HEADER TRANSPORT PROTEIN 11-JUL-06 2HMW
TITLE SQUARE-SHAPED OCTAMERIC RING STRUCTURE OF AN RCK DOMAIN WITH ATP BOUND
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: YUAA PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RCK CORE DOMAIN (KTN), RESIDUES 1-144;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_TAXID: 1423;
SOURCE 4 GENE: YUAA;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET15B
KEYWDS RCK, KTN, KTR, KTRA, KTRAB, MEMBRANE PROTEIN, ION TRANSPORTER,
KEYWDS 2 SYMPORTER, TRANSPORT PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR R.A.ALBRIGHT,J.H.MORAIS-CABRAL
REVDAT 6 30-AUG-23 2HMW 1 REMARK
REVDAT 5 20-OCT-21 2HMW 1 REMARK SEQADV
REVDAT 4 18-OCT-17 2HMW 1 REMARK
REVDAT 3 24-FEB-09 2HMW 1 VERSN
REVDAT 2 03-OCT-06 2HMW 1 JRNL
REVDAT 1 26-SEP-06 2HMW 0
JRNL AUTH R.A.ALBRIGHT,J.L.IBAR,C.U.KIM,S.M.GRUNER,J.H.MORAIS-CABRAL
JRNL TITL THE RCK DOMAIN OF THE KTRAB K(+) TRANSPORTER: MULTIPLE
JRNL TITL 2 CONFORMATIONS OF AN OCTAMERIC RING.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 126 1147 2006
JRNL REFN ISSN 0092-8674
JRNL PMID 16990138
JRNL DOI 10.1016/J.CELL.2006.08.028
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH T.P.ROOSILD,S.MILLER,I.R.BOOTH,S.CHOE
REMARK 1 TITL A MECHANISM OF REGULATING TRANSMEMBRANE POTASSIUM FLUX
REMARK 1 TITL 2 THROUGH A LIGAND-MEDIATED CONFORMATIONAL SWITCH
REMARK 1 REF CELL(CAMBRIDGE,MASS.) V. 109 781 2002
REMARK 1 REFN ISSN 0092-8674
REMARK 1 REFERENCE 2
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. 417 501 2002
REMARK 1 REFN ISSN 0028-0836
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
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) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
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) (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 8044
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.264
REMARK 3 FREE R VALUE : 0.303
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.300
REMARK 3 FREE R VALUE TEST SET COUNT : 856
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 : 17
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.06
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 355
REMARK 3 BIN R VALUE (WORKING SET) : 0.3590
REMARK 3 BIN FREE R VALUE : 0.5320
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 43
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 : 2128
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 62
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 84.15
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) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.312
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 : 50.85
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_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ATP_ADJUSTED.PARAM
REMARK 3 PARAMETER FILE 4 : 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
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2HMW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-06.
REMARK 100 THE DEPOSITION ID IS D_1000038528.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-SEP-05
REMARK 200 TEMPERATURE (KELVIN) : NULL
REMARK 200 PH : 8.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X25
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.100
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK, HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 8231
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 9.900
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 10.20
REMARK 200 R MERGE FOR SHELL (I) : 0.73100
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: SINGLE DOMAIN FROM PDB ENTRY 1LSU
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 500MM MGCL2, 50MM TRIS PH 8.8, 8.5%
