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HEADER SIGNALING PROTEIN 11-SEP-04 1WPR
TITLE CRYSTAL STRUCTURE OF RSBQ INHIBITED BY PMSF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SIGMA FACTOR SIGB REGULATION PROTEIN RSBQ;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 5-269;
COMPND 5 SYNONYM: RSBQ;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 GENE: RSBQ;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: ER2566;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PTYB12
KEYWDS ALPHA/BETA HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR T.KANEKO,N.TANAKA,T.KUMASAKA
REVDAT 1 01-FEB-05 1WPR 0
JRNL AUTH T.KANEKO,N.TANAKA,T.KUMASAKA
JRNL TITL CRYSTAL STRUCTURES OF RSBQ, A STRESS-RESPONSE
JRNL TITL 2 REGULATOR IN BACILLUS SUBTILIS
JRNL REF PROTEIN SCI. V. 14 558 2005
JRNL REFN ASTM PRCIEI US ISSN 0961-8368
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.60 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) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.86
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1528633.810
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 26939
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) : 0.231
REMARK 3 FREE R VALUE : 0.292
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1339
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.008
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.80
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4218
REMARK 3 BIN R VALUE (WORKING SET) : 0.2960
REMARK 3 BIN FREE R VALUE : 0.3610
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.50
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 200
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.026
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4070
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 194
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 50.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.63000
REMARK 3 B22 (A**2) : 16.43000
REMARK 3 B33 (A**2) : -8.80000
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) : 0.35
REMARK 3 ESD FROM SIGMAA (A) : 0.37
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.47
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.48
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.011
REMARK 3 BOND ANGLES (DEGREES) : 1.50
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.90
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.98
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.400 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.360 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 1.990 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 2.970 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.35
REMARK 3 BSOL : 60.76
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 : GOL.PARAM
REMARK 3 PARAMETER FILE 4 : PMS.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
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 1WPR COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-SEP-2004.
REMARK 100 THE RCSB ID CODE IS RCSB023859.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-NOV-2003
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL38B1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTALCLEAR
REMARK 200 DATA SCALING SOFTWARE : CRYSTALCLEAR
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26989
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 35.860
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : NULL
