| content |
HEADER HYDROLASE 19-JUL-04 1U2E
TITLE CRYSTAL STRUCTURE OF THE C-C BOND HYDROLASE MHPC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 2-HYDROXY-6-KETONONA-2,4-DIENEDIOIC ACID
COMPND 3 HYDROLASE;
COMPND 4 CHAIN: A, B, C, D;
COMPND 5 SYNONYM: 2-HYDROXY-6-KETO-NONA-2,4-DIENE-1,9-DIOIC ACID 5,
COMPND 6 6-HYDROLASE;
COMPND 7 EC: 3.7.1.-;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_COMMON: BACTERIA;
SOURCE 4 GENE: MHPC;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: BACTERIA;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PIPC
KEYWDS ALPHA/BETA HYDROLASE FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR M.G.MONTGOMERY,G.DUNN,F.MOHAMMED,T.ROBERTSON,J.-L.GARCIA,
AUTHOR 2 A.COKER,T.D.H.BUGG,S.P.WOOD
REVDAT 1 15-FEB-05 1U2E 0
JRNL AUTH G.DUNN,M.G.MONTGOMERY,F.MOHAMMED,A.COKER,
JRNL AUTH 2 J.B.COOPER,T.ROBERTSON,J.-L.GARCIA,T.D.H.BUGG,
JRNL AUTH 3 S.P.WOOD
JRNL TITL THE STRUCTURE OF THE C-C BOND HYDROLASE MHPC
JRNL TITL 2 PROVIDES INSIGHTS INTO ITS CATALYTIC MECHANISM
JRNL REF J.MOL.BIOL. V. 346 253 2005
JRNL REFN ASTM JMOBAK UK ISSN 0022-2836
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.10 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) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
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) (%) : 93.2
REMARK 3 NUMBER OF REFLECTIONS : 71393
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE-R
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.219
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 3619
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 : 8944
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 544
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.20
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) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.24
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ANISOTROPIC
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 1U2E COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JUL-2004.
REMARK 100 THE RCSB ID CODE IS RCSB023159.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-2002
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SRS
REMARK 200 BEAMLINE : PX14.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.87
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 71688
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 20.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.7
REMARK 200 DATA REDUNDANCY : 4.600
