HEADER METAL TRANSPORT 19-NOV-14 4RUF
TITLE HUMAN K2P4.1 (TRAAAK) POTASSIUM CHANNEL, W262S MUTANT
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POTASSIUM CHANNEL SUBFAMILY K MEMBER 4;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 1-300;
COMPND 5 SYNONYM: TWIK-RELATED ARACHIDONIC ACID-STIMULATED POTASSIUM CHANNEL
COMPND 6 PROTEIN, TRAAK, TWO PORE POTASSIUM CHANNEL KT4.1, TWO PORE K(+)
COMPND 7 CHANNEL KT4.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: KCNK4, TRAAK;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SMD1163
KEYWDS TRAAK POTASSIUM ION CHANNEL, METAL TRANSPORT
EXPDTA X-RAY DIFFRACTION
AUTHOR M.LOLICATO,D.L.JR.MINOR
REVDAT 4 20-SEP-23 4RUF 1 REMARK SEQADV LINK
REVDAT 3 22-NOV-17 4RUF 1 REMARK
REVDAT 2 07-JAN-15 4RUF 1 JRNL
REVDAT 1 17-DEC-14 4RUF 0
JRNL AUTH M.LOLICATO,P.M.RIEGELHAUPT,C.ARRIGONI,K.A.CLARK,D.L.MINOR
JRNL TITL TRANSMEMBRANE HELIX STRAIGHTENING AND BUCKLING UNDERLIES
JRNL TITL 2 ACTIVATION OF MECHANOSENSITIVE AND THERMOSENSITIVE K2P
JRNL TITL 3 CHANNELS.
JRNL REF NEURON V. 84 1198 2014
JRNL REFN ISSN 0896-6273
JRNL PMID 25500157
JRNL DOI 10.1016/J.NEURON.2014.11.017
REMARK 2
REMARK 2 RESOLUTION. 3.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.8.4_1496)
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) : 3.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 14.99
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.120
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 38347
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.299
REMARK 3 R VALUE (WORKING SET) : 0.297
REMARK 3 FREE R VALUE : 0.328
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980
REMARK 3 FREE R VALUE TEST SET COUNT : 1911
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 14.9936 - 7.8181 1.00 2604 150 0.2150 0.2419
REMARK 3 2 7.8181 - 6.3592 1.00 2648 123 0.2855 0.3314
REMARK 3 3 6.3592 - 5.6032 1.00 2609 145 0.3208 0.3710
REMARK 3 4 5.6032 - 5.1132 1.00 2601 146 0.2825 0.2739
REMARK 3 5 5.1132 - 4.7593 0.98 2541 175 0.2617 0.3510
REMARK 3 6 4.7593 - 4.4866 0.98 2558 154 0.2961 0.3263
REMARK 3 7 4.4866 - 4.2674 0.98 2575 129 0.3303 0.3847
REMARK 3 8 4.2674 - 4.0855 0.98 2543 185 0.3470 0.4045
REMARK 3 9 4.0855 - 3.9312 0.99 2636 127 0.3763 0.4085
REMARK 3 10 3.9312 - 3.7978 0.99 2622 112 0.4119 0.4475
REMARK 3 11 3.7978 - 3.6808 0.99 2584 127 0.4184 0.4766
REMARK 3 12 3.6808 - 3.5771 0.98 2582 125 0.4734 0.5208
REMARK 3 13 3.5771 - 3.4841 1.00 2697 95 0.4428 0.5012
REMARK 3 14 3.4841 - 3.4000 1.00 2638 118 0.4242 0.4387
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) : 0.700
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 46.910
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 : 0.003 4017
REMARK 3 ANGLE : 0.852 5472
REMARK 3 CHIRALITY : 0.026 638
REMARK 3 PLANARITY : 0.006 683
REMARK 3 DIHEDRAL : 18.229 2392
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 4RUF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-NOV-14.
