HEADER PROTEIN BINDING 20-AUG-12 4GOW
TITLE CRYSTAL STRUCTURE OF CA2+/CAM:KV7.4 (KCNQ4) B HELIX COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALMODULIN;
COMPND 3 CHAIN: D;
COMPND 4 SYNONYM: CAM;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY KQT MEMBER 4;
COMPND 8 CHAIN: A;
COMPND 9 FRAGMENT: UNP RESIDUES 522-593;
COMPND 10 SYNONYM: KQT-LIKE 4, POTASSIUM CHANNEL SUBUNIT ALPHA KVLQT4, VOLTAGE-
COMPND 11 GATED POTASSIUM CHANNEL SUBUNIT KV7.4;
COMPND 12 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CALM1, CALM, CAM, CAM1, CALM2, CAM2, CAMB, CALM3, CALML2,
SOURCE 6 CAM3, CAMC, CAMIII;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET28;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 GENE: KCNQ4;
SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 18 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 19 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSS;
SOURCE 20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 21 EXPRESSION_SYSTEM_PLASMID: PET28
KEYWDS PROTEIN COMPLEX, PROTEIN BINDING, ION CHANNEL, CALMODULIN, POTASSIUM
KEYWDS 2 CHANNEL
EXPDTA X-RAY DIFFRACTION
AUTHOR Q.XU,A.CHANG,A.TOLIA,D.L.MINOR JR.
REVDAT 3 28-FEB-24 4GOW 1 REMARK LINK
REVDAT 2 22-MAY-13 4GOW 1 JRNL
REVDAT 1 12-DEC-12 4GOW 0
JRNL AUTH Q.XU,A.CHANG,A.TOLIA,D.L.MINOR
JRNL TITL STRUCTURE OF A CA(2+)/CAM:KV7.4 (KCNQ4) B-HELIX COMPLEX
JRNL TITL 2 PROVIDES INSIGHT INTO M CURRENT MODULATION.
JRNL REF J.MOL.BIOL. V. 425 378 2013
JRNL REFN ISSN 0022-2836
JRNL PMID 23178170
JRNL DOI 10.1016/J.JMB.2012.11.023
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.2_869
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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.09
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 11699
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.238
REMARK 3 R VALUE (WORKING SET) : 0.236
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 562
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 48.1011 - 4.1268 1.00 2932 157 0.2175 0.2201
REMARK 3 2 4.1268 - 3.2758 1.00 2758 139 0.2214 0.2889
REMARK 3 3 3.2758 - 2.8617 1.00 2755 118 0.2788 0.3394
REMARK 3 4 2.8617 - 2.6001 1.00 2692 148 0.3252 0.4055
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.20
REMARK 3 SHRINKAGE RADIUS : 0.98
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 55.17
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.570
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.710
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) : -3.82600
REMARK 3 B22 (A**2) : -3.82600
REMARK 3 B33 (A**2) : 7.65190
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 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 1351
REMARK 3 ANGLE : 0.790 1809
REMARK 3 CHIRALITY : 0.055 202
REMARK 3 PLANARITY : 0.003 241
REMARK 3 DIHEDRAL : 19.503 522
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 3:78)
REMARK 3 ORIGIN FOR THE GROUP (A): -34.6552 27.7043 -4.8043
REMARK 3 T TENSOR
REMARK 3 T11: 0.2971 T22: 0.2269
REMARK 3 T33: 0.2564 T12: -0.0618
REMARK 3 T13: -0.2212 T23: 0.0273
REMARK 3 L TENSOR
REMARK 3 L11: 4.5014 L22: 6.6490
REMARK 3 L33: 4.3616 L12: 0.4108
REMARK 3 L13: -0.3667 L23: 0.0144
REMARK 3 S TENSOR
REMARK 3 S11: -0.2434 S12: 0.4209 S13: 0.2464
REMARK 3 S21: -0.2187 S22: 0.5699 S23: 0.4436
REMARK 3 S31: 0.2098 S32: 0.0766 S33: -0.2663
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'D' AND (RESSEQ 81:146)
REMARK 3 ORIGIN FOR THE GROUP (A): -14.7476 27.5230 5.6861
REMARK 3 T TENSOR
REMARK 3 T11: 0.4320 T22: 0.6931
REMARK 3 T33: 0.3349 T12: -0.1136
REMARK 3 T13: -0.1189 T23: 0.0161
REMARK 3 L TENSOR
REMARK 3 L11: 4.7442 L22: 4.4483
REMARK 3 L33: 2.9159 L12: 1.9305
REMARK 3 L13: 0.9674 L23: 0.2493
REMARK 3 S TENSOR
REMARK 3 S11: 0.3294 S12: 0.8231 S13: -0.4348
REMARK 3 S21: -0.2621 S22: -0.3290 S23: -0.1692
REMARK 3 S31: 0.6169 S32: -0.2184 S33: 0.0580
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 524:549)
REMARK 3 ORIGIN FOR THE GROUP (A): -34.0704 27.3885 2.9346
REMARK 3 T TENSOR
REMARK 3 T11: 0.3057 T22: 0.2511
REMARK 3 T33: 0.2640 T12: 0.0607
REMARK 3 T13: -0.1783 T23: 0.0142
REMARK 3 L TENSOR
REMARK 3 L11: 2.8297 L22: 7.0852
REMARK 3 L33: 6.7579 L12: 1.0775
REMARK 3 L13: -1.5615 L23: -1.3172
REMARK 3 S TENSOR
REMARK 3 S11: 0.2694 S12: -0.4431 S13: -0.4162
REMARK 3 S21: 0.8272 S22: -0.0125 S23: 0.0322
REMARK 3 S31: 0.1707 S32: 0.2715 S33: -0.1075
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 4GOW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-AUG-12.