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 6.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 72.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.00
REMARK 200 R MERGE FOR SHELL (I) : 0.54800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 1.300
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: MAD STRUCTURE OF MHPC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: MPD, PEG 8000, TRIS, CALCIUM
REMARK 280 CHLORIDE, PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 298.0K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 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 1/2-X,1/2+Y,-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 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 -1.000000 0.000000 0.000000 72.42900
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 72.07700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 72.42900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 72.07700
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 4 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, C
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, D
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 MET A -4
REMARK 465 MET A -3
REMARK 465 SER A -2
REMARK 465 MET B 996
REMARK 465 MET B 997
REMARK 465 SER B 998
REMARK 465 MET C 1996
REMARK 465 MET C 1997
REMARK 465 SER C 1998
REMARK 465 MET D 2996
REMARK 465 MET D 2997
REMARK 465 SER D 2998
REMARK 465 TYR D 2999
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 240 SD MET A 240 CE -0.037
REMARK 500 MET B1111 SD MET B1111 CE -0.035
REMARK 500 PRO D3070 CB PRO D3070 CG 0.035
REMARK 500 MET D3240 SD MET D3240 CE -0.035
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 63 N - CA - C ANGL. DEV. =-11.6 DEGREES
REMARK 500 ASP A 68 N - CA - C ANGL. DEV. = -8.1 DEGREES
REMARK 500 HIS A 105 N - CA - C ANGL. DEV. =-10.8 DEGREES
REMARK 500 LEU A 107 N - CA - C ANGL. DEV. = -7.4 DEGREES
REMARK 500 SER A 141 N - CA - C ANGL. DEV. = -7.7 DEGREES
REMARK 500 GLN A 226 N - CA - C ANGL. DEV. = -9.8 DEGREES
REMARK 500 LEU A 246 CA - CB - CG ANGL. DEV. = 9.3 DEGREES
REMARK 500 LEU A 247 CA - CB - CG ANGL. DEV. = 8.3 DEGREES
REMARK 500 LEU B1020 CA - CB - CG ANGL. DEV. = 7.6 DEGREES
REMARK 500 PHE B1050 N - CA - C ANGL. DEV. = 7.4 DEGREES
REMARK 500 ARG B1063 N - CA - C ANGL. DEV. =-12.5 DEGREES
REMARK 500 ASP B1068 N - CA - C ANGL. DEV. = -7.7 DEGREES
REMARK 500 HIS B1105 N - CA - C ANGL. DEV. = -9.0 DEGREES
REMARK 500 LEU B1107 N - CA - C ANGL. DEV. = -9.2 DEGREES