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) : 2.69
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
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 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: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.10
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM MALONATE, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 1/2-X,-Y,1/2+Z
REMARK 290 3555 -X,1/2+Y,1/2-Z
REMARK 290 4555 1/2+X,1/2-Y,-Z
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 38.60100
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.46700
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 40.49950
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.46700
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.60100
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 40.49950
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).
REMARK 350
REMARK 350 GENERATING THE BIOMOLECULE
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 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 BIOMOLECULE: 2
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 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 ALA A -1
REMARK 465 ARG A 61
REMARK 465 ALA A 62
REMARK 465 ALA B -1
REMARK 465 SER B 58
REMARK 465 ASP B 59
REMARK 465 LEU B 60
REMARK 465 ARG B 61
REMARK 465 ALA B 62
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 MET A 2 CG SD CE
REMARK 470 SER A 4 OG
REMARK 470 LYS A 18 CG CD CE NZ
REMARK 470 ASP A 44 CG OD1 OD2
REMARK 470 SER A 55 OG
REMARK 470 HIS A 57 CG ND1 CD2 CE1 NE2
REMARK 470 SER A 58 OG
REMARK 470 ASP A 59 CG OD1 OD2
REMARK 470 LEU A 60 CG CD1 CD2
REMARK 470 LYS A 150 CG CD CE NZ
REMARK 470 GLU A 174 CG CD OE1 OE2
REMARK 470 GLN A 259 CG CD OE1 NE2
REMARK 470 LYS A 266 CG CD CE NZ
REMARK 470 MET B 2 CG SD CE
REMARK 470 SER B 4 OG
REMARK 470 ASP B 44 CG OD1 OD2
REMARK 470 SER B 55 OG
REMARK 470 HIS B 57 CG ND1 CD2 CE1 NE2
REMARK 470 TYR B 63 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 ASP B 64 CG OD1 OD2
REMARK 470 LEU B 65 CG CD1 CD2
REMARK 470 ASN B 66 CG OD1 ND2
REMARK 470 LYS B 88 CG CD CE NZ
REMARK 470 ARG B 109 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 131 CG CD OE1 OE2
REMARK 470 TYR B 133 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU B 142 CG CD1 CD2
REMARK 470 GLU B 149 CG CD OE1 OE2
REMARK 470 LYS B 150 CG CD CE NZ
REMARK 470 GLN B 190 CG CD OE1 NE2
REMARK 470 LYS B 228 CG CD CE NZ
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
REMARK 500 O HIS A 231 O HOH 168 2.18
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),F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 MET A 103 SD MET A 103 CE -0.076
REMARK 500 MET A 230 SD MET A 230 CE 0.080
REMARK 500 MET B 118 SD MET B 118 CE 0.064
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 46 N - CA - C ANGL. DEV. =-12.8 DEGREES
REMARK 500 GLY A 56 N - CA - C ANGL. DEV. =-11.9 DEGREES
REMARK 500 ASN A 127 N - CA - C ANGL. DEV. = -9.7 DEGREES
REMARK 500 PRO A 130 N - CA - C ANGL. DEV. = 9.4 DEGREES
REMARK 500 GLU A 131 N - CA - C ANGL. DEV. = 10.8 DEGREES
REMARK 500 ASN B 35 N - CA - C ANGL. DEV. = 9.3 DEGREES
REMARK 500 ARG B 46 N - CA - C ANGL. DEV. =-12.8 DEGREES
REMARK 500 TYR B 52 N - CA - C ANGL. DEV. = -9.3 DEGREES
REMARK 525
REMARK 525 SOLVENT
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH 71 DISTANCE = 6.17 ANGSTROMS
REMARK 525 HOH 77 DISTANCE = 10.24 ANGSTROMS
REMARK 525 HOH 79 DISTANCE = 5.28 ANGSTROMS
REMARK 525 HOH 92 DISTANCE = 6.06 ANGSTROMS
