HEADER METAL TRANSPORT 09-OCT-17 6B8M
TITLE CRYSTAL STRUCTURE OF THE CA2+/CAM:KV7.4 (KCNQ4) AB DOMAIN COMPLEX, 1
TITLE 2 MM CACL2 SOAK
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,D.L.MINOR
REVDAT 4 04-OCT-23 6B8M 1 REMARK
REVDAT 3 27-APR-22 6B8M 1 REMARK
REVDAT 2 21-JUL-21 6B8M 1 LINK
REVDAT 1 14-MAR-18 6B8M 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 CA
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) : 14.94
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 56744
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.229
REMARK 3 R VALUE (WORKING SET) : 0.228
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.520
REMARK 3 FREE R VALUE TEST SET COUNT : 1999
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 14.9425 - 5.4583 1.00 4096 150 0.1835 0.1985
REMARK 3 2 5.4583 - 4.3681 1.00 3979 145 0.1882 0.2140
REMARK 3 3 4.3681 - 3.8265 1.00 3949 143 0.1774 0.2212
REMARK 3 4 3.8265 - 3.4815 1.00 3931 144 0.2022 0.2144
REMARK 3 5 3.4815 - 3.2347 1.00 3930 144 0.2242 0.2947
REMARK 3 6 3.2347 - 3.0456 1.00 3894 142 0.2436 0.2910
REMARK 3 7 3.0456 - 2.8943 1.00 3910 142 0.2535 0.2989
REMARK 3 8 2.8943 - 2.7691 0.99 3864 141 0.2596 0.2914
REMARK 3 9 2.7691 - 2.6631 1.00 3899 142 0.2896 0.3459
REMARK 3 10 2.6631 - 2.5717 1.00 3872 142 0.2987 0.3502
REMARK 3 11 2.5717 - 2.4917 1.00 3884 142 0.3246 0.3551
REMARK 3 12 2.4917 - 2.4207 1.00 3862 142 0.3524 0.4014
REMARK 3 13 2.4207 - 2.3573 1.00 3858 140 0.3712 0.4272
REMARK 3 14 2.3573 - 2.3000 0.99 3817 140 0.3859 0.4051
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) : 0.320
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.310
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 39.97
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 61.40
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 7266
REMARK 3 ANGLE : 0.504 9756
REMARK 3 CHIRALITY : 0.039 1065
REMARK 3 PLANARITY : 0.003 1275
REMARK 3 DIHEDRAL : 24.405 2790
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 6B8M 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_1000230455.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 20-AUG-16
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
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) : 0.9795
REMARK 200 MONOCHROMATOR : SI(111) DOUBLE CRYSTAL KHOZU
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 109615
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 14.942
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 5.512
REMARK 200 R MERGE (I) : 0.19500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.8800
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) : 2.44
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.27
REMARK 200 R MERGE FOR SHELL (I) : 2.23400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.740
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: 6B8L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.81
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULFATE, 0.1M BISTRIS PH
REMARK 280 6.5, 1MM CACL2, 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 54.12150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 71.92650
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 82.13600
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 54.12150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 71.92650
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 82.13600
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 54.12150
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 71.92650