REMARK 500 LEU B1132 CA - CB - CG ANGL. DEV. = 8.1 DEGREES
REMARK 500 GLN B1226 N - CA - C ANGL. DEV. = -7.4 DEGREES
REMARK 500 LEU C2020 CA - CB - CG ANGL. DEV. = 7.5 DEGREES
REMARK 500 ARG C2063 N - CA - C ANGL. DEV. =-11.1 DEGREES
REMARK 500 HIS C2105 N - CA - C ANGL. DEV. =-11.0 DEGREES
REMARK 500 LEU C2107 N - CA - C ANGL. DEV. = -9.9 DEGREES
REMARK 500 GLY C2128 N - CA - C ANGL. DEV. = -7.7 DEGREES
REMARK 500 LEU C2132 CA - CB - CG ANGL. DEV. = 8.9 DEGREES
REMARK 500 PHE C2143 N - CA - C ANGL. DEV. = 8.1 DEGREES
REMARK 500 GLN C2226 N - CA - C ANGL. DEV. = -8.2 DEGREES
REMARK 500 LEU D3020 CA - CB - CG ANGL. DEV. = 8.0 DEGREES
REMARK 500 HIS D3038 N - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 PHE D3050 N - CA - C ANGL. DEV. = 8.6 DEGREES
REMARK 500 ARG D3063 N - CA - C ANGL. DEV. =-11.5 DEGREES
REMARK 500 HIS D3105 N - CA - C ANGL. DEV. =-11.8 DEGREES
REMARK 500 LEU D3107 N - CA - C ANGL. DEV. = -8.4 DEGREES
REMARK 500 SER D3141 N - CA - C ANGL. DEV. = -8.0 DEGREES
REMARK 500 PHE D3143 N - CA - C ANGL. DEV. = 8.1 DEGREES
REMARK 500 GLN D3226 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 LEU D3246 CA - CB - CG ANGL. DEV. = 9.0 DEGREES
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 M RES CSSEQI PSI PHI
REMARK 500 SER A 110 -116.10 55.12
REMARK 500 SER B1110 -110.58 49.57
REMARK 500 SER C2110 -108.59 60.02
REMARK 500 SER D3110 -115.68 58.15
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 228 DISTANCE = 5.21 ANGSTROMS
REMARK 525 HOH 237 DISTANCE = 5.59 ANGSTROMS
REMARK 525 HOH 301 DISTANCE = 5.04 ANGSTROMS
REMARK 525 HOH 363 DISTANCE = 5.63 ANGSTROMS
REMARK 525 HOH 384 DISTANCE = 5.34 ANGSTROMS
REMARK 525 HOH 418 DISTANCE = 5.36 ANGSTROMS
DBREF 1U2E A -4 284 SWS P77044 MHPC_ECOLI 5 293
DBREF 1U2E B 996 1284 SWS P77044 MHPC_ECOLI 5 293
DBREF 1U2E C 1996 2284 SWS P77044 MHPC_ECOLI 5 293
DBREF 1U2E D 2996 3284 SWS P77044 MHPC_ECOLI 5 293
SEQRES 1 A 289 MET MET SER TYR GLN PRO GLN THR GLU ALA ALA THR SER
SEQRES 2 A 289 ARG PHE LEU ASN VAL GLU GLU ALA GLY LYS THR LEU ARG
SEQRES 3 A 289 ILE HIS PHE ASN ASP CYS GLY GLN GLY ASP GLU THR VAL
SEQRES 4 A 289 VAL LEU LEU HIS GLY SER GLY PRO GLY ALA THR GLY TRP
SEQRES 5 A 289 ALA ASN PHE SER ARG ASN ILE ASP PRO LEU VAL GLU ALA
SEQRES 6 A 289 GLY TYR ARG VAL ILE LEU LEU ASP CYS PRO GLY TRP GLY
SEQRES 7 A 289 LYS SER ASP SER VAL VAL ASN SER GLY SER ARG SER ASP
SEQRES 8 A 289 LEU ASN ALA ARG ILE LEU LYS SER VAL VAL ASP GLN LEU
SEQRES 9 A 289 ASP ILE ALA LYS ILE HIS LEU LEU GLY ASN SER MET GLY