REMARK 100 THE DEPOSITION ID IS D_1000087808.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 06-DEC-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 6
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.03320
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38349
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400
REMARK 200 RESOLUTION RANGE LOW (A) : 48.310
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
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) : 3.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
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: 4I9W
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 77.58
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.49
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG400, 10MM SARCOSINE, PH 8.0,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277.15K
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 44.02650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 65.20300
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 63.99100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 65.20300
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 44.02650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 63.99100
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: 10110 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28000 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -98.0 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 MET A 1
REMARK 465 THR A 2
REMARK 465 THR A 3
REMARK 465 ALA A 4
REMARK 465 PRO A 5
REMARK 465 GLN A 6
REMARK 465 GLU A 7
REMARK 465 PRO A 8
REMARK 465 PRO A 9
REMARK 465 ALA A 10
REMARK 465 ARG A 11
REMARK 465 PRO A 12
REMARK 465 LEU A 13
REMARK 465 GLN A 14
REMARK 465 ALA A 15
REMARK 465 GLY A 16
REMARK 465 SER A 17
REMARK 465 GLY A 18
REMARK 465 ALA A 19
REMARK 465 THR A 103
REMARK 465 GLN A 104
REMARK 465 SER A 105
REMARK 465 THR A 106
REMARK 465 SER A 107
REMARK 465 GLN A 108
REMARK 465 SER A 109
REMARK 465 ARG A 284
REMARK 465 VAL A 285
REMARK 465 VAL A 286
REMARK 465 SER A 287
REMARK 465 ARG A 288
REMARK 465 ARG A 289
REMARK 465 THR A 290
REMARK 465 ARG A 291
REMARK 465 ALA A 292
REMARK 465 GLU A 293
REMARK 465 MET A 294
REMARK 465 GLY A 295
REMARK 465 GLY A 296
REMARK 465 LEU A 297
REMARK 465 THR A 298
REMARK 465 ALA A 299
REMARK 465 GLN A 300
REMARK 465 SER A 301
REMARK 465 ASN A 302
REMARK 465 SER A 303
REMARK 465 LEU A 304
REMARK 465 GLU A 305
REMARK 465 VAL A 306
REMARK 465 LEU A 307
REMARK 465 PHE A 308
REMARK 465 GLN A 309
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 THR B 3
REMARK 465 ALA B 4
REMARK 465 PRO B 5
REMARK 465 GLN B 6
REMARK 465 GLU B 7
REMARK 465 PRO B 8
REMARK 465 PRO B 9
REMARK 465 ALA B 10
REMARK 465 ARG B 11
REMARK 465 PRO B 12
REMARK 465 LEU B 13
REMARK 465 GLN B 14
REMARK 465 ALA B 15
REMARK 465 GLY B 16
REMARK 465 SER B 17
REMARK 465 GLY B 18
REMARK 465 ALA B 19
REMARK 465 GLY B 20
