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HEADER HYDROLASE 18-MAY-09 3HI4
TITLE SWITCHING CATALYSIS FROM HYDROLYSIS TO PERHYDROLYSIS IN P.
TITLE 2 FLUORESCENS ESTERASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ARYLESTERASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: ARYL-ESTER HYDROLASE, PFE, PUTATIVE
COMPND 5 BROMOPEROXIDASE;
COMPND 6 EC: 3.1.1.2, 1.-.-.-;
COMPND 7 ENGINEERED: YES;
COMPND 8 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: PSEUDOMONAS FLUORESCENS;
SOURCE 3 ORGANISM_TAXID: 294;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PJOE2792
KEYWDS ESTERASE, HYDROLYSIS, PERHYDROLYSIS, HYDROLASE, PEROXIDASE
EXPDTA X-RAY DIFFRACTION
AUTHOR V.M.PURPERO
REVDAT 1 23-FEB-10 3HI4 0
JRNL AUTH D.L.YIN,P.BERNHARDT,K.L.MORLEY,Y.JIANG,
JRNL AUTH 2 J.D.CHEESEMAN,V.PURPERO,J.D.SCHRAG,R.J.KAZLAUSKAS
JRNL TITL SWITCHING CATALYSIS FROM HYDROLYSIS TO
JRNL TITL 2 PERHYDROLYSIS IN PSEUDOMONAS FLUORESCENS ESTERASE.
JRNL REF BIOCHEMISTRY 2010
JRNL REFN ISSN 0006-2960
JRNL PMID 20112920
JRNL DOI 10.1021/BI9021268
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 6.1.1
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 146673
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 + TEST SET) : 0.166
REMARK 3 R VALUE (WORKING SET) : 0.165
REMARK 3 FREE R VALUE : 0.202
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7330
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 12802
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 185
REMARK 3 SOLVENT ATOMS : 1036
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 37.65
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 29.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : 0.00000
REMARK 3 B33 (A**2) : 0.00000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.155
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.147
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.097
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.939
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 DISTANCE RESTRAINTS. RMS SIGMA
REMARK 3 BOND LENGTH (A) : NULL ; NULL
REMARK 3 ANGLE DISTANCE (A) : NULL ; NULL
REMARK 3 INTRAPLANAR 1-4 DISTANCE (A) : NULL ; NULL
REMARK 3 H-BOND OR METAL COORDINATION (A) : NULL ; NULL
REMARK 3
REMARK 3 PLANE RESTRAINT (A) : NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINT (A**3) : NULL ; NULL
REMARK 3
REMARK 3 NON-BONDED CONTACT RESTRAINTS.
REMARK 3 SINGLE TORSION (A) : NULL ; NULL
REMARK 3 MULTIPLE TORSION (A) : NULL ; NULL
REMARK 3 H-BOND (X...Y) (A) : NULL ; NULL
REMARK 3 H-BOND (X-H...Y) (A) : NULL ; NULL
REMARK 3
REMARK 3 CONFORMATIONAL TORSION ANGLE RESTRAINTS.
REMARK 3 SPECIFIED (DEGREES) : NULL ; NULL
REMARK 3 PLANAR (DEGREES) : NULL ; NULL
REMARK 3 STAGGERED (DEGREES) : NULL ; NULL
REMARK 3 TRANSVERSE (DEGREES) : NULL ; 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 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS
REMARK 4
REMARK 4 3HI4 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-MAY-09.