SEQRES 10 A 289 GLY HIS SER SER VAL ALA PHE THR LEU LYS TRP PRO GLU
SEQRES 11 A 289 ARG VAL GLY LYS LEU VAL LEU MET GLY GLY GLY THR GLY
SEQRES 12 A 289 GLY MET SER LEU PHE THR PRO MET PRO THR GLU GLY ILE
SEQRES 13 A 289 LYS ARG LEU ASN GLN LEU TYR ARG GLN PRO THR ILE GLU
SEQRES 14 A 289 ASN LEU LYS LEU MET MET ASP ILE PHE VAL PHE ASP THR
SEQRES 15 A 289 SER ASP LEU THR ASP ALA LEU PHE GLU ALA ARG LEU ASN
SEQRES 16 A 289 ASN MET LEU SER ARG ARG ASP HIS LEU GLU ASN PHE VAL
SEQRES 17 A 289 LYS SER LEU GLU ALA ASN PRO LYS GLN PHE PRO ASP PHE
SEQRES 18 A 289 GLY PRO ARG LEU ALA GLU ILE LYS ALA GLN THR LEU ILE
SEQRES 19 A 289 VAL TRP GLY ARG ASN ASP ARG PHE VAL PRO MET ASP ALA
SEQRES 20 A 289 GLY LEU ARG LEU LEU SER GLY ILE ALA GLY SER GLU LEU
SEQRES 21 A 289 HIS ILE PHE ARG ASP CYS GLY HIS TRP ALA GLN TRP GLU
SEQRES 22 A 289 HIS ALA ASP ALA PHE ASN GLN LEU VAL LEU ASN PHE LEU
SEQRES 23 A 289 ALA ARG PRO
SEQRES 1 B 289 MET MET SER TYR GLN PRO GLN THR GLU ALA ALA THR SER
SEQRES 2 B 289 ARG PHE LEU ASN VAL GLU GLU ALA GLY LYS THR LEU ARG
SEQRES 3 B 289 ILE HIS PHE ASN ASP CYS GLY GLN GLY ASP GLU THR VAL
SEQRES 4 B 289 VAL LEU LEU HIS GLY SER GLY PRO GLY ALA THR GLY TRP
SEQRES 5 B 289 ALA ASN PHE SER ARG ASN ILE ASP PRO LEU VAL GLU ALA
SEQRES 6 B 289 GLY TYR ARG VAL ILE LEU LEU ASP CYS PRO GLY TRP GLY
SEQRES 7 B 289 LYS SER ASP SER VAL VAL ASN SER GLY SER ARG SER ASP
SEQRES 8 B 289 LEU ASN ALA ARG ILE LEU LYS SER VAL VAL ASP GLN LEU
SEQRES 9 B 289 ASP ILE ALA LYS ILE HIS LEU LEU GLY ASN SER MET GLY
SEQRES 10 B 289 GLY HIS SER SER VAL ALA PHE THR LEU LYS TRP PRO GLU
SEQRES 11 B 289 ARG VAL GLY LYS LEU VAL LEU MET GLY GLY GLY THR GLY
SEQRES 12 B 289 GLY MET SER LEU PHE THR PRO MET PRO THR GLU GLY ILE
SEQRES 13 B 289 LYS ARG LEU ASN GLN LEU TYR ARG GLN PRO THR ILE GLU
SEQRES 14 B 289 ASN LEU LYS LEU MET MET ASP ILE PHE VAL PHE ASP THR
SEQRES 15 B 289 SER ASP LEU THR ASP ALA LEU PHE GLU ALA ARG LEU ASN
SEQRES 16 B 289 ASN MET LEU SER ARG ARG ASP HIS LEU GLU ASN PHE VAL
SEQRES 17 B 289 LYS SER LEU GLU ALA ASN PRO LYS GLN PHE PRO ASP PHE
SEQRES 18 B 289 GLY PRO ARG LEU ALA GLU ILE LYS ALA GLN THR LEU ILE
SEQRES 19 B 289 VAL TRP GLY ARG ASN ASP ARG PHE VAL PRO MET ASP ALA
SEQRES 20 B 289 GLY LEU ARG LEU LEU SER GLY ILE ALA GLY SER GLU LEU
SEQRES 21 B 289 HIS ILE PHE ARG ASP CYS GLY HIS TRP ALA GLN TRP GLU
SEQRES 22 B 289 HIS ALA ASP ALA PHE ASN GLN LEU VAL LEU ASN PHE LEU
SEQRES 23 B 289 ALA ARG PRO
SEQRES 1 C 289 MET MET SER TYR GLN PRO GLN THR GLU ALA ALA THR SER
