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HEADER HYDROLASE 13-MAY-05 1ZOI
TITLE CRYSTAL STRUCTURE OF A STEREOSELECTIVE ESTERASE FROM
TITLE 2 PSEUDOMONAS PUTIDA IFO12996
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ESTERASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 EC: 3.1.-.-;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS PUTIDA;
SOURCE 3 ORGANISM_COMMON: BATERIA;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_COMMON: BACTERIA
KEYWDS ESTERASE, PSEUDOMONAS PUTIDA, ALPHA/BETA HYDROLASE FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR F.ELMI,H.T.LEE,J.Y.HUANG,Y.C.HSIEH,Y.L.WANG,Y.J.CHEN,
AUTHOR 2 S.Y.SHAW,C.J.CHEN
REVDAT 1 02-MAY-06 1ZOI 0
JRNL AUTH F.ELMI,H.T.LEE,J.Y.HUANG,Y.C.HSIEH,Y.L.WANG,
JRNL AUTH 2 Y.J.CHEN,S.Y.SHAW,C.J.CHEN
JRNL TITL STEREOSELECTIVE ESTERASE FROM PSEUDOMONAS PUTIDA
JRNL TITL 2 IFO12996 REVEALS ALPHA/BETA HYDROLASE FOLDS FOR
JRNL TITL 3 D-BETA-ACETYLTHIOISOBUTYRIC ACID SYNTHESIS
JRNL REF J.BACTERIOL. V. 187 8470 2005
JRNL REFN ASTM JOBAAY US ISSN 0021-9193
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 1.60 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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 25.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 93768
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 9413
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 : 6377
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 317
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
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) : 0.21
REMARK 3 ESD FROM SIGMAA (A) : 0.07
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) : 0.23
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.11
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.005
REMARK 3 BOND ANGLES (DEGREES) : 1.30
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 : 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 1ZOI COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-MAY-2005.
REMARK 100 THE RCSB ID CODE IS RCSB032958.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-OCT-2004
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 4.00
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL12B2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
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 : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 93768
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.3
REMARK 200 DATA REDUNDANCY : 6.300
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) : 1.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.66
REMARK 200 COMPLETENESS FOR SHELL (%) : 82.3
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 (%): 40.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, CITRIC ACID, PH
REMARK 280 4.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K