REMARK 100 THE RCSB ID CODE IS RCSB053161.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 08-DEC-08
REMARK 200 TEMPERATURE (KELVIN) : 120
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 146673
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 39.970
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 2.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07900
REMARK 200 FOR THE DATA SET : 12.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.29
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.50
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.35600
REMARK 200 FOR SHELL : 2.150
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: 1VA4
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 72.15
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.75M AMMONIUM SULFATE 1% PEG 400,
REMARK 280 0.1M HEPES PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE
REMARK 280 291K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 86.66000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 43.33000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8560 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27800 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -38.0 KCAL/MOL
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 8990 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F
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 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 DISTANCE
REMARK 500 OD2 ASP C 138 O HOH C 380 2.03
REMARK 500
REMARK 500 REMARK: NULL
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),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 SER A 44 CB SER A 44 OG -0.081
REMARK 500 SER C 44 CB SER C 44 OG -0.093
REMARK 500 SER D 44 CB SER D 44 OG -0.115
REMARK 500 GLU D 87 CD GLU D 87 OE1 0.069
REMARK 500
REMARK 500 REMARK: NULL
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 PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ASP A 15 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ASP A 15 CB - CG - OD2 ANGL. DEV. = -6.5 DEGREES
REMARK 500 ARG A 59 NE - CZ - NH2 ANGL. DEV. = -3.2 DEGREES
REMARK 500 ASP A 74 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 LYS A 189 CD - CE - NZ ANGL. DEV. = -14.5 DEGREES
REMARK 500 ASP B 138 CB - CG - OD1 ANGL. DEV. = -5.7 DEGREES
REMARK 500 ASP B 220 CB - CG - OD1 ANGL. DEV. = 5.7 DEGREES
REMARK 500 ASP B 220 CB - CG - OD2 ANGL. DEV. = -7.0 DEGREES
REMARK 500 ARG C 102 NE - CZ - NH2 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG D 59 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ARG E 151 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP E 202 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG F 111 NE - CZ - NH1 ANGL. DEV. = -3.7 DEGREES
REMARK 500 ARG F 111 NE - CZ - NH2 ANGL. DEV. = 4.9 DEGREES
REMARK 500 ASP F 211 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
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 PRO A 29 65.37 -105.41
REMARK 500 LEU A 30 -147.19 -102.69
REMARK 500 ASP A 31 -168.88 -161.94
REMARK 500 GLN A 62 76.09 -118.57
REMARK 500 SER A 94 -117.20 57.20
REMARK 500 PHE A 125 -63.69 -101.11
REMARK 500 ASP A 150 87.11 -158.72
REMARK 500 THR A 230 -91.47 -127.39
REMARK 500 PRO B 29 72.83 -102.03
REMARK 500 LEU B 30 -148.06 -109.27
REMARK 500 GLN B 62 68.82 -116.67
REMARK 500 SER B 94 -126.00 63.32
REMARK 500 THR B 230 -92.80 -126.88
REMARK 500 PRO C 29 65.23 -110.77
REMARK 500 LEU C 30 -145.40 -98.92