SEQRES 2 C 289 ARG PHE LEU ASN VAL GLU GLU ALA GLY LYS THR LEU ARG
SEQRES 3 C 289 ILE HIS PHE ASN ASP CYS GLY GLN GLY ASP GLU THR VAL
SEQRES 4 C 289 VAL LEU LEU HIS GLY SER GLY PRO GLY ALA THR GLY TRP
SEQRES 5 C 289 ALA ASN PHE SER ARG ASN ILE ASP PRO LEU VAL GLU ALA
SEQRES 6 C 289 GLY TYR ARG VAL ILE LEU LEU ASP CYS PRO GLY TRP GLY
SEQRES 7 C 289 LYS SER ASP SER VAL VAL ASN SER GLY SER ARG SER ASP
SEQRES 8 C 289 LEU ASN ALA ARG ILE LEU LYS SER VAL VAL ASP GLN LEU
SEQRES 9 C 289 ASP ILE ALA LYS ILE HIS LEU LEU GLY ASN SER MET GLY
SEQRES 10 C 289 GLY HIS SER SER VAL ALA PHE THR LEU LYS TRP PRO GLU
SEQRES 11 C 289 ARG VAL GLY LYS LEU VAL LEU MET GLY GLY GLY THR GLY
SEQRES 12 C 289 GLY MET SER LEU PHE THR PRO MET PRO THR GLU GLY ILE
SEQRES 13 C 289 LYS ARG LEU ASN GLN LEU TYR ARG GLN PRO THR ILE GLU
SEQRES 14 C 289 ASN LEU LYS LEU MET MET ASP ILE PHE VAL PHE ASP THR
SEQRES 15 C 289 SER ASP LEU THR ASP ALA LEU PHE GLU ALA ARG LEU ASN
SEQRES 16 C 289 ASN MET LEU SER ARG ARG ASP HIS LEU GLU ASN PHE VAL
SEQRES 17 C 289 LYS SER LEU GLU ALA ASN PRO LYS GLN PHE PRO ASP PHE
SEQRES 18 C 289 GLY PRO ARG LEU ALA GLU ILE LYS ALA GLN THR LEU ILE
SEQRES 19 C 289 VAL TRP GLY ARG ASN ASP ARG PHE VAL PRO MET ASP ALA
SEQRES 20 C 289 GLY LEU ARG LEU LEU SER GLY ILE ALA GLY SER GLU LEU
SEQRES 21 C 289 HIS ILE PHE ARG ASP CYS GLY HIS TRP ALA GLN TRP GLU
SEQRES 22 C 289 HIS ALA ASP ALA PHE ASN GLN LEU VAL LEU ASN PHE LEU
SEQRES 23 C 289 ALA ARG PRO
SEQRES 1 D 289 MET MET SER TYR GLN PRO GLN THR GLU ALA ALA THR SER
SEQRES 2 D 289 ARG PHE LEU ASN VAL GLU GLU ALA GLY LYS THR LEU ARG
SEQRES 3 D 289 ILE HIS PHE ASN ASP CYS GLY GLN GLY ASP GLU THR VAL
SEQRES 4 D 289 VAL LEU LEU HIS GLY SER GLY PRO GLY ALA THR GLY TRP
SEQRES 5 D 289 ALA ASN PHE SER ARG ASN ILE ASP PRO LEU VAL GLU ALA
SEQRES 6 D 289 GLY TYR ARG VAL ILE LEU LEU ASP CYS PRO GLY TRP GLY
SEQRES 7 D 289 LYS SER ASP SER VAL VAL ASN SER GLY SER ARG SER ASP
SEQRES 8 D 289 LEU ASN ALA ARG ILE LEU LYS SER VAL VAL ASP GLN LEU
SEQRES 9 D 289 ASP ILE ALA LYS ILE HIS LEU LEU GLY ASN SER MET GLY
SEQRES 10 D 289 GLY HIS SER SER VAL ALA PHE THR LEU LYS TRP PRO GLU
SEQRES 11 D 289 ARG VAL GLY LYS LEU VAL LEU MET GLY GLY GLY THR GLY
SEQRES 12 D 289 GLY MET SER LEU PHE THR PRO MET PRO THR GLU GLY ILE
SEQRES 13 D 289 LYS ARG LEU ASN GLN LEU TYR ARG GLN PRO THR ILE GLU
SEQRES 14 D 289 ASN LEU LYS LEU MET MET ASP ILE PHE VAL PHE ASP THR
SEQRES 15 D 289 SER ASP LEU THR ASP ALA LEU PHE GLU ALA ARG LEU ASN