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 25.27800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 76.81500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 49.05400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 76.81500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.27800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 49.05400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT
REMARK 300 WHICH CONSISTS OF 3 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, B, 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 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 MET B 1
REMARK 465 SER B 276
REMARK 465 MET C 1
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 PRO A 32 CG PRO A 32 CD 0.038
REMARK 500 MET A 72 SD MET A 72 CE -0.059
REMARK 500 MET A 189 CG MET A 189 SD 0.040
REMARK 500 MET A 222 SD MET A 222 CE -0.042
REMARK 500 PRO B 32 CB PRO B 32 CG 0.050
REMARK 500 PRO B 32 CG PRO B 32 CD 0.046
REMARK 500 PRO C 32 CG PRO C 32 CD 0.032
REMARK 500 MET C 107 CG MET C 107 SD -0.033
REMARK 500 MET C 189 CG MET C 189 SD 0.037
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 9 N - CA - C ANGL. DEV. = 7.8 DEGREES
REMARK 500 VAL A 24 N - CA - C ANGL. DEV. = 8.6 DEGREES
REMARK 500 PRO A 32 C - N - CA ANGL. DEV. = 9.6 DEGREES
REMARK 500 LEU A 33 N - CA - C ANGL. DEV. = 8.0 DEGREES
REMARK 500 ARG A 51 N - CA - C ANGL. DEV. =-12.0 DEGREES
REMARK 500 VAL A 92 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 PRO A 165 N - CA - C ANGL. DEV. = 9.6 DEGREES
REMARK 500 GLY B 9 N - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 ILE B 25 N - CA - C ANGL. DEV. = -7.9 DEGREES
REMARK 500 PRO B 32 C - N - CA ANGL. DEV. = 9.1 DEGREES
REMARK 500 LEU B 33 N - CA - C ANGL. DEV. = 7.6 DEGREES
REMARK 500 GLY B 49 N - CA - C ANGL. DEV. = 9.9 DEGREES
REMARK 500 ARG B 51 N - CA - C ANGL. DEV. =-13.7 DEGREES
REMARK 500 VAL B 92 N - CA - C ANGL. DEV. = -8.6 DEGREES
REMARK 500 VAL B 124 N - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 SER B 152 N - CA - C ANGL. DEV. = 9.0 DEGREES
REMARK 500 ARG B 159 N - CA - C ANGL. DEV. = -7.7 DEGREES
REMARK 500 PRO B 165 N - CA - C ANGL. DEV. = 9.8 DEGREES
REMARK 500 GLY C 9 N - CA - C ANGL. DEV. = 9.3 DEGREES
REMARK 500 VAL C 24 N - CA - C ANGL. DEV. = 8.3 DEGREES
REMARK 500 ILE C 25 N - CA - C ANGL. DEV. = -7.7 DEGREES
REMARK 500 PRO C 32 C - N - CA ANGL. DEV. = 9.5 DEGREES
REMARK 500 LEU C 33 N - CA - C ANGL. DEV. = 7.7 DEGREES
REMARK 500 GLY C 49 N - CA - C ANGL. DEV. = 9.9 DEGREES
REMARK 500 ARG C 51 N - CA - C ANGL. DEV. =-13.0 DEGREES
REMARK 500 SER C 152 N - CA - C ANGL. DEV. = 7.8 DEGREES
REMARK 500 PRO C 165 N - CA - C ANGL. DEV. = 9.2 DEGREES
REMARK 500 PRO C 259 C - N - CA ANGL. DEV. = -7.7 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 97 -118.81 50.24
REMARK 500 SER B 97 -118.90 51.65
DBREF 1ZOI A 1 276 GB 1110542 AAB35246 1 276
DBREF 1ZOI B 1 276 GB 1110542 AAB35246 1 276
DBREF 1ZOI C 1 276 GB 1110542 AAB35246 1 276