REMARK 465 PRO B 21
REMARK 465 ALA B 22
REMARK 465 PRO B 23
REMARK 465 GLY B 24
REMARK 465 ARG B 25
REMARK 465 ALA B 26
REMARK 465 MET B 27
REMARK 465 THR B 106
REMARK 465 SER B 107
REMARK 465 GLN B 108
REMARK 465 SER B 109
REMARK 465 LEU B 283
REMARK 465 ARG B 284
REMARK 465 VAL B 285
REMARK 465 VAL B 286
REMARK 465 SER B 287
REMARK 465 ARG B 288
REMARK 465 ARG B 289
REMARK 465 THR B 290
REMARK 465 ARG B 291
REMARK 465 ALA B 292
REMARK 465 GLU B 293
REMARK 465 MET B 294
REMARK 465 GLY B 295
REMARK 465 GLY B 296
REMARK 465 LEU B 297
REMARK 465 THR B 298
REMARK 465 ALA B 299
REMARK 465 GLN B 300
REMARK 465 SER B 301
REMARK 465 ASN B 302
REMARK 465 SER B 303
REMARK 465 LEU B 304
REMARK 465 GLU B 305
REMARK 465 VAL B 306
REMARK 465 LEU B 307
REMARK 465 PHE B 308
REMARK 465 GLN B 309
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 SER A 110 OG
REMARK 470 HIS A 111 CG ND1 CD2 CE1 NE2
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 OE2 GLU A 102 NH2 ARG A 251 2.16
REMARK 500 O LEU A 172 N ILE A 176 2.18
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 PRO A 189 C - N - CA ANGL. DEV. = 11.7 DEGREES
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 GLU A 58 -57.87 -135.92
REMARK 500 GLN A 60 44.50 -91.91
REMARK 500 ALA A 61 -41.45 -144.46
REMARK 500 HIS A 111 41.17 -94.97
REMARK 500 TRP A 114 14.42 -142.79
REMARK 500 THR A 129 15.80 59.10
REMARK 500 TRP A 186 35.46 -81.29
REMARK 500 VAL A 195 -28.76 -144.75
REMARK 500 VAL A 210 -64.66 -132.86
REMARK 500 THR A 238 16.67 59.85
REMARK 500 VAL A 245 -50.43 -127.29
REMARK 500 ASP A 253 -53.88 69.73
REMARK 500 GLU B 54 -28.35 -140.52
REMARK 500 HIS B 111 86.56 61.29
REMARK 500 THR B 129 19.90 58.28
REMARK 500 ARG B 138 -46.72 -142.39
REMARK 500 TRP B 186 32.21 -80.09
REMARK 500 HIS B 187 19.40 59.48
REMARK 500 VAL B 210 -55.84 -135.03
REMARK 500 TYR B 219 -60.33 -101.18
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 K A 401 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 129 O
REMARK 620 2 ILE A 130 O 74.7
REMARK 620 3 THR A 238 O 64.0 90.2
REMARK 620 4 VAL A 239 O 132.0 78.4 77.2
REMARK 620 5 THR B 129 O 98.7 154.1 64.8 88.6
REMARK 620 6 ILE B 130 O 153.4 120.5 131.7 74.4 76.2
REMARK 620 7 THR B 238 O 63.0 127.0 98.0 154.5 67.1 91.5
REMARK 620 8 VAL B 239 O 88.1 68.7 149.1 117.8 136.9 79.1 79.0
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 402 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 129 OG1
REMARK 620 2 THR A 129 O 65.3
REMARK 620 3 THR A 238 OG1 81.1 106.8
REMARK 620 4 THR A 238 O 100.4 60.8 64.9
REMARK 620 5 THR B 129 OG1 137.0 157.4 78.5 104.3
REMARK 620 6 THR B 129 O 158.4 93.7 101.6 62.7 63.7
REMARK 620 7 THR B 238 OG1 88.7 104.4 139.2 155.8 82.8 102.0
REMARK 620 8 THR B 238 O 105.7 59.3 157.3 92.5 107.7 64.3 63.4
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K B 401 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ILE A 130 O
REMARK 620 2 GLY A 131 O 65.1
REMARK 620 3 VAL A 239 O 79.0 131.2
