HEADER METAL TRANSPORT, MEMBRANE PROTEIN 22-JUL-05 2AEM
TITLE CRYSTAL STRUCTURES OF THE MTHK RCK DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CALCIUM-GATED POTASSIUM CHANNEL MTHK;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOTHERMOBACTER THERMAUTOTROPHICUS;
SOURCE 3 ORGANISM_TAXID: 145262;
SOURCE 4 GENE: MTHK;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: M15;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PQE70
KEYWDS ROSSMANN FOLD, HELIX-TURN-HELIX, METAL TRANSPORT, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR J.DONG,N.SHI,I.BERKE,L.CHEN,Y.JIANG
REVDAT 5 23-AUG-23 2AEM 1 SEQADV
REVDAT 4 13-JUL-11 2AEM 1 VERSN
REVDAT 3 24-FEB-09 2AEM 1 VERSN
REVDAT 2 03-JAN-06 2AEM 1 JRNL
REVDAT 1 25-OCT-05 2AEM 0
JRNL AUTH J.DONG,N.SHI,I.BERKE,L.CHEN,Y.JIANG
JRNL TITL STRUCTURES OF THE MTHK RCK DOMAIN AND THE EFFECT OF CA2+ ON
JRNL TITL 2 GATING RING STABILITY
JRNL REF J.BIOL.CHEM. V. 280 41716 2005
JRNL REFN ISSN 0021-9258
JRNL PMID 16227203
JRNL DOI 10.1074/JBC.M508144200
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH Y.JIANG,A.LEE,J.CHEN,M.CADENE,B.T.CHAIT,R.MACKINNON
REMARK 1 TITL CRYSTAL STRUCTURE AND MECHANISM OF A CALCIUM-GATED POTASSIUM
REMARK 1 TITL 2 CHANNEL
REMARK 1 REF NATURE V. 417 515 2002
REMARK 1 REFN ISSN 0028-0836
REMARK 1 PMID 12037559
REMARK 1 DOI 10.1038/417515A
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.80
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 10711
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 542
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1737
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 5
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 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : NULL
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2AEM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-AUG-05.
REMARK 100 THE DEPOSITION ID IS D_1000033801.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 05-JUN-04
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9790
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10728
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 35.800
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.770
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.100
REMARK 200 R MERGE (I) : 0.06800
REMARK 200 R SYM (I) : 0.06800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 23.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.52400
REMARK 200 R SYM FOR SHELL (I) : 0.52400
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: CNS
REMARK 200 STARTING MODEL: PDB ENTRY 1LNQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, AMMONIUM SULFATE, CACODYLATE
REMARK 280 , PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z
REMARK 290 6555 -X,-X+Y,-Z
REMARK 290 7555 X+2/3,Y+1/3,Z+1/3
REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3
REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3
REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3
REMARK 290 13555 X+1/3,Y+2/3,Z+2/3
REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3
REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3
REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3
REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3
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 0.00000
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 0.00000
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 82.44000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 47.59676
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 27.61733
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 82.44000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 47.59676
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 27.61733
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 82.44000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 47.59676
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 27.61733
REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 82.44000
REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 47.59676
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 27.61733
REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 82.44000
REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 47.59676
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 27.61733
REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 82.44000
REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 47.59676
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 27.61733
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 95.19351
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 55.23467
REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 95.19351
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 55.23467
REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 95.19351
REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 55.23467
REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 95.19351
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 55.23467
REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 95.19351
REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 55.23467
REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 95.19351
REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 55.23467
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,PQS
REMARK 350 TOTAL BURIED SURFACE AREA: 7180 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19130 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 BIOMT1 2 -0.500000 0.866025 0.000000 82.44000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 -47.59676
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 138.08667
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 4 LIES ON A SPECIAL POSITION.