SEQADV 1ZOI LEU A 42 GB 1110542 MET 42 CONFLICT
SEQADV 1ZOI GLU A 112 GB 1110542 ALA 112 CONFLICT
SEQADV 1ZOI GLY A 133 GB 1110542 ASP 133 CONFLICT
SEQADV 1ZOI GLU A 175 GB 1110542 ASP 175 CONFLICT
SEQADV 1ZOI GLN A 216 GB 1110542 THR 216 CONFLICT
SEQADV 1ZOI VAL A 237 GB 1110542 LEU 237 CONFLICT
SEQADV 1ZOI ALA A 247 GB 1110542 THR 247 CONFLICT
SEQADV 1ZOI LYS A 252 GB 1110542 GLN 252 CONFLICT
SEQADV 1ZOI LEU B 42 GB 1110542 MET 42 CONFLICT
SEQADV 1ZOI GLU B 112 GB 1110542 ALA 112 CONFLICT
SEQADV 1ZOI GLY B 133 GB 1110542 ASP 133 CONFLICT
SEQADV 1ZOI GLU B 175 GB 1110542 ASP 175 CONFLICT
SEQADV 1ZOI GLN B 216 GB 1110542 THR 216 CONFLICT
SEQADV 1ZOI VAL B 237 GB 1110542 LEU 237 CONFLICT
SEQADV 1ZOI ALA B 247 GB 1110542 THR 247 CONFLICT
SEQADV 1ZOI LYS B 252 GB 1110542 GLN 252 CONFLICT
SEQADV 1ZOI LEU C 42 GB 1110542 MET 42 CONFLICT
SEQADV 1ZOI GLU C 112 GB 1110542 ALA 112 CONFLICT
SEQADV 1ZOI GLY C 133 GB 1110542 ASP 133 CONFLICT
SEQADV 1ZOI GLU C 175 GB 1110542 ASP 175 CONFLICT
SEQADV 1ZOI GLN C 216 GB 1110542 THR 216 CONFLICT
SEQADV 1ZOI VAL C 237 GB 1110542 LEU 237 CONFLICT
SEQADV 1ZOI ALA C 247 GB 1110542 THR 247 CONFLICT
SEQADV 1ZOI LYS C 252 GB 1110542 GLN 252 CONFLICT
SEQRES 1 A 276 MET SER TYR VAL THR THR LYS ASP GLY VAL GLN ILE PHE
SEQRES 2 A 276 TYR LYS ASP TRP GLY PRO ARG ASP ALA PRO VAL ILE HIS
SEQRES 3 A 276 PHE HIS HIS GLY TRP PRO LEU SER ALA ASP ASP TRP ASP
SEQRES 4 A 276 ALA GLN LEU LEU PHE PHE LEU ALA HIS GLY TYR ARG VAL
SEQRES 5 A 276 VAL ALA HIS ASP ARG ARG GLY HIS GLY ARG SER SER GLN
SEQRES 6 A 276 VAL TRP ASP GLY HIS ASP MET ASP HIS TYR ALA ASP ASP
SEQRES 7 A 276 VAL ALA ALA VAL VAL ALA HIS LEU GLY ILE GLN GLY ALA
SEQRES 8 A 276 VAL HIS VAL GLY HIS SER THR GLY GLY GLY GLU VAL VAL
SEQRES 9 A 276 ARG TYR MET ALA ARG HIS PRO GLU ASP LYS VAL ALA LYS
SEQRES 10 A 276 ALA VAL LEU ILE ALA ALA VAL PRO PRO LEU MET VAL GLN
SEQRES 11 A 276 THR PRO GLY ASN PRO GLY GLY LEU PRO LYS SER VAL PHE
SEQRES 12 A 276 ASP GLY PHE GLN ALA GLN VAL ALA SER ASN ARG ALA GLN
SEQRES 13 A 276 PHE TYR ARG ASP VAL PRO ALA GLY PRO PHE TYR GLY TYR
SEQRES 14 A 276 ASN ARG PRO GLY VAL GLU ALA SER GLU GLY ILE ILE GLY
SEQRES 15 A 276 ASN TRP TRP ARG GLN GLY MET ILE GLY SER ALA LYS ALA
SEQRES 16 A 276 HIS TYR ASP GLY ILE VAL ALA PHE SER GLN THR ASP PHE
SEQRES 17 A 276 THR GLU ASP LEU LYS GLY ILE GLN GLN PRO VAL LEU VAL
SEQRES 18 A 276 MET HIS GLY ASP ASP ASP GLN ILE VAL PRO TYR GLU ASN
SEQRES 19 A 276 SER GLY VAL LEU SER ALA LYS LEU LEU PRO ASN GLY ALA
SEQRES 20 A 276 LEU LYS THR TYR LYS GLY TYR PRO HIS GLY MET PRO THR
SEQRES 21 A 276 THR HIS ALA ASP VAL ILE ASN ALA ASP LEU LEU ALA PHE
SEQRES 22 A 276 ILE ARG SER
SEQRES 1 B 276 MET SER TYR VAL THR THR LYS ASP GLY VAL GLN ILE PHE
SEQRES 2 B 276 TYR LYS ASP TRP GLY PRO ARG ASP ALA PRO VAL ILE HIS
SEQRES 3 B 276 PHE HIS HIS GLY TRP PRO LEU SER ALA ASP ASP TRP ASP
SEQRES 4 B 276 ALA GLN LEU LEU PHE PHE LEU ALA HIS GLY TYR ARG VAL