REMARK 280 (W/V) PEG 2000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 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 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 16555 -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 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 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 63.14000
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 63.14000
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 49.30600
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 63.14000
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 63.14000
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 49.30600
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 63.14000
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 63.14000
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 49.30600
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 63.14000
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 63.14000
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 49.30600
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 63.14000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 63.14000
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 49.30600
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 63.14000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 63.14000
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 49.30600
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 63.14000
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 63.14000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 49.30600
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 63.14000
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 63.14000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 49.30600
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS AN OCTAMERIC RING GENERATED FROM
REMARK 300 THE ASYMMETRIC UNIT DIMER USING THESE SYMMETRY OPERATORS: X, Y, Z
REMARK 300 AND Y, 1-X, Z AND 1-X, 1-Y, Z AND 1-Y, X, Z
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: OCTAMERIC
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 BIOMT1 2 -1.000000 0.000000 0.000000 126.28000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 126.28000
REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000
REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 126.28000
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 126.28000
REMARK 350 BIOMT3 4 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 GLY A 2
REMARK 465 ARG A 3
REMARK 465 ILE A 4
REMARK 465 LYS A 5
REMARK 465 VAL A 141
REMARK 465 LEU A 142
REMARK 465 ASN A 143
REMARK 465 TYR A 144
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 ARG B 3
REMARK 465 ILE B 4
REMARK 465 LYS B 5
REMARK 465 ASN B 6
REMARK 465 LYS B 7
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 ASN A 6 CG OD1 ND2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OG SER B 65 OG SER B 65 5656 1.73
REMARK 500 CB SER B 47 CB SER B 47 7556 1.95
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 LEU A 14 73.22 -100.91
REMARK 500 ASP A 36 124.33 -178.81
REMARK 500 ILE A 68 -19.85 -48.29
REMARK 500 ALA A 80 51.19 -69.53
REMARK 500 ASN A 81 64.93 -160.41
REMARK 500 LEU A 95 5.64 -69.10
REMARK 500 PRO A 98 -65.75 -29.11
REMARK 500 LEU B 14 74.50 -103.84
REMARK 500 ASP B 36 123.48 178.39
REMARK 500 ILE B 68 -18.05 -49.78
REMARK 500 ALA B 80 54.52 -68.69
REMARK 500 ASN B 81 71.18 -155.99
REMARK 500 GLN B 83 -71.53 -66.57
REMARK 500 LEU B 95 4.01 -63.41
REMARK 500 HIS B 123 77.96 -115.13
REMARK 500 ASN B 143 85.94 62.57
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 ATP A 601
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 602
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1LSU RELATED DB: PDB
REMARK 900 RELATED ID: 1LSS RELATED DB: PDB