SEQRES 16 D 289 ASN MET LEU SER ARG ARG ASP HIS LEU GLU ASN PHE VAL
SEQRES 17 D 289 LYS SER LEU GLU ALA ASN PRO LYS GLN PHE PRO ASP PHE
SEQRES 18 D 289 GLY PRO ARG LEU ALA GLU ILE LYS ALA GLN THR LEU ILE
SEQRES 19 D 289 VAL TRP GLY ARG ASN ASP ARG PHE VAL PRO MET ASP ALA
SEQRES 20 D 289 GLY LEU ARG LEU LEU SER GLY ILE ALA GLY SER GLU LEU
SEQRES 21 D 289 HIS ILE PHE ARG ASP CYS GLY HIS TRP ALA GLN TRP GLU
SEQRES 22 D 289 HIS ALA ASP ALA PHE ASN GLN LEU VAL LEU ASN PHE LEU
SEQRES 23 D 289 ALA ARG PRO
HET CL 1001 1
HET CL 1002 1
HET CL 1003 1
HET CL 1004 1
HETNAM CL CHLORIDE ION
FORMUL 5 CL 4(CL1 1-)
FORMUL 9 HOH *544(H2 O1)
HELIX 1 1 THR A 3 THR A 7 1 5
HELIX 2 2 THR A 45 PHE A 50 1 6
HELIX 3 3 ASN A 53 ALA A 60 1 8
HELIX 4 4 SER A 83 LEU A 99 1 17
HELIX 5 5 SER A 110 TRP A 123 1 14
HELIX 6 6 THR A 148 GLN A 160 1 13
HELIX 7 7 THR A 162 ILE A 172 1 11
HELIX 8 8 THR A 181 ARG A 195 1 15
HELIX 9 9 ARG A 195 ASN A 209 1 15
HELIX 10 10 PHE A 216 ILE A 223 5 8
HELIX 11 11 MET A 240 ILE A 250 1 11
HELIX 12 12 TRP A 264 HIS A 269 1 6
HELIX 13 13 HIS A 269 ALA A 282 1 14
HELIX 14 14 THR B 1003 THR B 1007 1 5
HELIX 15 15 THR B 1045 SER B 1051 1 7
HELIX 16 16 ASN B 1053 ALA B 1060 1 8
HELIX 17 17 SER B 1083 LEU B 1099 1 17
HELIX 18 18 SER B 1110 TRP B 1123 1 14
HELIX 19 19 THR B 1148 GLN B 1160 1 13
HELIX 20 20 THR B 1162 VAL B 1174 1 13
HELIX 21 21 THR B 1181 ARG B 1195 1 15
HELIX 22 22 ARG B 1195 ASN B 1209 1 15
HELIX 23 23 PHE B 1216 ILE B 1223 5 8
HELIX 24 24 MET B 1240 ILE B 1250 1 11
HELIX 25 25 TRP B 1264 HIS B 1269 1 6
HELIX 26 26 HIS B 1269 ALA B 1282 1 14
HELIX 27 27 THR C 2003 THR C 2007 1 5
HELIX 28 28 THR C 2045 SER C 2051 1 7
HELIX 29 29 ASN C 2053 ALA C 2060 1 8
HELIX 30 30 SER C 2083 LEU C 2099 1 17
HELIX 31 31 SER C 2110 TRP C 2123 1 14
HELIX 32 32 THR C 2148 GLN C 2160 1 13
HELIX 33 33 THR C 2162 ILE C 2172 1 11
HELIX 34 34 ASP C 2176 LEU C 2180 5 5
HELIX 35 35 THR C 2181 ARG C 2195 1 15
HELIX 36 36 ARG C 2195 ASN C 2209 1 15
HELIX 37 37 PHE C 2216 ILE C 2223 5 8
HELIX 38 38 MET C 2240 ILE C 2250 1 11
HELIX 39 39 TRP C 2264 HIS C 2269 1 6
HELIX 40 40 HIS C 2269 ALA C 2282 1 14
HELIX 41 41 THR D 3003 THR D 3007 1 5
HELIX 42 42 THR D 3045 SER D 3051 1 7
HELIX 43 43 ASN D 3053 ALA D 3060 1 8
HELIX 44 44 SER D 3083 LEU D 3099 1 17
HELIX 45 45 SER D 3110 TRP D 3123 1 14
HELIX 46 46 THR D 3148 GLN D 3160 1 13
HELIX 47 47 THR D 3162 ILE D 3172 1 11
HELIX 48 48 ASP D 3176 LEU D 3180 5 5
HELIX 49 49 THR D 3181 ARG D 3195 1 15
HELIX 50 50 ARG D 3195 ASN D 3209 1 15
