ARG GLN LYS HIS
SEQRES 2 E 82 PHE GLU LYS ARG ARG MET PRO ALA ALA ASN LEU ILE GLN
SEQRES 3 E 82 ALA ALA TRP ARG LEU TYR SER THR ASP MET SER ARG ALA
SEQRES 4 E 82 TYR LEU THR ALA THR TRP TYR LYS LEU ASP ASP ILE MET
SEQRES 5 E 82 PRO ALA VAL LYS THR VAL ILE ARG SER ILE ARG ILE LEU
SEQRES 6 E 82 LYS PHE LEU VAL ALA LYS ARG LYS PHE LYS GLU THR LEU
SEQRES 7 E 82 ARG PRO TYR ASP
SEQRES 1 F 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 F 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 F 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 F 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 F 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 F 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 F 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 F 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 F 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 F 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 F 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 F 149 GLN MET MET THR ALA LYS
SEQRES 1 G 82 GLY HIS MET LYS VAL GLN GLU GLN HIS ARG GLN LYS HIS
SEQRES 2 G 82 PHE GLU LYS ARG ARG MET PRO ALA ALA ASN LEU ILE GLN
SEQRES 3 G 82 ALA ALA TRP ARG LEU TYR SER THR ASP MET SER ARG ALA
SEQRES 4 G 82 TYR LEU THR ALA THR TRP TYR LYS LEU ASP ASP ILE MET
SEQRES 5 G 82 PRO ALA VAL LYS THR VAL ILE ARG SER ILE ARG ILE LEU
SEQRES 6 G 82 LYS PHE LEU VAL ALA LYS ARG LYS PHE LYS GLU THR LEU
SEQRES 7 G 82 ARG PRO TYR ASP
SEQRES 1 H 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE
SEQRES 2 H 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY
SEQRES 3 H 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER
SEQRES 4 H 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET
SEQRES 5 H 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP
SEQRES 6 H 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS
SEQRES 7 H 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG
SEQRES 8 H 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA
SEQRES 9 H 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU
SEQRES 10 H 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP
SEQRES 11 H 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL
SEQRES 12 H 149 GLN MET MET THR ALA LYS
HET SO4 D 201 5
HET SO4 D 202 5
HET SO4 G 601 5
HET SO4 H 201 5
HET SO4 H 202 5
HETNAM SO4 SULFATE ION
FORMUL 9 SO4 5(O4 S 2-)
FORMUL 14 HOH *284(H2 O)
HELIX 1 AA1 ARG A 338 THR A 355 1 18
HELIX 2 AA2 ASP A 356 MET A 357 5 2
HELIX 3 AA3 SER A 358 LEU A 362 5 5
HELIX 4 AA4 THR A 363 MET A 527 1 11
HELIX 5 AA5 PRO A 528 GLU A 551 1 24
HELIX 6 AA6 THR B 5 ASP B 20 1 16
HELIX 7 AA7 THR B 28 LEU B 39 1 12
HELIX 8 AA8 THR B 44 GLU B 54 1 11
HELIX 9 AA9 PHE B 65 LYS B 75 1 11
HELIX 10 AB1 ASP B 78 PHE B 92 1 15
HELIX 11 AB2 ALA B 102 LEU B 112 1 11