REMARK 500 GLN C 62 68.80 -117.90
REMARK 500 SER C 94 -122.24 55.35
REMARK 500 TYR C 131 57.56 -146.28
REMARK 500 ASP C 150 89.35 -153.69
REMARK 500 THR C 230 -91.45 -129.70
REMARK 500 ASP C 248 2.52 56.09
REMARK 500 PRO D 29 65.45 -107.09
REMARK 500 LEU D 30 -146.38 -100.50
REMARK 500 ASP D 31 -168.91 -161.21
REMARK 500 SER D 94 -122.50 63.72
REMARK 500 PHE D 125 -63.64 -121.42
REMARK 500 TYR D 131 59.85 -140.09
REMARK 500 ASP D 150 84.67 -150.73
REMARK 500 THR D 230 -86.53 -125.49
REMARK 500 ASP D 248 8.63 58.61
REMARK 500 PRO E 29 64.62 -108.00
REMARK 500 LEU E 30 -147.19 -103.06
REMARK 500 GLN E 62 77.84 -119.98
REMARK 500 SER E 94 -125.20 56.67
REMARK 500 PHE E 125 -61.86 -102.17
REMARK 500 TYR E 131 54.15 -142.28
REMARK 500 ASP E 150 89.01 -153.47
REMARK 500 THR E 230 -89.39 -129.63
REMARK 500 ASP E 248 9.18 57.03
REMARK 500 PRO F 29 64.39 -106.06
REMARK 500 LEU F 30 -147.24 -101.91
REMARK 500 GLN F 62 71.69 -112.29
REMARK 500 SER F 94 -126.98 65.39
REMARK 500 TYR F 131 56.32 -153.08
REMARK 500 ASP F 150 88.03 -160.98
REMARK 500 THR F 230 -93.38 -129.97
REMARK 500 ASP F 248 -0.70 59.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 VAL A 255 20.5 L L OUTSIDE RANGE
REMARK 500 PHE B 198 24.0 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH D1000 DISTANCE = 5.07 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 273
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 274
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 275
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 276
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 273
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 274
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 275
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 276
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 273
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT C 274
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 275
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 276
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 277
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 278
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT D 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 273
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 274
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 275
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 276
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT E 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 273
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT E 274
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 275
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 276
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 277
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT F 272
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT F 273
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT F 274
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 275
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 276
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 277
REMARK 800
REMARK 800 SITE_IDENTIFIER: DC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 278
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1VA4 RELATED DB: PDB
REMARK 900 PFE WITH MUTATION AT L29P
DBREF 3HI4 A 1 271 UNP P22862 ESTE_PSEFL 2 272
DBREF 3HI4 B 1 271 UNP P22862 ESTE_PSEFL 2 272
DBREF 3HI4 C 1 271 UNP P22862 ESTE_PSEFL 2 272