SEQRES 5 B 276 VAL ALA HIS ASP ARG ARG GLY HIS GLY ARG SER SER GLN
SEQRES 6 B 276 VAL TRP ASP GLY HIS ASP MET ASP HIS TYR ALA ASP ASP
SEQRES 7 B 276 VAL ALA ALA VAL VAL ALA HIS LEU GLY ILE GLN GLY ALA
SEQRES 8 B 276 VAL HIS VAL GLY HIS SER THR GLY GLY GLY GLU VAL VAL
SEQRES 9 B 276 ARG TYR MET ALA ARG HIS PRO GLU ASP LYS VAL ALA LYS
SEQRES 10 B 276 ALA VAL LEU ILE ALA ALA VAL PRO PRO LEU MET VAL GLN
SEQRES 11 B 276 THR PRO GLY ASN PRO GLY GLY LEU PRO LYS SER VAL PHE
SEQRES 12 B 276 ASP GLY PHE GLN ALA GLN VAL ALA SER ASN ARG ALA GLN
SEQRES 13 B 276 PHE TYR ARG ASP VAL PRO ALA GLY PRO PHE TYR GLY TYR
SEQRES 14 B 276 ASN ARG PRO GLY VAL GLU ALA SER GLU GLY ILE ILE GLY
SEQRES 15 B 276 ASN TRP TRP ARG GLN GLY MET ILE GLY SER ALA LYS ALA
SEQRES 16 B 276 HIS TYR ASP GLY ILE VAL ALA PHE SER GLN THR ASP PHE
SEQRES 17 B 276 THR GLU ASP LEU LYS GLY ILE GLN GLN PRO VAL LEU VAL
SEQRES 18 B 276 MET HIS GLY ASP ASP ASP GLN ILE VAL PRO TYR GLU ASN
SEQRES 19 B 276 SER GLY VAL LEU SER ALA LYS LEU LEU PRO ASN GLY ALA
SEQRES 20 B 276 LEU LYS THR TYR LYS GLY TYR PRO HIS GLY MET PRO THR
SEQRES 21 B 276 THR HIS ALA ASP VAL ILE ASN ALA ASP LEU LEU ALA PHE
SEQRES 22 B 276 ILE ARG SER
SEQRES 1 C 276 MET SER TYR VAL THR THR LYS ASP GLY VAL GLN ILE PHE
SEQRES 2 C 276 TYR LYS ASP TRP GLY PRO ARG ASP ALA PRO VAL ILE HIS
SEQRES 3 C 276 PHE HIS HIS GLY TRP PRO LEU SER ALA ASP ASP TRP ASP
SEQRES 4 C 276 ALA GLN LEU LEU PHE PHE LEU ALA HIS GLY TYR ARG VAL
SEQRES 5 C 276 VAL ALA HIS ASP ARG ARG GLY HIS GLY ARG SER SER GLN
SEQRES 6 C 276 VAL TRP ASP GLY HIS ASP MET ASP HIS TYR ALA ASP ASP
SEQRES 7 C 276 VAL ALA ALA VAL VAL ALA HIS LEU GLY ILE GLN GLY ALA
SEQRES 8 C 276 VAL HIS VAL GLY HIS SER THR GLY GLY GLY GLU VAL VAL
SEQRES 9 C 276 ARG TYR MET ALA ARG HIS PRO GLU ASP LYS VAL ALA LYS
SEQRES 10 C 276 ALA VAL LEU ILE ALA ALA VAL PRO PRO LEU MET VAL GLN
SEQRES 11 C 276 THR PRO GLY ASN PRO GLY GLY LEU PRO LYS SER VAL PHE
SEQRES 12 C 276 ASP GLY PHE GLN ALA GLN VAL ALA SER ASN ARG ALA GLN
SEQRES 13 C 276 PHE TYR ARG ASP VAL PRO ALA GLY PRO PHE TYR GLY TYR
SEQRES 14 C 276 ASN ARG PRO GLY VAL GLU ALA SER GLU GLY ILE ILE GLY
SEQRES 15 C 276 ASN TRP TRP ARG GLN GLY MET ILE GLY SER ALA LYS ALA
SEQRES 16 C 276 HIS TYR ASP GLY ILE VAL ALA PHE SER GLN THR ASP PHE
SEQRES 17 C 276 THR GLU ASP LEU LYS GLY ILE GLN GLN PRO VAL LEU VAL
SEQRES 18 C 276 MET HIS GLY ASP ASP ASP GLN ILE VAL PRO TYR GLU ASN
SEQRES 19 C 276 SER GLY VAL LEU SER ALA LYS LEU LEU PRO ASN GLY ALA
SEQRES 20 C 276 LEU LYS THR TYR LYS GLY TYR PRO HIS GLY MET PRO THR
SEQRES 21 C 276 THR HIS ALA ASP VAL ILE ASN ALA ASP LEU LEU ALA PHE
SEQRES 22 C 276 ILE ARG SER
FORMUL 4 HOH *317(H2 O1)
HELIX 1 1 SER A 34 ASP A 37 5 4
HELIX 2 2 TRP A 38 HIS A 48 1 11
HELIX 3 3 ASP A 71 GLY A 87 1 17
HELIX 4 4 THR A 98 HIS A 110 1 13
HELIX 5 5 PRO A 139 ASN A 153 1 15
HELIX 6 6 ASN A 153 GLY A 164 1 12