HELIX 12 AB3 THR B 117 ALA B 128 1 12
HELIX 13 AB4 TYR B 138 THR B 146 1 9
HELIX 14 AB5 ARG C 331 PHE C 335 1 5
HELIX 15 AB6 ARG C 338 THR C 355 1 18
HELIX 16 AB7 ASP C 356 MET C 357 5 2
HELIX 17 AB8 SER C 358 LEU C 362 5 5
HELIX 18 AB9 THR C 363 MET C 527 1 11
HELIX 19 AC1 PRO C 528 THR C 552 1 25
HELIX 20 AC2 GLU D 7 ASP D 20 1 14
HELIX 21 AC3 THR D 28 LEU D 39 1 12
HELIX 22 AC4 THR D 44 ASP D 56 1 13
HELIX 23 AC5 PHE D 65 LYS D 75 1 11
HELIX 24 AC6 ASP D 78 VAL D 91 1 14
HELIX 25 AC7 ALA D 102 LEU D 112 1 11
HELIX 26 AC8 THR D 117 ASP D 129 1 13
HELIX 27 AC9 TYR D 138 THR D 146 1 9
HELIX 28 AD1 HIS E 334 SER E 354 1 21
HELIX 29 AD2 SER E 358 LEU E 362 5 5
HELIX 30 AD3 THR E 363 MET E 527 1 11
HELIX 31 AD4 PRO E 528 GLU E 551 1 24
HELIX 32 AD5 THR F 5 ASP F 20 1 16
HELIX 33 AD6 THR F 28 LEU F 39 1 12
HELIX 34 AD7 THR F 44 GLU F 54 1 11
HELIX 35 AD8 ASP F 64 LYS F 75 1 12
HELIX 36 AD9 ASP F 78 PHE F 92 1 15
HELIX 37 AE1 ALA F 102 LEU F 112 1 11
HELIX 38 AE2 THR F 117 ALA F 128 1 12
HELIX 39 AE3 TYR F 138 THR F 146 1 9
HELIX 40 AE4 HIS G 334 THR G 355 1 22
HELIX 41 AE5 ASP G 356 MET G 357 5 2
HELIX 42 AE6 SER G 358 LEU G 362 5 5
HELIX 43 AE7 THR G 363 MET G 527 1 11
HELIX 44 AE8 PRO G 528 GLU G 551 1 24
HELIX 45 AE9 THR G 552 ARG G 554 5 3
HELIX 46 AF1 THR H 5 ASP H 20 1 16
HELIX 47 AF2 THR H 28 LEU H 39 1 12
HELIX 48 AF3 THR H 44 GLU H 54 1 11
HELIX 49 AF4 PHE H 65 LYS H 75 1 11
HELIX 50 AF5 ASP H 78 PHE H 92 1 15
HELIX 51 AF6 ALA H 102 LEU H 112 1 11
HELIX 52 AF7 THR H 117 ALA H 128 1 12
HELIX 53 AF8 TYR H 138 THR H 146 1 9
SHEET 1 AA1 2 THR B 26 ILE B 27 0
SHEET 2 AA1 2 ILE B 63 ASP B 64 -1 O ILE B 63 N ILE B 27
SHEET 1 AA2 2 TYR B 99 SER B 101 0
SHEET 2 AA2 2 GLN B 135 ASN B 137 -1 O VAL B 136 N ILE B 100
SHEET 1 AA3 2 THR D 26 ILE D 27 0
SHEET 2 AA3 2 ILE D 63 ASP D 64 -1 O ILE D 63 N ILE D 27
SHEET 1 AA4 2 TYR D 99 SER D 101 0
SHEET 2 AA4 2 GLN D 135 ASN D 137 -1 O VAL D 136 N ILE D 100
SHEET 1 AA5 2 TYR F 99 SER F 101 0
SHEET 2 AA5 2 GLN F 135 ASN F 137 -1 O VAL F 136 N ILE F 100
SHEET 1 AA6 2 THR H 26 ILE H 27 0
SHEET 2 AA6 2 ILE H 63 ASP H 64 -1 O ILE H 63 N ILE H 27
SHEET 1 AA7 2 TYR H 99 SER H 101 0
SHEET 2 AA7 2 GLN H 135 ASN H 137 -1 O VAL H 136 N ILE H 100
SITE 1 AC1 4 GLN D 41 ASN D 42 GLN F 41 ASN F 42
SITE 1 AC2 4 LYS D 21 LYS D 30 HOH D 311 ARG E 359
SITE 1 AC3 4 PHE E 335 ARG E 339 ARG G 331 PHE G 335
SITE 1 AC4 5 GLN B 41 ASN B 42 GLY H 40 GLN H 41
SITE 2 AC4 5 ASN H 42
SITE 1 AC5 2 LYS H 21 LYS H 30
CRYST1 108.435 142.453 164.313 90.00 90.00 90.00 I 2 2 2 32
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 0.009222 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007020 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006086 0.00000
(ATOM LINES ARE NOT SHOWN.)
END