REMARK 100 THE DEPOSITION ID IS D_1000074455.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL12-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.006
REMARK 200 MONOCHROMATOR : LN2-COOLED MONOCHROMATOR
REMARK 200 SI(220), PHI=0 OR 90 DEGREES
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM 3.3.9
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.9
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11737
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 90.131
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 16.70
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 12.70
REMARK 200 R MERGE FOR SHELL (I) : 0.96500
REMARK 200 R SYM FOR SHELL (I) : 0.96500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M AMMONIUM SULFATE, 0.2M SODIUM
REMARK 280 CITRATE (PH 6.0), 0.1M SODIUM TARTRATE, 4% ISOPROPANOL, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 -X,-Y,Z+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 75.81933
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 37.90967
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 56.86450
REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 18.95483
REMARK 290 SMTRY1 6 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 94.77417
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 75.81933
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 37.90967
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 18.95483
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 56.86450
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 94.77417
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: 3280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 9560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, A
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 THR D 79
REMARK 465 ASP D 80
REMARK 465 THR A 522
REMARK 465 VAL A 523
REMARK 465 LYS A 550
REMARK 465 GLU A 551
REMARK 465 THR A 552
REMARK 465 LEU A 553
REMARK 465 ARG A 554
REMARK 465 PRO A 555
REMARK 465 TYR A 556
REMARK 465 ASP A 557
REMARK 465 VAL A 558
REMARK 465 LYS A 559
REMARK 465 ASP A 560
REMARK 465 VAL A 561
REMARK 465 ILE A 562
REMARK 465 GLU A 563
REMARK 465 GLN A 564
REMARK 465 TYR A 565
REMARK 465 SER A 566
REMARK 465 ALA A 567
REMARK 465 GLY A 568
REMARK 465 HIS A 569
REMARK 465 LEU A 570
REMARK 465 ASP A 571
REMARK 465 MET A 572
REMARK 465 LEU A 573
REMARK 465 GLY A 574
REMARK 465 ARG A 575
REMARK 465 ILE A 576
REMARK 465 LYS A 577
REMARK 465 SER A 578
REMARK 465 LEU A 579
REMARK 465 GLN A 580
REMARK 465 THR A 581
REMARK 465 ARG A 582
REMARK 465 VAL A 583
REMARK 465 ASP A 584
REMARK 465 GLN A 585
REMARK 465 ILE A 586
REMARK 465 VAL A 587
REMARK 465 GLY A 588
REMARK 465 ARG A 589
REMARK 465 GLY A 590
REMARK 465 PRO A 591
REMARK 465 GLY A 592
REMARK 465 ASP A 593
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 ASP D 20 74.04 -69.45
REMARK 500 LYS D 75 54.92 -119.63