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 82.13600
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 54.12150
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 71.92650
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 82.13600
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: 4080 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12850 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 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: 4250 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 13070 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 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: 4500 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11990 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.0 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: 4560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11880 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 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 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 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 LYS D 148
REMARK 465 GLY E 322
REMARK 465 HIS E 323
REMARK 465 MET E 324
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 HIS G 330
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 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 MET A 324 -127.67 62.36
REMARK 500 VAL A 326 -8.64 -58.82
REMARK 500 LEU A 362 51.35 -92.75
REMARK 500 LYS B 75 -120.13 59.12
REMARK 500 MET C 357 -17.27 -147.21
REMARK 500 LEU C 362 41.70 -93.56
REMARK 500 LYS D 75 -120.05 58.27
REMARK 500 GLU D 114 88.24 -66.75
REMARK 500 LEU E 362 57.47 -91.89
REMARK 500 GLU E 551 3.03 -69.59
REMARK 500 LYS F 75 -115.58 53.26
REMARK 500 THR F 146 57.97 -106.79
REMARK 500 MET G 357 -18.24 -146.24
REMARK 500 LEU G 362 57.44 -101.40
REMARK 500 LYS H 75 -119.73 59.21
REMARK 500 ASN H 137 88.68 -66.70
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 B 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP B 20 OD1
REMARK 620 2 ASP B 22 OD1 68.4
REMARK 620 3 ASP B 22 OD2 112.5 44.6
REMARK 620 4 ASP B 24 OD1 71.7 73.7 82.3
REMARK 620 5 THR B 26 O 72.5 140.3 166.9 88.2
REMARK 620 6 GLU B 31 OE1 93.0 76.5 79.9 149.8 112.4
REMARK 620 7 GLU B 31 OE2 102.9 127.1 120.5 156.0 68.0 51.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP D 20 OD1
REMARK 620 2 ASP D 22 OD1 65.0
REMARK 620 3 ASP D 24 OD1 68.1 75.8
REMARK 620 4 THR D 26 O 66.7 131.1 79.7
REMARK 620 5 GLU D 31 OE1 91.8 122.8 144.8 65.6
REMARK 620 6 GLU D 31 OE2 79.5 71.9 141.5 106.4 52.0
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 20 OD1
REMARK 620 2 ASP F 22 OD1 61.0
REMARK 620 3 ASP F 22 OD2 105.3 44.2
REMARK 620 4 ASP F 24 OD1 63.1 68.1 87.4
REMARK 620 5 THR F 26 O 67.1 127.0 167.0 79.8
REMARK 620 6 GLU F 31 OE1 89.0 117.8 121.6 145.2 69.9
REMARK 620 7 GLU F 31 OE2 89.4 72.7 71.2 139.6 117.9 52.3
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP F 58 OD1
REMARK 620 2 ASN F 60 OD1 83.4
REMARK 620 3 GLU F 67 OE1 87.5 127.8
REMARK 620 4 HOH F 301 O 53.3 90.6 45.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA H 201 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP H 20 OD2
REMARK 620 2 ASP H 22 OD2 62.8
REMARK 620 3 ASP H 24 OD1 68.1 70.4
REMARK 620 4 THR H 26 O 68.2 129.2 80.1
REMARK 620 5 GLU H 31 OE1 81.5 117.5 140.6 65.3
REMARK 620 6 GLU H 31 OE2 76.6 72.2 137.1 108.9 49.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA H 202 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP H 56 OD1
REMARK 620 2 ASN H 60 OD1 64.5