REMARK 900 RELATED ID: 1LNQ RELATED DB: PDB
REMARK 900 RELATED ID: 2HMT RELATED DB: PDB
REMARK 900 RELATED ID: 2HMU RELATED DB: PDB
REMARK 900 RELATED ID: 2HMV RELATED DB: PDB
REMARK 900 RELATED ID: 2HMS RELATED DB: PDB
DBREF 2HMW A 1 144 UNP O32080 O32080_BACSU 1 144
DBREF 2HMW B 1 144 UNP O32080 O32080_BACSU 1 144
SEQADV 2HMW VAL A 22 UNP O32080 CYS 22 ENGINEERED MUTATION
SEQADV 2HMW VAL B 22 UNP O32080 CYS 22 ENGINEERED MUTATION
SEQRES 1 A 144 MET GLY ARG ILE LYS ASN LYS GLN PHE ALA VAL ILE GLY
SEQRES 2 A 144 LEU GLY ARG PHE GLY GLY SER ILE VAL LYS GLU LEU HIS
SEQRES 3 A 144 ARG MET GLY HIS GLU VAL LEU ALA VAL ASP ILE ASN GLU
SEQRES 4 A 144 GLU LYS VAL ASN ALA TYR ALA SER TYR ALA THR HIS ALA
SEQRES 5 A 144 VAL ILE ALA ASN ALA THR GLU GLU ASN GLU LEU LEU SER
SEQRES 6 A 144 LEU GLY ILE ARG ASN PHE GLU TYR VAL ILE VAL ALA ILE
SEQRES 7 A 144 GLY ALA ASN ILE GLN ALA SER THR LEU THR THR LEU LEU
SEQRES 8 A 144 LEU LYS GLU LEU ASP ILE PRO ASN ILE TRP VAL LYS ALA
SEQRES 9 A 144 GLN ASN TYR TYR HIS HIS LYS VAL LEU GLU LYS ILE GLY
SEQRES 10 A 144 ALA ASP ARG ILE ILE HIS PRO GLU LYS ASP MET GLY VAL
SEQRES 11 A 144 LYS ILE ALA GLN SER LEU SER ASP GLU ASN VAL LEU ASN
SEQRES 12 A 144 TYR
SEQRES 1 B 144 MET GLY ARG ILE LYS ASN LYS GLN PHE ALA VAL ILE GLY
SEQRES 2 B 144 LEU GLY ARG PHE GLY GLY SER ILE VAL LYS GLU LEU HIS
SEQRES 3 B 144 ARG MET GLY HIS GLU VAL LEU ALA VAL ASP ILE ASN GLU
SEQRES 4 B 144 GLU LYS VAL ASN ALA TYR ALA SER TYR ALA THR HIS ALA
SEQRES 5 B 144 VAL ILE ALA ASN ALA THR GLU GLU ASN GLU LEU LEU SER
SEQRES 6 B 144 LEU GLY ILE ARG ASN PHE GLU TYR VAL ILE VAL ALA ILE
SEQRES 7 B 144 GLY ALA ASN ILE GLN ALA SER THR LEU THR THR LEU LEU
SEQRES 8 B 144 LEU LYS GLU LEU ASP ILE PRO ASN ILE TRP VAL LYS ALA
SEQRES 9 B 144 GLN ASN TYR TYR HIS HIS LYS VAL LEU GLU LYS ILE GLY
SEQRES 10 B 144 ALA ASP ARG ILE ILE HIS PRO GLU LYS ASP MET GLY VAL
SEQRES 11 B 144 LYS ILE ALA GLN SER LEU SER ASP GLU ASN VAL LEU ASN
SEQRES 12 B 144 TYR
HET ATP A 601 31
HET ATP B 602 31
HETNAM ATP ADENOSINE-5'-TRIPHOSPHATE
FORMUL 3 ATP 2(C10 H16 N5 O13 P3)
HELIX 1 1 GLY A 15 MET A 28 1 14
HELIX 2 2 ASN A 38 ALA A 46 1 9
HELIX 3 3 ASN A 61 LEU A 66 1 6
HELIX 4 4 GLY A 67 PHE A 71 5 5
HELIX 5 5 ASN A 81 LEU A 95 1 15
HELIX 6 6 ASN A 106 GLY A 117 1 12
HELIX 7 7 HIS A 123 ASN A 140 1 18
HELIX 8 8 GLY B 15 MET B 28 1 14
HELIX 9 9 ASN B 38 ALA B 44 1 7
HELIX 10 10 ASN B 61 LEU B 66 1 6
HELIX 11 11 GLY B 67 PHE B 71 5 5
HELIX 12 12 ASN B 81 LEU B 95 1 15
HELIX 13 13 ASN B 106 GLY B 117 1 12
HELIX 14 14 HIS B 123 LEU B 142 1 20
SHEET 1 A 6 HIS A 51 VAL A 53 0
SHEET 2 A 6 LEU A 33 VAL A 35 1 N ALA A 34 O HIS A 51
SHEET 3 A 6 PHE A 9 ILE A 12 1 N VAL A 11 O LEU A 33
SHEET 4 A 6 TYR A 73 VAL A 76 1 O ILE A 75 N ILE A 12
SHEET 5 A 6 ASN A 99 LYS A 103 1 O TRP A 101 N VAL A 76
SHEET 6 A 6 ARG A 120 ILE A 122 1 O ARG A 120 N VAL A 102
SHEET 1 B 6 HIS B 51 VAL B 53 0
SHEET 2 B 6 VAL B 32 VAL B 35 1 N ALA B 34 O HIS B 51
SHEET 3 B 6 PHE B 9 ILE B 12 1 N VAL B 11 O LEU B 33
SHEET 4 B 6 TYR B 73 VAL B 76 1 O TYR B 73 N ALA B 10
SHEET 5 B 6 ASN B 99 LYS B 103 1 O TRP B 101 N VAL B 76
SHEET 6 B 6 ARG B 120 ILE B 122 1 O ILE B 122 N VAL B 102
SITE 1 AC1 15 GLY A 13 GLY A 15 ARG A 16 ASP A 36
SITE 2 AC1 15 ILE A 37 ASN A 38 LYS A 41 ALA A 55
SITE 3 AC1 15 ASN A 56 ALA A 57 THR A 58 ILE A 78
SITE 4 AC1 15 GLY A 79 ALA A 80 ALA A 84
SITE 1 AC2 14 GLU A 125 LEU B 14 ARG B 16 ASP B 36
SITE 2 AC2 14 ILE B 37 ASN B 38 LYS B 41 ALA B 55
SITE 3 AC2 14 ASN B 56 ALA B 57 THR B 58 ILE B 78
SITE 4 AC2 14 GLY B 79 ALA B 80
CRYST1 126.280 126.280 98.612 90.00 90.00 90.00 I 4 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 0.007919 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007919 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010141 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