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 D 204 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 131 OD1
REMARK 620 2 ASP D 131 OD2 40.7
REMARK 620 3 ASP D 133 OD2 91.7 55.6
REMARK 620 4 ASP D 133 OD1 101.6 83.4 40.6
REMARK 620 5 GLU D 140 OE1 97.1 82.2 94.6 131.0
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 D 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 204
DBREF 4GOW D 3 146 UNP P62158 CALM_HUMAN 4 147
DBREF 4GOW A 522 593 UNP P56696 KCNQ4_HUMAN 522 593
SEQRES 1 D 144 GLN LEU THR GLU GLU GLN ILE ALA GLU PHE LYS GLU ALA
SEQRES 2 D 144 PHE SER LEU PHE ASP LYS ASP GLY ASP GLY THR ILE THR
SEQRES 3 D 144 THR LYS GLU LEU GLY THR VAL MET ARG SER LEU GLY GLN
SEQRES 4 D 144 ASN PRO THR GLU ALA GLU LEU GLN ASP MET ILE ASN GLU
SEQRES 5 D 144 VAL ASP ALA ASP GLY ASN GLY THR ILE ASP PHE PRO GLU
SEQRES 6 D 144 PHE LEU THR MET MET ALA ARG LYS MET LYS ASP THR ASP
SEQRES 7 D 144 SER GLU GLU GLU ILE ARG GLU ALA PHE ARG VAL PHE ASP
SEQRES 8 D 144 LYS ASP GLY ASN GLY TYR ILE SER ALA ALA GLU LEU ARG
SEQRES 9 D 144 HIS VAL MET THR ASN LEU GLY GLU LYS LEU THR ASP GLU
SEQRES 10 D 144 GLU VAL ASP GLU MET ILE ARG GLU ALA ASP ILE ASP GLY
SEQRES 11 D 144 ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL GLN MET MET
SEQRES 12 D 144 THR
SEQRES 1 A 72 THR VAL ASP ASP ILE MET PRO ALA VAL LYS THR VAL ILE
SEQRES 2 A 72 ARG SER ILE ARG ILE LEU LYS PHE LEU VAL ALA LYS ARG
SEQRES 3 A 72 LYS PHE LYS GLU THR LEU ARG PRO TYR ASP VAL LYS ASP
SEQRES 4 A 72 VAL ILE GLU GLN TYR SER ALA GLY HIS LEU ASP MET LEU
SEQRES 5 A 72 GLY ARG ILE LYS SER LEU GLN THR ARG VAL ASP GLN ILE
SEQRES 6 A 72 VAL GLY ARG GLY PRO GLY ASP
HET CA D 201 1
HET CA D 202 1
HET CA D 203 1
HET CA D 204 1
HETNAM CA CALCIUM ION
FORMUL 3 CA 4(CA 2+)
FORMUL 7 HOH *18(H2 O)
HELIX 1 1 THR D 5 ASP D 20 1 16
HELIX 2 2 THR D 28 LEU D 39 1 12
HELIX 3 3 THR D 44 ASP D 56 1 13
HELIX 4 4 PHE D 65 LYS D 75 1 11
HELIX 5 5 GLU D 82 ASP D 93 1 12
HELIX 6 6 SER D 101 GLY D 113 1 13
HELIX 7 7 THR D 117 ASP D 129 1 13
HELIX 8 8 ASN D 137 THR D 146 1 10
HELIX 9 9 ASP A 525 PHE A 549 1 25
SHEET 1 A 2 THR D 26 ILE D 27 0
SHEET 2 A 2 ILE D 63 ASP D 64 -1 O ILE D 63 N ILE D 27
LINK OD1 ASN D 60 CA CA D 202 1555 1555 3.18
LINK OD1 ASP D 131 CA CA D 204 1555 1555 3.14
LINK OD2 ASP D 131 CA CA D 204 1555 1555 3.19
LINK OD2 ASP D 133 CA CA D 204 1555 1555 3.13
LINK OD1 ASP D 133 CA CA D 204 1555 1555 3.20
LINK OE1 GLU D 140 CA CA D 204 1555 1555 3.18
SITE 1 AC1 5 ASP D 22 ASP D 24 THR D 26 THR D 28
SITE 2 AC1 5 GLU D 31
SITE 1 AC2 6 ASP D 56 ASP D 58 ASN D 60 THR D 62
SITE 2 AC2 6 ASP D 64 GLU D 67
SITE 1 AC3 4 ASP D 95 ASN D 97 GLU D 104 GLN D 135
SITE 1 AC4 5 ASP D 131 ASP D 133 GLN D 135 ASN D 137
SITE 2 AC4 5 GLU D 140
CRYST1 104.075 104.075 113.729 90.00 90.00 120.00 P 65 2 2 12
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 0.009608 0.005547 0.000000 0.00000
SCALE2 0.000000 0.011095 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008793 0.00000
(ATOM LINES ARE NOT SHOWN.)
END