REMARK 620 4 GLY A 240 O 77.1 71.0 69.6
REMARK 620 5 ILE B 130 O 124.3 152.8 75.2 133.8
REMARK 620 6 GLY B 131 O 149.1 119.0 77.5 76.1 67.8
REMARK 620 7 VAL B 239 O 73.8 72.2 128.9 140.1 85.6 137.0
REMARK 620 8 GLY B 240 O 135.6 77.9 145.4 113.9 80.4 70.6 72.1
REMARK 620 N 1 2 3 4 5 6 7
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 K A 403 K
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLY A 131 O
REMARK 620 2 TYR A 132 O 74.2
REMARK 620 3 GLY A 240 O 64.7 90.1
REMARK 620 4 PHE A 241 O 125.6 71.9 74.1
REMARK 620 5 GLY B 131 O 103.7 155.7 68.0 91.4
REMARK 620 6 TYR B 132 O 155.8 120.1 129.7 78.5 71.4
REMARK 620 7 GLY B 240 O 73.4 133.5 105.0 154.4 65.5 83.3
REMARK 620 8 PHE B 241 O 96.2 79.7 160.4 117.5 124.3 69.7 71.7
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 K A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4RUE RELATED DB: PDB
REMARK 900 G124I MUTANT
DBREF 4RUF A 1 300 UNP Q9NYG8 KCNK4_HUMAN 1 300
DBREF 4RUF B 1 300 UNP Q9NYG8 KCNK4_HUMAN 1 300
SEQADV 4RUF GLN A 104 UNP Q9NYG8 ASN 104 ENGINEERED MUTATION
SEQADV 4RUF GLN A 108 UNP Q9NYG8 ASN 108 ENGINEERED MUTATION
SEQADV 4RUF SER A 262 UNP Q9NYG8 TRP 262 ENGINEERED MUTATION
SEQADV 4RUF SER A 301 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4RUF ASN A 302 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4RUF SER A 303 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4RUF LEU A 304 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4RUF GLU A 305 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4RUF VAL A 306 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4RUF LEU A 307 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4RUF PHE A 308 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4RUF GLN A 309 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4RUF GLN B 104 UNP Q9NYG8 ASN 104 ENGINEERED MUTATION
SEQADV 4RUF GLN B 108 UNP Q9NYG8 ASN 108 ENGINEERED MUTATION
SEQADV 4RUF SER B 262 UNP Q9NYG8 TRP 262 ENGINEERED MUTATION
SEQADV 4RUF SER B 301 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4RUF ASN B 302 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4RUF SER B 303 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4RUF LEU B 304 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4RUF GLU B 305 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4RUF VAL B 306 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4RUF LEU B 307 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4RUF PHE B 308 UNP Q9NYG8 EXPRESSION TAG
SEQADV 4RUF GLN B 309 UNP Q9NYG8 EXPRESSION TAG
SEQRES 1 A 309 MET THR THR ALA PRO GLN GLU PRO PRO ALA ARG PRO LEU
SEQRES 2 A 309 GLN ALA GLY SER GLY ALA GLY PRO ALA PRO GLY ARG ALA
SEQRES 3 A 309 MET ARG SER THR THR LEU LEU ALA LEU LEU ALA LEU VAL
SEQRES 4 A 309 LEU LEU TYR LEU VAL SER GLY ALA LEU VAL PHE ARG ALA
SEQRES 5 A 309 LEU GLU GLN PRO HIS GLU GLN GLN ALA GLN ARG GLU LEU
SEQRES 6 A 309 GLY GLU VAL ARG GLU LYS PHE LEU ARG ALA HIS PRO CYS