DBREF 3HI4 D 1 271 UNP P22862 ESTE_PSEFL 2 272
DBREF 3HI4 E 1 271 UNP P22862 ESTE_PSEFL 2 272
DBREF 3HI4 F 1 271 UNP P22862 ESTE_PSEFL 2 272
SEQADV 3HI4 PRO A 29 UNP P22862 LEU 30 ENGINEERED
SEQADV 3HI4 PRO B 29 UNP P22862 LEU 30 ENGINEERED
SEQADV 3HI4 PRO C 29 UNP P22862 LEU 30 ENGINEERED
SEQADV 3HI4 PRO D 29 UNP P22862 LEU 30 ENGINEERED
SEQADV 3HI4 PRO E 29 UNP P22862 LEU 30 ENGINEERED
SEQADV 3HI4 PRO F 29 UNP P22862 LEU 30 ENGINEERED
SEQRES 1 A 271 SER THR PHE VAL ALA LYS ASP GLY THR GLN ILE TYR PHE
SEQRES 2 A 271 LYS ASP TRP GLY SER GLY LYS PRO VAL LEU PHE SER HIS
SEQRES 3 A 271 GLY TRP PRO LEU ASP ALA ASP MET TRP GLU TYR GLN MET
SEQRES 4 A 271 GLU TYR LEU SER SER ARG GLY TYR ARG THR ILE ALA PHE
SEQRES 5 A 271 ASP ARG ARG GLY PHE GLY ARG SER ASP GLN PRO TRP THR
SEQRES 6 A 271 GLY ASN ASP TYR ASP THR PHE ALA ASP ASP ILE ALA GLN
SEQRES 7 A 271 LEU ILE GLU HIS LEU ASP LEU LYS GLU VAL THR LEU VAL
SEQRES 8 A 271 GLY PHE SER MET GLY GLY GLY ASP VAL ALA ARG TYR ILE
SEQRES 9 A 271 ALA ARG HIS GLY SER ALA ARG VAL ALA GLY LEU VAL LEU
SEQRES 10 A 271 LEU GLY ALA VAL THR PRO LEU PHE GLY GLN LYS PRO ASP
SEQRES 11 A 271 TYR PRO GLN GLY VAL PRO LEU ASP VAL PHE ALA ARG PHE
SEQRES 12 A 271 LYS THR GLU LEU LEU LYS ASP ARG ALA GLN PHE ILE SER
SEQRES 13 A 271 ASP PHE ASN ALA PRO PHE TYR GLY ILE ASN LYS GLY GLN
SEQRES 14 A 271 VAL VAL SER GLN GLY VAL GLN THR GLN THR LEU GLN ILE
SEQRES 15 A 271 ALA LEU LEU ALA SER LEU LYS ALA THR VAL ASP CYS VAL
SEQRES 16 A 271 THR ALA PHE ALA GLU THR ASP PHE ARG PRO ASP MET ALA
SEQRES 17 A 271 LYS ILE ASP VAL PRO THR LEU VAL ILE HIS GLY ASP GLY
SEQRES 18 A 271 ASP GLN ILE VAL PRO PHE GLU THR THR GLY LYS VAL ALA
SEQRES 19 A 271 ALA GLU LEU ILE LYS GLY ALA GLU LEU LYS VAL TYR LYS
SEQRES 20 A 271 ASP ALA PRO HIS GLY PHE ALA VAL THR HIS ALA GLN GLN
SEQRES 21 A 271 LEU ASN GLU ASP LEU LEU ALA PHE LEU LYS ARG
SEQRES 1 B 271 SER THR PHE VAL ALA LYS ASP GLY THR GLN ILE TYR PHE
SEQRES 2 B 271 LYS ASP TRP GLY SER GLY LYS PRO VAL LEU PHE SER HIS
SEQRES 3 B 271 GLY TRP PRO LEU ASP ALA ASP MET TRP GLU TYR GLN MET
SEQRES 4 B 271 GLU TYR LEU SER SER ARG GLY TYR ARG THR ILE ALA PHE
SEQRES 5 B 271 ASP ARG ARG GLY PHE GLY ARG SER ASP GLN PRO TRP THR
SEQRES 6 B 271 GLY ASN ASP TYR ASP THR PHE ALA ASP ASP ILE ALA GLN
SEQRES 7 B 271 LEU ILE GLU HIS LEU ASP LEU LYS GLU VAL THR LEU VAL
SEQRES 8 B 271 GLY PHE SER MET GLY GLY GLY ASP VAL ALA ARG TYR ILE
SEQRES 9 B 271 ALA ARG HIS GLY SER ALA ARG VAL ALA GLY LEU VAL LEU
SEQRES 10 B 271 LEU GLY ALA VAL THR PRO LEU PHE GLY GLN LYS PRO ASP
SEQRES 11 B 271 TYR PRO GLN GLY VAL PRO LEU ASP VAL PHE ALA ARG PHE
SEQRES 12 B 271 LYS THR GLU LEU LEU LYS ASP ARG ALA GLN PHE ILE SER
SEQRES 13 B 271 ASP PHE ASN ALA PRO PHE TYR GLY ILE ASN LYS GLY GLN
SEQRES 14 B 271 VAL VAL SER GLN GLY VAL GLN THR GLN THR LEU GLN ILE
SEQRES 15 B 271 ALA LEU LEU ALA SER LEU LYS ALA THR VAL ASP CYS VAL
SEQRES 16 B 271 THR ALA PHE ALA GLU THR ASP PHE ARG PRO ASP MET ALA
SEQRES 17 B 271 LYS ILE ASP VAL PRO THR LEU VAL ILE HIS GLY ASP GLY
SEQRES 18 B 271 ASP GLN ILE VAL PRO PHE GLU THR THR GLY LYS VAL ALA
SEQRES 19 B 271 ALA GLU LEU ILE LYS GLY ALA GLU LEU LYS VAL TYR LYS
SEQRES 20 B 271 ASP ALA PRO HIS GLY PHE ALA VAL THR HIS ALA GLN GLN
SEQRES 21 B 271 LEU ASN GLU ASP LEU LEU ALA PHE LEU LYS ARG
SEQRES 1 C 271 SER THR PHE VAL ALA LYS ASP GLY THR GLN ILE TYR PHE
SEQRES 2 C 271 LYS ASP TRP GLY SER GLY LYS PRO VAL LEU PHE SER HIS
SEQRES 3 C 271 GLY TRP PRO LEU ASP ALA ASP MET TRP GLU TYR GLN MET