HELIX 51 51 PHE D 3216 ILE D 3223 5 8
HELIX 52 52 MET D 3240 ILE D 3250 1 11
HELIX 53 53 TRP D 3264 HIS D 3269 1 6
HELIX 54 54 HIS D 3269 ALA D 3282 1 14
SHEET 1 A16 SER A 8 GLU A 15 0
SHEET 2 A16 LYS A 18 CYS A 27 -1 O LYS A 18 N GLU A 15
SHEET 3 A16 ARG A 63 LEU A 67 -1 O VAL A 64 N CYS A 27
SHEET 4 A16 THR A 33 LEU A 37 1 N VAL A 34 O ARG A 63
SHEET 5 A16 ILE A 104 ASN A 109 1 O HIS A 105 N VAL A 35
SHEET 6 A16 VAL A 127 MET A 133 1 O GLY A 128 N ILE A 104
SHEET 7 A16 THR A 227 GLY A 232 1 O VAL A 230 N LEU A 132
SHEET 8 A16 GLU A 254 PHE A 258 1 O HIS A 256 N ILE A 229
SHEET 9 A16 GLU C2254 PHE C2258 -1 O ILE C2257 N LEU A 255
SHEET 10 A16 THR C2227 GLY C2232 1 N ILE C2229 O HIS C2256
SHEET 11 A16 VAL C2127 MET C2133 1 N LEU C2132 O VAL C2230
SHEET 12 A16 ILE C2104 ASN C2109 1 N ILE C2104 O GLY C2128
SHEET 13 A16 THR C2033 LEU C2037 1 N VAL C2035 O HIS C2105
SHEET 14 A16 ARG C2063 LEU C2067 1 O ARG C2063 N VAL C2034
SHEET 15 A16 LYS C2018 CYS C2027 -1 N CYS C2027 O VAL C2064
SHEET 16 A16 SER C2008 GLU C2015 -1 N LEU C2011 O ILE C2022
SHEET 1 B16 SER B1008 GLU B1015 0
SHEET 2 B16 LYS B1018 CYS B1027 -1 O ILE B1022 N LEU B1011
SHEET 3 B16 ARG B1063 LEU B1067 -1 O VAL B1064 N CYS B1027
SHEET 4 B16 THR B1033 LEU B1037 1 N VAL B1034 O ARG B1063
SHEET 5 B16 ILE B1104 ASN B1109 1 O HIS B1105 N VAL B1035
SHEET 6 B16 VAL B1127 MET B1133 1 O GLY B1128 N ILE B1104
SHEET 7 B16 THR B1227 GLY B1232 1 O VAL B1230 N LEU B1132
SHEET 8 B16 GLU B1254 PHE B1258 1 O GLU B1254 N ILE B1229
SHEET 9 B16 GLU D3254 PHE D3258 -1 O ILE D3257 N LEU B1255
SHEET 10 B16 THR D3227 GLY D3232 1 N ILE D3229 O GLU D3254
SHEET 11 B16 VAL D3127 MET D3133 1 N LEU D3132 O VAL D3230
SHEET 12 B16 ILE D3104 ASN D3109 1 N LEU D3106 O VAL D3131
SHEET 13 B16 THR D3033 LEU D3037 1 N VAL D3035 O HIS D3105
SHEET 14 B16 ARG D3063 LEU D3067 1 O ILE D3065 N LEU D3036
SHEET 15 B16 LYS D3018 CYS D3027 -1 N CYS D3027 O VAL D3064
SHEET 16 B16 SER D3008 GLU D3015 -1 N GLU D3015 O LYS D3018
CISPEP 1 MET A 146 PRO A 147 0 -0.26
CISPEP 2 MET B 1146 PRO B 1147 0 -0.09
CISPEP 3 MET C 2146 PRO C 2147 0 -0.19
CISPEP 4 MET D 3146 PRO D 3147 0 0.22
CRYST1 144.858 144.154 62.107 90.00 90.00 90.00 P 21 21 2 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 0.006903 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006937 0.000000 0.00000
SCALE3 0.000000 0.000000 0.016101 0.00000
TER 2245 PRO A 284
TER 4490 PRO B1284
TER 6725 PRO C2284
TER 8948 PRO D3284
MASTER 332 0 4 54 32 0 0 6 9492 4 0 92
END |