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HEADER SIGNALING PROTEIN 21-AUG-04 1WOM
TITLE CRYSTAL STRUCTURE OF RSBQ
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,T.KUMASAKA,N.TANAKA
REVDAT 1 01-FEB-05 1WOM 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. 2.50 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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.23
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1707875.880
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 30951
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) : 0.217
REMARK 3 FREE R VALUE : 0.262
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 1519
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.007
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.66
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4877
REMARK 3 BIN R VALUE (WORKING SET) : 0.2630
REMARK 3 BIN FREE R VALUE : 0.3050
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.30
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 218
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.021
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4213
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 67
REMARK 3 SOLVENT ATOMS : 148
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 47.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -8.17000
REMARK 3 B22 (A**2) : 16.27000
REMARK 3 B33 (A**2) : -8.10000
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) : 0.31
REMARK 3 ESD FROM SIGMAA (A) : 0.32
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) : 0.39
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.36
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.20
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 22.60
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.80
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) : 1.330 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.240 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.070 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.050 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 44.76
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 : MLA.PARAM
REMARK 3 PARAMETER FILE 4 : PGQ.PARAM
REMARK 3 PARAMETER FILE 5 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : PROST.TOP
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 1WOM COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-AUG-2004.
REMARK 100 THE RCSB ID CODE IS RCSB023819.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-MAR-2004
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) : 1.00
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : CRYSTALCLEAR 1.35
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31002
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 31.230
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) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.59
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
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: MOLREP
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 MALONIC ACID, VAPOR
REMARK 280 DIFFUSION, 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 38.75400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.67950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 41.20200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 68.67950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.75400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 41.20200
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 B -1
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 HIS A 57 CG ND1 CD2 CE1 NE2
REMARK 470 SER A 58 OG
REMARK 470 ARG A 61 CG CD NE CZ NH1 NH2
REMARK 470 MET B 2 CG SD CE
REMARK 470 ASP B 59 CG OD1 OD2
REMARK 470 ARG B 61 CG CD NE CZ NH1 NH2
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 22 SD MET A 22 CE -0.066
REMARK 500 MET A 148 SD MET A 148 CE -0.042
REMARK 500 MET A 251 CG MET A 251 SD 0.050
REMARK 500 GLY B 0 N GLY B 0 CA 0.051