REMARK 620 3 THR H 62 O 69.4 85.2
REMARK 620 4 GLU H 67 OE1 99.6 161.7 80.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA F 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA H 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CA H 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 204
DBREF 6B8M A 325 367 UNP P56696 KCNQ4_HUMAN 325 367
DBREF 6B8M A 524 557 UNP P56696 KCNQ4_HUMAN 524 557
DBREF 6B8M B 0 148 UNP P0DP23 CALM1_HUMAN 1 149
DBREF 6B8M C 325 367 UNP P56696 KCNQ4_HUMAN 325 367
DBREF 6B8M C 524 557 UNP P56696 KCNQ4_HUMAN 524 557
DBREF 6B8M D 0 148 UNP P0DP23 CALM1_HUMAN 1 149
DBREF 6B8M E 325 367 UNP P56696 KCNQ4_HUMAN 325 367
DBREF 6B8M E 524 557 UNP P56696 KCNQ4_HUMAN 524 557
DBREF 6B8M F 0 148 UNP P0DP23 CALM1_HUMAN 1 149
DBREF 6B8M G 325 367 UNP P56696 KCNQ4_HUMAN 325 367
DBREF 6B8M G 524 557 UNP P56696 KCNQ4_HUMAN 524 557
DBREF 6B8M H 0 148 UNP P0DP23 CALM1_HUMAN 1 149
SEQADV 6B8M GLY A 322 UNP P56696 EXPRESSION TAG
SEQADV 6B8M HIS A 323 UNP P56696 EXPRESSION TAG
SEQADV 6B8M MET A 324 UNP P56696 EXPRESSION TAG
SEQADV 6B8M LYS A 368 UNP P56696 LINKER
SEQADV 6B8M LEU A 369 UNP P56696 LINKER
SEQADV 6B8M GLY C 322 UNP P56696 EXPRESSION TAG
SEQADV 6B8M HIS C 323 UNP P56696 EXPRESSION TAG
SEQADV 6B8M MET C 324 UNP P56696 EXPRESSION TAG
SEQADV 6B8M LYS C 368 UNP P56696 LINKER
SEQADV 6B8M LEU C 369 UNP P56696 LINKER
SEQADV 6B8M GLY E 322 UNP P56696 EXPRESSION TAG
SEQADV 6B8M HIS E 323 UNP P56696 EXPRESSION TAG
SEQADV 6B8M MET E 324 UNP P56696 EXPRESSION TAG
SEQADV 6B8M LYS E 368 UNP P56696 LINKER
SEQADV 6B8M LEU E 369 UNP P56696 LINKER
SEQADV 6B8M GLY G 322 UNP P56696 EXPRESSION TAG
SEQADV 6B8M HIS G 323 UNP P56696 EXPRESSION TAG
SEQADV 6B8M MET G 324 UNP P56696 EXPRESSION TAG
SEQADV 6B8M LYS G 368 UNP P56696 LINKER
SEQADV 6B8M 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 CA B 201 1
HET SO4 C 601 5
HET CA D 201 1
HET SO4 D 202 5
HET SO4 E 601 5
HET CA F 201 1
HET CA F 202 1
HET CA H 201 1
HET CA H 202 1
HET SO4 H 203 5
HET SO4 H 204 5
HETNAM CA CALCIUM ION
HETNAM SO4 SULFATE ION
FORMUL 9 CA 6(CA 2+)
FORMUL 10 SO4 5(O4 S 2-)
FORMUL 20 HOH *223(H2 O)
HELIX 1 AA1 MET A 324 THR A 355 1 32
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 THR B 110 1 9
HELIX 12 AB3 THR B 117 ALA B 128 1 12
HELIX 13 AB4 ASN B 137 THR B 146 1 10
HELIX 14 AB5 LYS C 325 HIS C 330 1 6
HELIX 15 AB6 HIS C 330 PHE C 335 1 6
HELIX 16 AB7 ARG C 338 SER C 354 1 17
HELIX 17 AB8 THR C 355 MET C 357 5 3
HELIX 18 AB9 SER C 358 LEU C 362 5 5
HELIX 19 AC1 THR C 363 MET C 527 1 11
HELIX 20 AC2 PRO C 528 GLU C 551 1 24
HELIX 21 AC3 GLU D 7 ASP D 20 1 14
HELIX 22 AC4 THR D 28 LEU D 39 1 12
HELIX 23 AC5 THR D 44 ASP D 56 1 13
HELIX 24 AC6 PHE D 65 LYS D 75 1 11
HELIX 25 AC7 ASP D 78 VAL D 91 1 14
HELIX 26 AC8 ALA D 102 LEU D 112 1 11
HELIX 27 AC9 THR D 117 ASP D 129 1 13
HELIX 28 AD1 ASN D 137 THR D 146 1 10
HELIX 29 AD2 VAL E 326 HIS E 334 1 9
HELIX 30 AD3 HIS E 334 SER E 354 1 21
HELIX 31 AD4 SER E 358 LEU E 362 5 5
HELIX 32 AD5 THR E 363 MET E 527 1 11
HELIX 33 AD6 PRO E 528 GLU E 551 1 24
HELIX 34 AD7 THR F 5 ASP F 20 1 16
HELIX 35 AD8 THR F 28 LEU F 39 1 12
HELIX 36 AD9 THR F 44 GLU F 54 1 11
HELIX 37 AE1 PHE F 65 LYS F 75 1 11
HELIX 38 AE2 ASP F 78 ARG F 90 1 13
HELIX 39 AE3 VAL F 91 ASP F 93 5 3
HELIX 40 AE4 ALA F 102 LEU F 112 1 11
HELIX 41 AE5 THR F 117 ALA F 128 1 12
HELIX 42 AE6 ASN F 137 THR F 146 1 10
HELIX 43 AE7 GLN G 332 THR G 355 1 24
HELIX 44 AE8 ASP G 356 MET G 357 5 2
HELIX 45 AE9 SER G 358 LEU G 362 5 5
HELIX 46 AF1 THR G 363 MET G 527 1 11
