HEADER MEMBRANE PROTEIN 19-AUG-08 3E8B
TITLE CRYSTAL STRUCTURE OF THE THE OPEN NAK CHANNEL- RB+ COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: POTASSIUM CHANNEL PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: TRANSMEMBRANE DOMAIN, RESIDUES 19-110;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS CEREUS;
SOURCE 3 ORGANISM_TAXID: 1396;
SOURCE 4 ATCC: 14579;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: SG13009;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PQE60
KEYWDS NON-SELECTIVE CATION CHANNEL, MEMBRANE PROTEIN, TETRAMERIC CATION
KEYWDS 2 CHANNEL FAMILY, 2-TRANSMEMBRANE HELIX CHANNELS, IONIC CHANNEL
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.JIANG,A.ALAM
REVDAT 5 21-FEB-24 3E8B 1 REMARK SEQADV
REVDAT 4 25-OCT-17 3E8B 1 REMARK
REVDAT 3 16-NOV-11 3E8B 1 VERSN HETATM
REVDAT 2 20-JAN-09 3E8B 1 JRNL
REVDAT 1 23-DEC-08 3E8B 0
JRNL AUTH A.ALAM,Y.JIANG
JRNL TITL STRUCTURAL ANALYSIS OF ION SELECTIVITY IN THE NAK CHANNEL
JRNL REF NAT.STRUCT.MOL.BIOL. V. 16 35 2009
JRNL REFN ISSN 1545-9993
JRNL PMID 19098915
JRNL DOI 10.1038/NSMB.1537
REMARK 2
REMARK 2 RESOLUTION. 1.70 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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.09
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) (%) : 95.9
REMARK 3 NUMBER OF REFLECTIONS : 21522
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.229
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1083
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 : 1461
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 43
REMARK 3 SOLVENT ATOMS : 94
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.73
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.38400
REMARK 3 B22 (A**2) : 0.38400
REMARK 3 B33 (A**2) : -0.76700
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 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) : 1.476 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.174 ; 3.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.954 ; 4.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 4.018 ; 5.000
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : 132.5
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 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : MPD.PAR
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 5 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3E8B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-OCT-08.
REMARK 100 THE DEPOSITION ID IS D_1000049001.
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 : 7.5
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) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : NULL
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21705
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.700
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 (%) : NULL
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) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.21
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES BUFFER, 55-70% (4S)-2
REMARK 280 -METHYL-2,4-PENTANEDIOL (MPD), PH 7.5, VAPOR DIFFUSION, SITTING
REMARK 280 DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4
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 -Y,X,Z
REMARK 290 4555 Y,-X,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 -Y+1/2,X+1/2,Z+1/2
REMARK 290 8555 Y+1/2,-X+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 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 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 34.06700
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.06700
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 44.67950
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 34.06700
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.06700
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 44.67950
REMARK 290 SMTRY1 7 0.000000 -1.000000 0.000000 34.06700
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 34.06700
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 44.67950
REMARK 290 SMTRY1 8 0.000000 1.000000 0.000000 34.06700
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 34.06700
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 44.67950
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6880 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 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 -1.000000 0.000000 0.000000 -68.13400
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -68.13400
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 -68.13400
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 -68.13400
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7160 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 BIOMT1 2 -1.000000 0.000000 0.000000 -68.13400
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 -68.13400
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 -68.13400
REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 -68.13400
REMARK 350 BIOMT3 4 0.000000 0.000000 1.000000 0.00000
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 RB RB A 2 LIES ON A SPECIAL POSITION.
REMARK 375 RB RB A 3 LIES ON A SPECIAL POSITION.
REMARK 375 RB RB A 4 LIES ON A SPECIAL POSITION.
REMARK 375 RB RB A 6 LIES ON A SPECIAL POSITION.
REMARK 375 RB RB A 9 LIES ON A SPECIAL POSITION.
REMARK 375 RB RB A 10 LIES ON A SPECIAL POSITION.
REMARK 375 RB RB B 1 LIES ON A SPECIAL POSITION.
REMARK 375 RB RB B 5 LIES ON A SPECIAL POSITION.
REMARK 375 RB RB B 7 LIES ON A SPECIAL POSITION.
REMARK 375 RB RB B 8 LIES ON A SPECIAL POSITION.