REMARK 525 HOH 101 DISTANCE = 6.80 ANGSTROMS
REMARK 525 HOH 105 DISTANCE = 6.89 ANGSTROMS
REMARK 525 HOH 119 DISTANCE = 5.20 ANGSTROMS
REMARK 525 HOH 126 DISTANCE = 15.11 ANGSTROMS
REMARK 525 HOH 127 DISTANCE = 13.31 ANGSTROMS
REMARK 525 HOH 132 DISTANCE = 13.60 ANGSTROMS
REMARK 525 HOH 135 DISTANCE = 6.88 ANGSTROMS
REMARK 525 HOH 139 DISTANCE = 11.36 ANGSTROMS
REMARK 525 HOH 141 DISTANCE = 6.13 ANGSTROMS
REMARK 525 HOH 145 DISTANCE = 5.62 ANGSTROMS
REMARK 525 HOH 147 DISTANCE = 6.66 ANGSTROMS
REMARK 525 HOH 152 DISTANCE = 7.15 ANGSTROMS
REMARK 525 HOH 153 DISTANCE = 8.45 ANGSTROMS
REMARK 525 HOH 159 DISTANCE = 13.05 ANGSTROMS
REMARK 525 HOH 161 DISTANCE = 5.56 ANGSTROMS
REMARK 525 HOH 162 DISTANCE = 13.66 ANGSTROMS
REMARK 525 HOH 163 DISTANCE = 7.27 ANGSTROMS
REMARK 525 HOH 164 DISTANCE = 17.68 ANGSTROMS
REMARK 525 HOH 165 DISTANCE = 15.52 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1WOM RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE NATIVE RSBQ
DBREF 1WPR A 5 269 SWS O07015 RSBQ_BACSU 5 269
DBREF 1WPR B 5 269 SWS O07015 RSBQ_BACSU 5 269
SEQADV 1WPR ALA A -1 SWS O07015 CLONING ARTIFACT
SEQADV 1WPR GLY A 0 SWS O07015 CLONING ARTIFACT
SEQADV 1WPR HIS A 1 SWS O07015 CLONING ARTIFACT
SEQADV 1WPR MET A 2 SWS O07015 CLONING ARTIFACT
SEQADV 1WPR THR A 3 SWS O07015 CLONING ARTIFACT
SEQADV 1WPR SER A 4 SWS O07015 CLONING ARTIFACT
SEQADV 1WPR ALA B -1 SWS O07015 CLONING ARTIFACT
SEQADV 1WPR GLY B 0 SWS O07015 CLONING ARTIFACT
SEQADV 1WPR HIS B 1 SWS O07015 CLONING ARTIFACT
SEQADV 1WPR MET B 2 SWS O07015 CLONING ARTIFACT
SEQADV 1WPR THR B 3 SWS O07015 CLONING ARTIFACT
SEQADV 1WPR SER B 4 SWS O07015 CLONING ARTIFACT
SEQRES 1 A 271 ALA GLY HIS MET THR SER ILE LEU SER ARG ASN HIS VAL
SEQRES 2 A 271 LYS VAL LYS GLY SER GLY LYS ALA SER ILE MET PHE ALA
SEQRES 3 A 271 PRO GLY PHE GLY CYS ASP GLN SER VAL TRP ASN ALA VAL
SEQRES 4 A 271 ALA PRO ALA PHE GLU GLU ASP HIS ARG VAL ILE LEU PHE
SEQRES 5 A 271 ASP TYR VAL GLY SER GLY HIS SER ASP LEU ARG ALA TYR
SEQRES 6 A 271 ASP LEU ASN ARG TYR GLN THR LEU ASP GLY TYR ALA GLN
SEQRES 7 A 271 ASP VAL LEU ASP VAL CYS GLU ALA LEU ASP LEU LYS GLU
SEQRES 8 A 271 THR VAL PHE VAL GLY HIS SER VAL GLY ALA LEU ILE GLY
SEQRES 9 A 271 MET LEU ALA SER ILE ARG ARG PRO GLU LEU PHE SER HIS
SEQRES 10 A 271 LEU VAL MET VAL GLY PRO SER PRO CYS TYR LEU ASN ASP
SEQRES 11 A 271 PRO PRO GLU TYR TYR GLY GLY PHE GLU GLU GLU GLN LEU
SEQRES 12 A 271 LEU GLY LEU LEU GLU MET MET GLU LYS ASN TYR ILE GLY
SEQRES 13 A 271 TRP ALA THR VAL PHE ALA ALA THR VAL LEU ASN GLN PRO
SEQRES 14 A 271 ASP ARG PRO GLU ILE LYS GLU GLU LEU GLU SER ARG PHE
SEQRES 15 A 271 CYS SER THR ASP PRO VAL ILE ALA ARG GLN PHE ALA LYS
SEQRES 16 A 271 ALA ALA PHE PHE SER ASP HIS ARG GLU ASP LEU SER LYS
SEQRES 17 A 271 VAL THR VAL PRO SER LEU ILE LEU GLN CYS ALA ASP ASP
SEQRES 18 A 271 ILE ILE ALA PRO ALA THR VAL GLY LYS TYR MET HIS GLN
SEQRES 19 A 271 HIS LEU PRO TYR SER SER LEU LYS GLN MET GLU ALA ARG
SEQRES 20 A 271 GLY HIS CYS PRO HIS MET SER HIS PRO ASP GLU THR ILE
SEQRES 21 A 271 GLN LEU ILE GLY ASP TYR LEU LYS ALA HIS VAL
SEQRES 1 B 271 ALA GLY HIS MET THR SER ILE LEU SER ARG ASN HIS VAL
SEQRES 2 B 271 LYS VAL LYS GLY SER GLY LYS ALA SER ILE MET PHE ALA
SEQRES 3 B 271 PRO GLY PHE GLY CYS ASP GLN SER VAL TRP ASN ALA VAL
SEQRES 4 B 271 ALA PRO ALA PHE GLU GLU ASP HIS ARG VAL ILE LEU PHE
SEQRES 5 B 271 ASP TYR VAL GLY SER GLY HIS SER ASP LEU ARG ALA TYR
SEQRES 6 B 271 ASP LEU ASN ARG TYR GLN THR LEU ASP GLY TYR ALA GLN
SEQRES 7 B 271 ASP VAL LEU ASP VAL CYS GLU ALA LEU ASP LEU LYS GLU