REMARK 500 MET B 251 CG MET B 251 SD 0.040
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 GLY A 0 N - CA - C ANGL. DEV. = -8.7 DEGREES
REMARK 500 HIS A 1 N - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 ALA A 38 N - CA - C ANGL. DEV. = 7.3 DEGREES
REMARK 500 ARG A 46 N - CA - C ANGL. DEV. =-12.8 DEGREES
REMARK 500 TYR A 52 N - CA - C ANGL. DEV. =-11.0 DEGREES
REMARK 500 VAL A 91 N - CA - C ANGL. DEV. = -9.7 DEGREES
REMARK 500 GLU A 137 N - CA - C ANGL. DEV. = -8.5 DEGREES
REMARK 500 HIS A 233 N - CA - C ANGL. DEV. = 7.6 DEGREES
REMARK 500 LEU A 234 CA - CB - CG ANGL. DEV. = 8.0 DEGREES
REMARK 500 LEU A 234 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 PRO A 235 N - CA - C ANGL. DEV. = 7.9 DEGREES
REMARK 500 ARG B 46 N - CA - C ANGL. DEV. =-12.5 DEGREES
REMARK 500 VAL B 91 N - CA - C ANGL. DEV. = -7.9 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 85 DISTANCE = 5.46 ANGSTROMS
REMARK 525 HOH 89 DISTANCE = 5.72 ANGSTROMS
REMARK 525 HOH 122 DISTANCE = 5.22 ANGSTROMS
REMARK 525 HOH 126 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH 140 DISTANCE = 5.72 ANGSTROMS
REMARK 525 HOH 147 DISTANCE = 5.02 ANGSTROMS
DBREF 1WOM A 5 269 SWS O07015 RSBQ_BACSU 5 269
DBREF 1WOM B 5 269 SWS O07015 RSBQ_BACSU 5 269
SEQADV 1WOM ALA A -1 SWS O07015 CLONING ARTIFACT
SEQADV 1WOM GLY A 0 SWS O07015 CLONING ARTIFACT
SEQADV 1WOM HIS A 1 SWS O07015 CLONING ARTIFACT
SEQADV 1WOM MET A 2 SWS O07015 CLONING ARTIFACT
SEQADV 1WOM THR A 3 SWS O07015 CLONING ARTIFACT
SEQADV 1WOM SER A 4 SWS O07015 CLONING ARTIFACT
SEQADV 1WOM ALA B -1 SWS O07015 CLONING ARTIFACT
SEQADV 1WOM GLY B 0 SWS O07015 CLONING ARTIFACT
SEQADV 1WOM HIS B 1 SWS O07015 CLONING ARTIFACT
SEQADV 1WOM MET B 2 SWS O07015 CLONING ARTIFACT
SEQADV 1WOM THR B 3 SWS O07015 CLONING ARTIFACT
SEQADV 1WOM 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 MLA 501 7
HET PGQ 601 5
HET PGQ 602 5
HET PGQ 603 5
HET PGQ 604 5
HET PGQ 605 5
HET PGQ 606 5
HET PGQ 607 5
HET PGQ 608 5
HET PGQ 609 5
HET PGQ 610 5
HET PGQ 611 5
HET PGQ 612 5
HETNAM MLA MALONIC ACID
HETNAM PGQ S-1,2-PROPANEDIOL
HETSYN MLA DICARBOXYLIC ACID C3; PROPANEDIOLIC ACID;
HETSYN 2 MLA METAHNEDICARBOXYLIC ACID
FORMUL 3 MLA C3 H4 O4
FORMUL 4 PGQ 12(C3 H8 O2)
FORMUL 16 HOH *148(H2 O1)
HELIX 1 1 GLY A 0 ASN A 9 1 10
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 ASN A 66 GLN A 69 5 4
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 THR A 183 1 15
HELIX 10 10 ASP A 184 PHE A 197 1 14
HELIX 11 11 HIS A 200 VAL A 207 5 8
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 VAL A 269 1 17
HELIX 15 15 HIS B 1 ASN B 9 1 9
HELIX 16 16 ASP B 30 ASN B 35 5 6
HELIX 17 17 VAL B 37 GLU B 42 5 6
HELIX 18 18 SER B 58 TYR B 63 5 6
HELIX 19 19 ASN B 66 GLN B 69 5 4
HELIX 20 20 THR B 70 LEU B 85 1 16
HELIX 21 21 SER B 96 ARG B 109 1 14
HELIX 22 22 GLU B 137 ASN B 151 1 15
HELIX 23 23 ASN B 151 ASN B 165 1 15
HELIX 24 24 ARG B 169 CYS B 181 1 13
HELIX 25 25 ASP B 184 PHE B 197 1 14
HELIX 26 26 ARG B 201 VAL B 207 5 7
HELIX 27 27 PRO B 223 LEU B 234 1 12
HELIX 28 28 CYS B 248 HIS B 253 1 6
HELIX 29 29 HIS B 253 ALA B 267 1 15
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 ILE A 21 O ILE A 48
SHEET 4 A 7 THR A 90 HIS A 95 1 O VAL A 93 N MET A 22
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 MET A 242 N GLN A 215
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 93 N MET B 22
SHEET 5 C 7 PHE B 113 VAL B 119 1 O VAL B 117 N GLY B 94
SHEET 6 C 7 SER B 211 ALA B 217 1 O LEU B 212 N MET B 118
SHEET 7 C 7 SER B 238 ARG B 245 1 O SER B 238 N ILE B 213
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
CISPEP 1 PRO A 129 PRO A 130 0 0.02
CISPEP 2 PRO B 129 PRO B 130 0 -0.08
CRYST1 77.508 82.404 137.359 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 0.012902 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012135 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007280 0.00000
TER 2111 VAL A 269
TER 4215 VAL B 269
MASTER 304 0 13 29 18 0 0 6 4428 2 67 42
END |