HELIX 47 AF2 PRO G 528 GLU G 551 1 24
HELIX 48 AF3 THR H 5 ASP H 20 1 16
HELIX 49 AF4 THR H 28 LEU H 39 1 12
HELIX 50 AF5 THR H 44 GLU H 54 1 11
HELIX 51 AF6 ASP H 64 LYS H 75 1 12
HELIX 52 AF7 ASP H 78 PHE H 92 1 15
HELIX 53 AF8 ALA H 102 LEU H 112 1 11
HELIX 54 AF9 THR H 117 ALA H 128 1 12
HELIX 55 AG1 ASN H 137 THR H 146 1 10
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 3 ILE B 100 SER B 101 0
SHEET 2 AA2 3 GLN B 135 VAL B 136 -1 O VAL B 136 N ILE B 100
SHEET 3 AA2 3 ILE B 130 ASP B 131 -1 O ASP B 131 N GLN B 135
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 ILE D 100 SER D 101 0
SHEET 2 AA4 2 GLN D 135 VAL D 136 -1 O VAL D 136 N ILE D 100
SHEET 1 AA5 2 THR F 26 ILE F 27 0
SHEET 2 AA5 2 ILE F 63 ASP F 64 -1 O ILE F 63 N ILE F 27
SHEET 1 AA6 2 ILE F 100 SER F 101 0
SHEET 2 AA6 2 GLN F 135 VAL F 136 -1 O VAL F 136 N ILE F 100
SHEET 1 AA7 2 ILE H 100 SER H 101 0
SHEET 2 AA7 2 GLN H 135 VAL H 136 -1 O VAL H 136 N ILE H 100
LINK OD1 ASP B 20 CA CA B 201 1555 1555 2.48
LINK OD1 ASP B 22 CA CA B 201 1555 1555 2.40
LINK OD2 ASP B 22 CA CA B 201 1555 1555 3.11
LINK OD1 ASP B 24 CA CA B 201 1555 1555 2.44
LINK O THR B 26 CA CA B 201 1555 1555 2.53
LINK OE1 GLU B 31 CA CA B 201 1555 1555 2.65
LINK OE2 GLU B 31 CA CA B 201 1555 1555 2.40
LINK OD1 ASP D 20 CA CA D 201 1555 1555 2.58
LINK OD1 ASP D 22 CA CA D 201 1555 1555 2.60
LINK OD1 ASP D 24 CA CA D 201 1555 1555 2.37
LINK O THR D 26 CA CA D 201 1555 1555 2.57
LINK OE1 GLU D 31 CA CA D 201 1555 1555 2.57
LINK OE2 GLU D 31 CA CA D 201 1555 1555 2.44
LINK OD1 ASP F 20 CA CA F 201 1555 1555 2.91
LINK OD1 ASP F 22 CA CA F 201 1555 1555 2.56
LINK OD2 ASP F 22 CA CA F 201 1555 1555 3.11
LINK OD1 ASP F 24 CA CA F 201 1555 1555 2.41
LINK O THR F 26 CA CA F 201 1555 1555 2.58
LINK OE1 GLU F 31 CA CA F 201 1555 1555 2.42
LINK OE2 GLU F 31 CA CA F 201 1555 1555 2.56
LINK OD1 ASP F 58 CA CA F 202 1555 1555 2.48
LINK OD1 ASN F 60 CA CA F 202 1555 1555 3.10
LINK OE1 GLU F 67 CA CA F 202 1555 1555 2.89
LINK CA CA F 202 O HOH F 301 1555 1555 2.83
LINK OD2 ASP H 20 CA CA H 201 1555 1555 2.46
LINK OD2 ASP H 22 CA CA H 201 1555 1555 2.76
LINK OD1 ASP H 24 CA CA H 201 1555 1555 2.38
LINK O THR H 26 CA CA H 201 1555 1555 2.63
LINK OE1 GLU H 31 CA CA H 201 1555 1555 2.57
LINK OE2 GLU H 31 CA CA H 201 1555 1555 2.68
LINK OD1 ASP H 56 CA CA H 202 1555 1555 2.66
LINK OD1 ASN H 60 CA CA H 202 1555 1555 2.74
LINK O THR H 62 CA CA H 202 1555 1555 3.08
LINK OE1 GLU H 67 CA CA H 202 1555 1555 2.85
SITE 1 AC1 5 ASP B 20 ASP B 22 ASP B 24 THR B 26
SITE 2 AC1 5 GLU B 31
SITE 1 AC2 5 THR C 363 ALA C 364 HOH C 711 HOH C 717
SITE 2 AC2 5 TYR G 367
SITE 1 AC3 5 ASP D 20 ASP D 22 ASP D 24 THR D 26
SITE 2 AC3 5 GLU D 31
SITE 1 AC4 4 ASN D 42 HOH D 324 GLN F 41 ASN F 42
SITE 1 AC5 6 TYR A 367 LYS D 21 LEU E 362 THR E 363
SITE 2 AC5 6 ALA E 364 HOH E 713
SITE 1 AC6 5 ASP F 20 ASP F 22 ASP F 24 THR F 26
SITE 2 AC6 5 GLU F 31
SITE 1 AC7 6 ASP F 58 ASN F 60 THR F 62 ASP F 64
SITE 2 AC7 6 GLU F 67 HOH F 301
SITE 1 AC8 5 ASP H 20 ASP H 22 ASP H 24 THR H 26
SITE 2 AC8 5 GLU H 31
SITE 1 AC9 5 ASP H 56 ASP H 58 ASN H 60 THR H 62
SITE 2 AC9 5 GLU H 67
SITE 1 AD1 5 GLN B 41 ASN B 42 GLY H 40 GLN H 41
SITE 2 AD1 5 ASN H 42
SITE 1 AD2 5 ARG C 359 ARG D 126 ARG G 359 ARG H 126
SITE 2 AD2 5 HOH H 301
CRYST1 108.243 143.853 164.272 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 0.009238 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006952 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006087 0.00000
(ATOM LINES ARE NOT SHOWN.)
END