SEQRES 7 A 309 VAL SER ASP GLN GLU LEU GLY LEU LEU ILE LYS GLU VAL
SEQRES 8 A 309 ALA ASP ALA LEU GLY GLY GLY ALA ASP PRO GLU THR GLN
SEQRES 9 A 309 SER THR SER GLN SER SER HIS SER ALA TRP ASP LEU GLY
SEQRES 10 A 309 SER ALA PHE PHE PHE SER GLY THR ILE ILE THR THR ILE
SEQRES 11 A 309 GLY TYR GLY ASN VAL ALA LEU ARG THR ASP ALA GLY ARG
SEQRES 12 A 309 LEU PHE CYS ILE PHE TYR ALA LEU VAL GLY ILE PRO LEU
SEQRES 13 A 309 PHE GLY ILE LEU LEU ALA GLY VAL GLY ASP ARG LEU GLY
SEQRES 14 A 309 SER SER LEU ARG HIS GLY ILE GLY HIS ILE GLU ALA ILE
SEQRES 15 A 309 PHE LEU LYS TRP HIS VAL PRO PRO GLU LEU VAL ARG VAL
SEQRES 16 A 309 LEU SER ALA MET LEU PHE LEU LEU ILE GLY CYS LEU LEU
SEQRES 17 A 309 PHE VAL LEU THR PRO THR PHE VAL PHE CYS TYR MET GLU
SEQRES 18 A 309 ASP TRP SER LYS LEU GLU ALA ILE TYR PHE VAL ILE VAL
SEQRES 19 A 309 THR LEU THR THR VAL GLY PHE GLY ASP TYR VAL ALA GLY
SEQRES 20 A 309 ALA ASP PRO ARG GLN ASP SER PRO ALA TYR GLN PRO LEU
SEQRES 21 A 309 VAL SER PHE TRP ILE LEU LEU GLY LEU ALA TYR PHE ALA
SEQRES 22 A 309 SER VAL LEU THR THR ILE GLY ASN TRP LEU ARG VAL VAL
SEQRES 23 A 309 SER ARG ARG THR ARG ALA GLU MET GLY GLY LEU THR ALA
SEQRES 24 A 309 GLN SER ASN SER LEU GLU VAL LEU PHE GLN
SEQRES 1 B 309 MET THR THR ALA PRO GLN GLU PRO PRO ALA ARG PRO LEU
SEQRES 2 B 309 GLN ALA GLY SER GLY ALA GLY PRO ALA PRO GLY ARG ALA
SEQRES 3 B 309 MET ARG SER THR THR LEU LEU ALA LEU LEU ALA LEU VAL
SEQRES 4 B 309 LEU LEU TYR LEU VAL SER GLY ALA LEU VAL PHE ARG ALA
SEQRES 5 B 309 LEU GLU GLN PRO HIS GLU GLN GLN ALA GLN ARG GLU LEU
SEQRES 6 B 309 GLY GLU VAL ARG GLU LYS PHE LEU ARG ALA HIS PRO CYS
SEQRES 7 B 309 VAL SER ASP GLN GLU LEU GLY LEU LEU ILE LYS GLU VAL
SEQRES 8 B 309 ALA ASP ALA LEU GLY GLY GLY ALA ASP PRO GLU THR GLN
SEQRES 9 B 309 SER THR SER GLN SER SER HIS SER ALA TRP ASP LEU GLY
SEQRES 10 B 309 SER ALA PHE PHE PHE SER GLY THR ILE ILE THR THR ILE
SEQRES 11 B 309 GLY TYR GLY ASN VAL ALA LEU ARG THR ASP ALA GLY ARG
SEQRES 12 B 309 LEU PHE CYS ILE PHE TYR ALA LEU VAL GLY ILE PRO LEU
SEQRES 13 B 309 PHE GLY ILE LEU LEU ALA GLY VAL GLY ASP ARG LEU GLY
SEQRES 14 B 309 SER SER LEU ARG HIS GLY ILE GLY HIS ILE GLU ALA ILE
SEQRES 15 B 309 PHE LEU LYS TRP HIS VAL PRO PRO GLU LEU VAL ARG VAL
SEQRES 16 B 309 LEU SER ALA MET LEU PHE LEU LEU ILE GLY CYS LEU LEU
SEQRES 17 B 309 PHE VAL LEU THR PRO THR PHE VAL PHE CYS TYR MET GLU
SEQRES 18 B 309 ASP TRP SER LYS LEU GLU ALA ILE TYR PHE VAL ILE VAL
SEQRES 19 B 309 THR LEU THR THR VAL GLY PHE GLY ASP TYR VAL ALA GLY
SEQRES 20 B 309 ALA ASP PRO ARG GLN ASP SER PRO ALA TYR GLN PRO LEU
SEQRES 21 B 309 VAL SER PHE TRP ILE LEU LEU GLY LEU ALA TYR PHE ALA
SEQRES 22 B 309 SER VAL LEU THR THR ILE GLY ASN TRP LEU ARG VAL VAL
SEQRES 23 B 309 SER ARG ARG THR ARG ALA GLU MET GLY GLY LEU THR ALA
SEQRES 24 B 309 GLN SER ASN SER LEU GLU VAL LEU PHE GLN
HET K A 401 1
HET K A 402 1
HET K A 403 1
HET K B 401 1
HET K B 402 1
HET K B 403 1