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 107
REMARK 465 GLY A 108
REMARK 465 LEU A 109
REMARK 465 ILE A 110
REMARK 465 ASP A 111
REMARK 465 VAL A 112
REMARK 465 PRO A 339
REMARK 465 ARG A 340
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 ARG A 176 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 186 CG CD OE1 OE2
REMARK 470 ARG A 308 CG CD NE CZ NH1 NH2
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 SER A 115 50.12 -142.79
REMARK 500 ARG A 116 -153.20 -88.74
REMARK 500 ARG A 135 98.58 -58.58
REMARK 500 ARG A 154 24.38 -70.71
REMARK 500 SER A 155 12.49 -144.54
REMARK 500 ASP A 184 84.08 -152.11
REMARK 500 GLU A 186 11.36 -68.59
REMARK 500 ALA A 257 -75.24 -108.47
REMARK 500 GLU A 259 42.08 34.31
REMARK 500 SER A 260 -99.59 -59.06
REMARK 500 ASP A 300 38.24 32.88
REMARK 500 ILE A 304 -73.54 -53.89
REMARK 500 ASP A 305 74.68 -112.81
REMARK 500 SER A 335 153.95 -37.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1LNQ RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH TRANSMEMBRANE DOMAIN
REMARK 900 RELATED ID: 2AEF RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITH CA2+ BOUND FORM
REMARK 900 RELATED ID: 2AEJ RELATED DB: PDB
REMARK 900 THE SAME PROTEIN WITHOUT CA2+ BOUND FORM
DBREF 2AEM A 107 336 UNP O27564 MTHK_METTH 107 336
SEQADV 2AEM LEU A 337 UNP O27564 CLONING ARTIFACT
SEQADV 2AEM VAL A 338 UNP O27564 CLONING ARTIFACT
SEQADV 2AEM PRO A 339 UNP O27564 CLONING ARTIFACT
SEQADV 2AEM ARG A 340 UNP O27564 CLONING ARTIFACT
SEQRES 1 A 234 MET GLY LEU ILE ASP VAL ALA LYS SER ARG HIS VAL VAL
SEQRES 2 A 234 ILE CYS GLY TRP SER GLU SER THR LEU GLU CYS LEU ARG
SEQRES 3 A 234 GLU LEU ARG GLY SER GLU VAL PHE VAL LEU ALA GLU ASP
SEQRES 4 A 234 GLU ASN VAL ARG LYS LYS VAL LEU ARG SER GLY ALA ASN
SEQRES 5 A 234 PHE VAL HIS GLY ASP PRO THR ARG VAL SER ASP LEU GLU
SEQRES 6 A 234 LYS ALA ASN VAL ARG GLY ALA ARG ALA VAL ILE VAL ASP
SEQRES 7 A 234 LEU GLU SER ASP SER GLU THR ILE HIS CYS ILE LEU GLY
SEQRES 8 A 234 ILE ARG LYS ILE ASP GLU SER VAL ARG ILE ILE ALA GLU
SEQRES 9 A 234 ALA GLU ARG TYR GLU ASN ILE GLU GLN LEU ARG MET ALA
SEQRES 10 A 234 GLY ALA ASP GLN VAL ILE SER PRO PHE VAL ILE SER GLY
SEQRES 11 A 234 ARG LEU MET SER ARG SER ILE ASP ASP GLY TYR GLU ALA
SEQRES 12 A 234 MET PHE VAL GLN ASP VAL LEU ALA GLU GLU SER THR ARG
SEQRES 13 A 234 ARG MET VAL GLU VAL PRO ILE PRO GLU GLY SER LYS LEU
SEQRES 14 A 234 GLU GLY VAL SER VAL LEU ASP ALA ASP ILE HIS ASP VAL
SEQRES 15 A 234 THR GLY VAL ILE ILE ILE GLY VAL GLY ARG GLY ASP GLU
SEQRES 16 A 234 LEU ILE ILE ASP PRO PRO ARG ASP TYR SER PHE ARG ALA
SEQRES 17 A 234 GLY ASP ILE ILE LEU GLY ILE GLY LYS PRO GLU GLU ILE
SEQRES 18 A 234 GLU ARG LEU LYS ASN TYR ILE SER ALA LEU VAL PRO ARG
FORMUL 2 HOH *5(H2 O)
HELIX 1 1 SER A 124 LEU A 134 1 11
HELIX 2 2 ASP A 145 ASN A 147 5 3
HELIX 3 3 VAL A 148 ARG A 154 1 7
HELIX 4 4 ARG A 166 ALA A 173 1 8
HELIX 5 5 SER A 187 ASP A 202 1 16
HELIX 6 6 ARG A 213 GLU A 215 5 3
HELIX 7 7 ASN A 216 GLY A 224 1 9
HELIX 8 8 SER A 230 ARG A 241 1 12
HELIX 9 9 GLY A 246 ALA A 257 1 12
HELIX 10 10 SER A 279 ASP A 284 1 6
HELIX 11 11 ASP A 284 GLY A 290 1 7
HELIX 12 12 LYS A 323 SER A 335 1 13
SHEET 1 A 6 ASN A 158 HIS A 161 0
SHEET 2 A 6 VAL A 139 ALA A 143 1 N VAL A 141 O ASN A 158
SHEET 3 A 6 VAL A 118 CYS A 121 1 N ILE A 120 O PHE A 140
SHEET 4 A 6 ALA A 180 VAL A 183 1 O ILE A 182 N CYS A 121
SHEET 5 A 6 ILE A 207 GLU A 210 1 O ILE A 208 N VAL A 183
SHEET 6 A 6 GLN A 227 ILE A 229 1 O GLN A 227 N ALA A 209
SHEET 1 B 4 ARG A 263 PRO A 268 0
SHEET 2 B 4 ILE A 317 GLY A 322 -1 O GLY A 320 N VAL A 265
SHEET 3 B 4 ILE A 292 ARG A 298 -1 N GLY A 295 O LEU A 319
SHEET 4 B 4 GLU A 301 ILE A 303 -1 O ILE A 303 N VAL A 296
CRYST1 164.880 164.880 82.852 90.00 90.00 120.00 H 3 2 18
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 0.006065 0.003502 0.000000 0.00000
SCALE2 0.000000 0.007003 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012070 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