HELIX 7 7 SER A 177 GLY A 191 1 15
HELIX 8 8 SER A 192 GLN A 205 1 14
HELIX 9 9 PHE A 208 ILE A 215 1 8
HELIX 10 10 SER A 235 LEU A 243 1 9
HELIX 11 11 GLY A 257 HIS A 262 1 6
HELIX 12 12 HIS A 262 ARG A 275 1 14
HELIX 13 13 SER B 34 ASP B 37 5 4
HELIX 14 14 TRP B 38 ALA B 47 1 10
HELIX 15 15 ASP B 71 GLY B 87 1 17
HELIX 16 16 THR B 98 HIS B 110 1 13
HELIX 17 17 PRO B 139 ASN B 153 1 15
HELIX 18 18 ASN B 153 GLY B 164 1 12
HELIX 19 19 SER B 177 GLY B 191 1 15
HELIX 20 20 SER B 192 GLN B 205 1 14
HELIX 21 21 PHE B 208 ILE B 215 1 8
HELIX 22 22 SER B 235 LEU B 243 1 9
HELIX 23 23 GLY B 257 HIS B 262 1 6
HELIX 24 24 HIS B 262 ARG B 275 1 14
HELIX 25 25 SER C 34 ASP C 37 5 4
HELIX 26 26 TRP C 38 ALA C 47 1 10
HELIX 27 27 ASP C 71 GLY C 87 1 17
HELIX 28 28 THR C 98 HIS C 110 1 13
HELIX 29 29 PRO C 139 ASN C 153 1 15
HELIX 30 30 ASN C 153 GLY C 164 1 12
HELIX 31 31 SER C 177 ILE C 190 1 14
HELIX 32 32 SER C 192 GLN C 205 1 14
HELIX 33 33 PHE C 208 ILE C 215 1 8
HELIX 34 34 SER C 235 LEU C 243 1 9
HELIX 35 35 GLY C 257 HIS C 262 1 6
HELIX 36 36 HIS C 262 ARG C 275 1 14
SHEET 1 A 8 TYR A 3 THR A 5 0
SHEET 2 A 8 GLN A 11 TRP A 17 -1 O ILE A 12 N VAL A 4
SHEET 3 A 8 ARG A 51 HIS A 55 -1 O VAL A 52 N TRP A 17
SHEET 4 A 8 VAL A 24 HIS A 28 1 N PHE A 27 O VAL A 53
SHEET 5 A 8 VAL A 92 HIS A 96 1 O VAL A 92 N HIS A 26
SHEET 6 A 8 ALA A 118 ILE A 121 1 O ILE A 121 N GLY A 95
SHEET 7 A 8 VAL A 219 GLY A 224 1 O LEU A 220 N LEU A 120
SHEET 8 A 8 GLY A 246 TYR A 251 1 O ALA A 247 N VAL A 221
SHEET 1 B 8 TYR B 3 THR B 5 0
SHEET 2 B 8 GLN B 11 TRP B 17 -1 O ILE B 12 N VAL B 4
SHEET 3 B 8 ARG B 51 HIS B 55 -1 O VAL B 52 N TRP B 17
SHEET 4 B 8 VAL B 24 HIS B 28 1 N PHE B 27 O VAL B 53
SHEET 5 B 8 VAL B 92 HIS B 96 1 O VAL B 92 N HIS B 26
SHEET 6 B 8 ALA B 118 ILE B 121 1 O ILE B 121 N GLY B 95
SHEET 7 B 8 VAL B 219 GLY B 224 1 O MET B 222 N LEU B 120
SHEET 8 B 8 GLY B 246 TYR B 251 1 O ALA B 247 N VAL B 221
SHEET 1 C 8 TYR C 3 THR C 5 0
SHEET 2 C 8 GLN C 11 TRP C 17 -1 O ILE C 12 N VAL C 4
SHEET 3 C 8 ARG C 51 HIS C 55 -1 O VAL C 52 N TRP C 17
SHEET 4 C 8 VAL C 24 HIS C 28 1 N PHE C 27 O VAL C 53
SHEET 5 C 8 VAL C 92 HIS C 96 1 O VAL C 92 N HIS C 26
SHEET 6 C 8 ALA C 118 ILE C 121 1 O ILE C 121 N GLY C 95
SHEET 7 C 8 VAL C 219 GLY C 224 1 O LEU C 220 N LEU C 120
SHEET 8 C 8 GLY C 246 TYR C 251 1 O ALA C 247 N VAL C 221
CISPEP 1 TRP A 31 PRO A 32 0 -0.40
CISPEP 2 PRO A 125 PRO A 126 0 0.16
CISPEP 3 TRP B 31 PRO B 32 0 -0.49
CISPEP 4 PRO B 125 PRO B 126 0 0.27
CISPEP 5 TRP C 31 PRO C 32 0 -0.49
CISPEP 6 PRO C 125 PRO C 126 0 0.02
CRYST1 50.556 98.108 153.630 90.00 90.00 90.00 P 21 21 21 12
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 0.019780 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010193 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006509 0.00000
TER 2129 SER A 276
TER 4251 ARG B 275
TER 6380 SER C 276
MASTER 299 0 0 36 24 0 0 6 6694 3 0 66
END |