HETNAM K POTASSIUM ION
FORMUL 3 K 6(K 1+)
HELIX 1 1 GLY A 20 ARG A 28 1 9
HELIX 2 2 ARG A 28 GLN A 55 1 28
HELIX 3 3 ARG A 63 ARG A 74 1 12
HELIX 4 4 SER A 80 GLY A 96 1 17
HELIX 5 5 ASP A 115 THR A 128 1 14
HELIX 6 6 THR A 139 TRP A 186 1 48
HELIX 7 7 PRO A 189 VAL A 193 5 5
HELIX 8 8 ALA A 198 PHE A 209 1 12
HELIX 9 9 VAL A 210 GLU A 221 1 12
HELIX 10 10 SER A 224 THR A 237 1 14
HELIX 11 11 ALA A 256 LEU A 283 1 28
HELIX 12 12 SER B 29 LEU B 53 1 25
HELIX 13 13 GLU B 54 HIS B 76 1 23
HELIX 14 14 SER B 80 GLY B 97 1 18
HELIX 15 15 ASP B 115 THR B 128 1 14
HELIX 16 16 THR B 139 LEU B 184 1 46
HELIX 17 17 PRO B 189 VAL B 210 1 22
HELIX 18 18 VAL B 210 GLU B 221 1 12
HELIX 19 19 SER B 224 THR B 237 1 14
HELIX 20 20 ALA B 256 TRP B 282 1 27
SSBOND 1 CYS A 78 CYS B 78 1555 1555 2.03
LINK O THR A 129 K K A 401 1555 1555 2.73
LINK OG1 THR A 129 K K A 402 1555 1555 2.87
LINK O THR A 129 K K A 402 1555 1555 2.89
LINK O ILE A 130 K K A 401 1555 1555 2.79
LINK O ILE A 130 K K B 401 1555 1555 2.75
LINK O GLY A 131 K K A 403 1555 1555 3.00
LINK O GLY A 131 K K B 401 1555 1555 2.78
LINK O TYR A 132 K K A 403 1555 1555 2.78
LINK O THR A 238 K K A 401 1555 1555 2.76
LINK OG1 THR A 238 K K A 402 1555 1555 2.83
LINK O THR A 238 K K A 402 1555 1555 2.87
LINK O VAL A 239 K K A 401 1555 1555 2.76
LINK O VAL A 239 K K B 401 1555 1555 2.77
LINK O GLY A 240 K K A 403 1555 1555 2.96
LINK O GLY A 240 K K B 401 1555 1555 2.71
LINK O PHE A 241 K K A 403 1555 1555 2.95
LINK K K A 401 O THR B 129 1555 1555 2.78
LINK K K A 401 O ILE B 130 1555 1555 2.79
LINK K K A 401 O THR B 238 1555 1555 2.69
LINK K K A 401 O VAL B 239 1555 1555 3.01
LINK K K A 402 OG1 THR B 129 1555 1555 2.78
LINK K K A 402 O THR B 129 1555 1555 2.84
LINK K K A 402 OG1 THR B 238 1555 1555 2.68
LINK K K A 402 O THR B 238 1555 1555 2.84
LINK K K A 403 O GLY B 131 1555 1555 3.02
LINK K K A 403 O TYR B 132 1555 1555 2.78
LINK K K A 403 O GLY B 240 1555 1555 2.83
LINK K K A 403 O PHE B 241 1555 1555 3.28
LINK O ILE B 130 K K B 401 1555 1555 2.74
LINK O GLY B 131 K K B 401 1555 1555 2.72
LINK O VAL B 239 K K B 401 1555 1555 2.71
LINK O GLY B 240 K K B 401 1555 1555 2.77
CISPEP 1 VAL A 193 ARG A 194 0 7.36
CISPEP 2 GLY A 247 ALA A 248 0 8.87
SITE 1 AC1 9 THR A 129 ILE A 130 THR A 238 VAL A 239
SITE 2 AC1 9 THR B 129 ILE B 130 THR B 238 VAL B 239
SITE 3 AC1 9 K B 401
SITE 1 AC2 4 THR A 129 THR A 238 THR B 129 THR B 238
SITE 1 AC3 9 GLY A 131 TYR A 132 GLY A 240 PHE A 241
SITE 2 AC3 9 GLY B 131 TYR B 132 GLY B 240 PHE B 241
SITE 3 AC3 9 K B 401
SITE 1 AC4 10 ILE A 130 GLY A 131 VAL A 239 GLY A 240
SITE 2 AC4 10 K A 401 K A 403 ILE B 130 GLY B 131
SITE 3 AC4 10 VAL B 239 GLY B 240
CRYST1 88.053 127.982 130.406 90.00 90.00 90.00 P 21 21 21 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 0.011357 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007814 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007668 0.00000
(ATOM LINES ARE NOT SHOWN.)
END