SEQRES 8 B 271 THR VAL PHE VAL GLY HIS SER VAL GLY ALA LEU ILE GLY
SEQRES 9 B 271 MET LEU ALA SER ILE ARG ARG PRO GLU LEU PHE SER HIS
SEQRES 10 B 271 LEU VAL MET VAL GLY PRO SER PRO CYS TYR LEU ASN ASP
SEQRES 11 B 271 PRO PRO GLU TYR TYR GLY GLY PHE GLU GLU GLU GLN LEU
SEQRES 12 B 271 LEU GLY LEU LEU GLU MET MET GLU LYS ASN TYR ILE GLY
SEQRES 13 B 271 TRP ALA THR VAL PHE ALA ALA THR VAL LEU ASN GLN PRO
SEQRES 14 B 271 ASP ARG PRO GLU ILE LYS GLU GLU LEU GLU SER ARG PHE
SEQRES 15 B 271 CYS SER THR ASP PRO VAL ILE ALA ARG GLN PHE ALA LYS
SEQRES 16 B 271 ALA ALA PHE PHE SER ASP HIS ARG GLU ASP LEU SER LYS
SEQRES 17 B 271 VAL THR VAL PRO SER LEU ILE LEU GLN CYS ALA ASP ASP
SEQRES 18 B 271 ILE ILE ALA PRO ALA THR VAL GLY LYS TYR MET HIS GLN
SEQRES 19 B 271 HIS LEU PRO TYR SER SER LEU LYS GLN MET GLU ALA ARG
SEQRES 20 B 271 GLY HIS CYS PRO HIS MET SER HIS PRO ASP GLU THR ILE
SEQRES 21 B 271 GLN LEU ILE GLY ASP TYR LEU LYS ALA HIS VAL
HET PMS A1001 10
HET PMS B1002 10
HET GOL 2001 6
HET GOL 2002 6
HET GOL 2003 6
HET GOL 2004 6
HETNAM PMS BENZYLSULFINIC ACID
HETNAM GOL GLYCEROL
FORMUL 3 PMS 2(C7 H8 O2 S1)
FORMUL 5 GOL 4(C3 H8 O3)
FORMUL 9 HOH *170(H2 O1)
HELIX 1 1 HIS A 1 ASN A 9 1 9
HELIX 2 2 ASP A 30 ASN A 35 5 6
HELIX 3 3 VAL A 37 GLU A 42 5 6
HELIX 4 4 LEU A 65 GLN A 69 5 5
HELIX 5 5 THR A 70 LEU A 85 1 16
HELIX 6 6 SER A 96 ARG A 109 1 14
HELIX 7 7 GLU A 137 ASN A 151 1 15
HELIX 8 8 ASN A 151 ASN A 165 1 15
HELIX 9 9 ARG A 169 SER A 182 1 14
HELIX 10 10 ASP A 184 PHE A 197 1 14
HELIX 11 11 ASP A 203 VAL A 207 5 5
HELIX 12 12 PRO A 223 LEU A 234 1 12
HELIX 13 13 CYS A 248 HIS A 253 1 6
HELIX 14 14 HIS A 253 HIS A 268 1 16
HELIX 15 15 HIS B 1 ASN B 9 1 9
HELIX 16 16 ASP B 30 GLU B 42 5 13
HELIX 17 17 LEU B 71 LEU B 85 1 15
HELIX 18 18 SER B 96 ARG B 109 1 14
HELIX 19 19 GLU B 137 ASN B 151 1 15
HELIX 20 20 ASN B 151 ASN B 165 1 15
HELIX 21 21 ARG B 169 SER B 182 1 14
HELIX 22 22 ASP B 184 PHE B 197 1 14
HELIX 23 23 GLU B 202 VAL B 207 5 6
HELIX 24 24 PRO B 223 LEU B 234 1 12
HELIX 25 25 CYS B 248 HIS B 253 1 6
HELIX 26 26 HIS B 253 VAL B 269 1 17
SHEET 1 A 7 LYS A 12 GLY A 15 0
SHEET 2 A 7 ARG A 46 LEU A 49 -1 O VAL A 47 N LYS A 14
SHEET 3 A 7 SER A 20 ALA A 24 1 N PHE A 23 O ILE A 48
SHEET 4 A 7 THR A 90 HIS A 95 1 O VAL A 91 N SER A 20
SHEET 5 A 7 PHE A 113 VAL A 119 1 O VAL A 117 N PHE A 92
SHEET 6 A 7 SER A 211 ALA A 217 1 O LEU A 212 N MET A 118
SHEET 7 A 7 SER A 237 ARG A 245 1 O SER A 238 N ILE A 213
SHEET 1 B 2 ASN A 127 ASP A 128 0
SHEET 2 B 2 TYR A 132 TYR A 133 -1 O TYR A 132 N ASP A 128
SHEET 1 C 7 LYS B 12 GLY B 15 0
SHEET 2 C 7 HIS B 45 LEU B 49 -1 O VAL B 47 N LYS B 14
SHEET 3 C 7 ALA B 19 ALA B 24 1 N ILE B 21 O ILE B 48
SHEET 4 C 7 THR B 90 HIS B 95 1 O VAL B 91 N SER B 20
SHEET 5 C 7 PHE B 113 VAL B 119 1 O VAL B 119 N GLY B 94
SHEET 6 C 7 SER B 211 ALA B 217 1 O LEU B 214 N MET B 118
SHEET 7 C 7 SER B 238 ARG B 245 1 O MET B 242 N GLN B 215
SHEET 1 D 2 ASN B 127 ASP B 128 0
SHEET 2 D 2 TYR B 132 TYR B 133 -1 O TYR B 132 N ASP B 128
LINK S PMS A1001 OG SER A 96
LINK S PMS B1002 OG SER B 96
CISPEP 1 PRO A 129 PRO A 130 0 0.31
CISPEP 2 PRO B 129 PRO B 130 0 -0.09
CRYST1 77.202 80.999 136.934 90.00 90.00 90.00 P 21 21 21 8
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 0.012953 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012346 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007303 0.00000
TER 2063 VAL A 269
TER 4072 VAL B 269
MASTER 358 0 6 26 18 0 0 6 4284 2 46 42
END |