REMARK 375 RB RB B 11 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 TRP A 19
REMARK 465 LYS A 20
REMARK 465 ASP A 21
REMARK 465 LYS A 22
REMARK 465 ARG A 114
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 TRP B 19 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 19 CZ3 CH2
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 HOH B 539 O HOH B 547 2.05
REMARK 500 OH TYR A 55 O HOH A 543 2.06
REMARK 500 O HOH B 509 O HOH B 529 2.07
REMARK 500 NH1 ARG B 114 O HOH B 541 2.10
REMARK 500 O HOH B 510 O HOH B 546 2.13
REMARK 500 O HOH B 523 O HOH B 545 2.15
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 ASP B 66 C GLY B 67 N -0.184
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 ASN B 68 -38.30 -142.51
REMARK 500 VAL B 102 -54.07 -124.63
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 MPD A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RB A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RB A 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RB A 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RB A 6
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RB A 10
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MPD B 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RB B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RB B 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RB B 7
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RB B 8
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3E83 RELATED DB: PDB
REMARK 900 RELATED ID: 3E86 RELATED DB: PDB
REMARK 900 RELATED ID: 3E89 RELATED DB: PDB
REMARK 900 RELATED ID: 3E8F RELATED DB: PDB
REMARK 900 RELATED ID: 3E8G RELATED DB: PDB
REMARK 900 RELATED ID: 3E8H RELATED DB: PDB
DBREF 3E8B A 19 110 UNP Q81HW2 Q81HW2_BACCR 19 110
DBREF 3E8B B 19 110 UNP Q81HW2 Q81HW2_BACCR 19 110
SEQADV 3E8B LEU A 111 UNP Q81HW2 EXPRESSION TAG
SEQADV 3E8B VAL A 112 UNP Q81HW2 EXPRESSION TAG
SEQADV 3E8B PRO A 113 UNP Q81HW2 EXPRESSION TAG
SEQADV 3E8B ARG A 114 UNP Q81HW2 EXPRESSION TAG
SEQADV 3E8B LEU B 111 UNP Q81HW2 EXPRESSION TAG
SEQADV 3E8B VAL B 112 UNP Q81HW2 EXPRESSION TAG
SEQADV 3E8B PRO B 113 UNP Q81HW2 EXPRESSION TAG
SEQADV 3E8B ARG B 114 UNP Q81HW2 EXPRESSION TAG
SEQRES 1 A 96 TRP LYS ASP LYS GLU PHE GLN VAL LEU PHE VAL LEU THR
SEQRES 2 A 96 ILE LEU THR LEU ILE SER GLY THR ILE PHE TYR SER THR
SEQRES 3 A 96 VAL GLU GLY LEU ARG PRO ILE ASP ALA LEU TYR PHE SER
SEQRES 4 A 96 VAL VAL THR LEU THR THR VAL GLY ASP GLY ASN PHE SER
SEQRES 5 A 96 PRO GLN THR ASP PHE GLY LYS ILE PHE THR ILE LEU TYR
SEQRES 6 A 96 ILE PHE ILE GLY ILE GLY LEU VAL PHE GLY PHE ILE HIS
SEQRES 7 A 96 LYS LEU ALA VAL ASN VAL GLN LEU PRO SER ILE LEU SER
SEQRES 8 A 96 ASN LEU VAL PRO ARG
SEQRES 1 B 96 TRP LYS ASP LYS GLU PHE GLN VAL LEU PHE VAL LEU THR
SEQRES 2 B 96 ILE LEU THR LEU ILE SER GLY THR ILE PHE TYR SER THR
SEQRES 3 B 96 VAL GLU GLY LEU ARG PRO ILE ASP ALA LEU TYR PHE SER
SEQRES 4 B 96 VAL VAL THR LEU THR THR VAL GLY ASP GLY ASN PHE SER
SEQRES 5 B 96 PRO GLN THR ASP PHE GLY LYS ILE PHE THR ILE LEU TYR
SEQRES 6 B 96 ILE PHE ILE GLY ILE GLY LEU VAL PHE GLY PHE ILE HIS
SEQRES 7 B 96 LYS LEU ALA VAL ASN VAL GLN LEU PRO SER ILE LEU SER
SEQRES 8 B 96 ASN LEU VAL PRO ARG
HET MPD A 501 8
HET MPD A 504 8
HET RB A 2 1
HET RB A 3 1
HET RB A 4 1
HET RB A 6 1
HET RB A 9 1
HET RB A 10 1
HET MPD B 502 8
HET MPD B 503 8
HET RB B 1 1
HET RB B 5 1
HET RB B 7 1
HET RB B 8 1
HET RB B 11 1
HETNAM MPD (4S)-2-METHYL-2,4-PENTANEDIOL
HETNAM RB RUBIDIUM ION
FORMUL 3 MPD 4(C6 H14 O2)
FORMUL 5 RB 11(RB 1+)
FORMUL 18 HOH *94(H2 O)
HELIX 1 1 GLU A 23 GLU A 46 1 24
HELIX 2 2 ARG A 49 THR A 62 1 14
HELIX 3 3 THR A 73 ASN A 101 1 29
HELIX 4 4 GLN A 103 SER A 109 1 7
HELIX 5 5 TRP B 19 GLU B 46 1 28
HELIX 6 6 ARG B 49 THR B 62 1 14
HELIX 7 7 THR B 73 VAL B 102 1 30
HELIX 8 8 VAL B 102 VAL B 112 1 11
SITE 1 AC1 4 ASP A 52 TYR A 55 ASP A 66 HOH A 533
SITE 1 AC2 4 SER A 37 TYR A 83 ILE B 36 MPD B 503
SITE 1 AC3 3 RB A 3 THR A 63 VAL A 64
SITE 1 AC4 4 RB A 2 RB A 10 VAL A 64 HOH A 506
SITE 1 AC5 2 GLY A 67 HOH A 505
SITE 1 AC6 1 THR A 63
SITE 1 AC7 2 RB A 3 HOH A 506
SITE 1 AC8 2 SER B 37 PHE B 79
SITE 1 AC9 6 TYR A 83 ILE A 86 MPD A 504 LEU B 33
SITE 2 AC9 6 ILE B 36 SER B 37
SITE 1 BC1 3 RB B 7 THR B 63 VAL B 64
SITE 1 BC2 1 THR B 63
SITE 1 BC3 3 RB B 1 VAL B 64 HOH B 513
SITE 1 BC4 1 GLY B 67
CRYST1 68.134 68.134 89.359 90.00 90.00 90.00 I 4 16
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 0.014677 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014677 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011191 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