SEQRES 4 C 271 GLU TYR LEU SER SER ARG GLY TYR ARG THR ILE ALA PHE
SEQRES 5 C 271 ASP ARG ARG GLY PHE GLY ARG SER ASP GLN PRO TRP THR
SEQRES 6 C 271 GLY ASN ASP TYR ASP THR PHE ALA ASP ASP ILE ALA GLN
SEQRES 7 C 271 LEU ILE GLU HIS LEU ASP LEU LYS GLU VAL THR LEU VAL
SEQRES 8 C 271 GLY PHE SER MET GLY GLY GLY ASP VAL ALA ARG TYR ILE
SEQRES 9 C 271 ALA ARG HIS GLY SER ALA ARG VAL ALA GLY LEU VAL LEU
SEQRES 10 C 271 LEU GLY ALA VAL THR PRO LEU PHE GLY GLN LYS PRO ASP
SEQRES 11 C 271 TYR PRO GLN GLY VAL PRO LEU ASP VAL PHE ALA ARG PHE
SEQRES 12 C 271 LYS THR GLU LEU LEU LYS ASP ARG ALA GLN PHE ILE SER
SEQRES 13 C 271 ASP PHE ASN ALA PRO PHE TYR GLY ILE ASN LYS GLY GLN
SEQRES 14 C 271 VAL VAL SER GLN GLY VAL GLN THR GLN THR LEU GLN ILE
SEQRES 15 C 271 ALA LEU LEU ALA SER LEU LYS ALA THR VAL ASP CYS VAL
SEQRES 16 C 271 THR ALA PHE ALA GLU THR ASP PHE ARG PRO ASP MET ALA
SEQRES 17 C 271 LYS ILE ASP VAL PRO THR LEU VAL ILE HIS GLY ASP GLY
SEQRES 18 C 271 ASP GLN ILE VAL PRO PHE GLU THR THR GLY LYS VAL ALA
SEQRES 19 C 271 ALA GLU LEU ILE LYS GLY ALA GLU LEU LYS VAL TYR LYS
SEQRES 20 C 271 ASP ALA PRO HIS GLY PHE ALA VAL THR HIS ALA GLN GLN
SEQRES 21 C 271 LEU ASN GLU ASP LEU LEU ALA PHE LEU LYS ARG
SEQRES 1 D 271 SER THR PHE VAL ALA LYS ASP GLY THR GLN ILE TYR PHE
SEQRES 2 D 271 LYS ASP TRP GLY SER GLY LYS PRO VAL LEU PHE SER HIS
SEQRES 3 D 271 GLY TRP PRO LEU ASP ALA ASP MET TRP GLU TYR GLN MET
SEQRES 4 D 271 GLU TYR LEU SER SER ARG GLY TYR ARG THR ILE ALA PHE
SEQRES 5 D 271 ASP ARG ARG GLY PHE GLY ARG SER ASP GLN PRO TRP THR
SEQRES 6 D 271 GLY ASN ASP TYR ASP THR PHE ALA ASP ASP ILE ALA GLN
SEQRES 7 D 271 LEU ILE GLU HIS LEU ASP LEU LYS GLU VAL THR LEU VAL
SEQRES 8 D 271 GLY PHE SER MET GLY GLY GLY ASP VAL ALA ARG TYR ILE
SEQRES 9 D 271 ALA ARG HIS GLY SER ALA ARG VAL ALA GLY LEU VAL LEU
SEQRES 10 D 271 LEU GLY ALA VAL THR PRO LEU PHE GLY GLN LYS PRO ASP
SEQRES 11 D 271 TYR PRO GLN GLY VAL PRO LEU ASP VAL PHE ALA ARG PHE
SEQRES 12 D 271 LYS THR GLU LEU LEU LYS ASP ARG ALA GLN PHE ILE SER
SEQRES 13 D 271 ASP PHE ASN ALA PRO PHE TYR GLY ILE ASN LYS GLY GLN
SEQRES 14 D 271 VAL VAL SER GLN GLY VAL GLN THR GLN THR LEU GLN ILE
SEQRES 15 D 271 ALA LEU LEU ALA SER LEU LYS ALA THR VAL ASP CYS VAL
SEQRES 16 D 271 THR ALA PHE ALA GLU THR ASP PHE ARG PRO ASP MET ALA
SEQRES 17 D 271 LYS ILE ASP VAL PRO THR LEU VAL ILE HIS GLY ASP GLY
SEQRES 18 D 271 ASP GLN ILE VAL PRO PHE GLU THR THR GLY LYS VAL ALA
SEQRES 19 D 271 ALA GLU LEU ILE LYS GLY ALA GLU LEU LYS VAL TYR LYS
SEQRES 20 D 271 ASP ALA PRO HIS GLY PHE ALA VAL THR HIS ALA GLN GLN
SEQRES 21 D 271 LEU ASN GLU ASP LEU LEU ALA PHE LEU LYS ARG
SEQRES 1 E 271 SER THR PHE VAL ALA LYS ASP GLY THR GLN ILE TYR PHE
SEQRES 2 E 271 LYS ASP TRP GLY SER GLY LYS PRO VAL LEU PHE SER HIS
SEQRES 3 E 271 GLY TRP PRO LEU ASP ALA ASP MET TRP GLU TYR GLN MET
SEQRES 4 E 271 GLU TYR LEU SER SER ARG GLY TYR ARG THR ILE ALA PHE
SEQRES 5 E 271 ASP ARG ARG GLY PHE GLY ARG SER ASP GLN PRO TRP THR
SEQRES 6 E 271 GLY ASN ASP TYR ASP THR PHE ALA ASP ASP ILE ALA GLN
SEQRES 7 E 271 LEU ILE GLU HIS LEU ASP LEU LYS GLU VAL THR LEU VAL
SEQRES 8 E 271 GLY PHE SER MET GLY GLY GLY ASP VAL ALA ARG TYR ILE
SEQRES 9 E 271 ALA ARG HIS GLY SER ALA ARG VAL ALA GLY LEU VAL LEU
SEQRES 10 E 271 LEU GLY ALA VAL THR PRO LEU PHE GLY GLN LYS PRO ASP
SEQRES 11 E 271 TYR PRO GLN GLY VAL PRO LEU ASP VAL PHE ALA ARG PHE
SEQRES 12 E 271 LYS THR GLU LEU LEU LYS ASP ARG ALA GLN PHE ILE SER
SEQRES 13 E 271 ASP PHE ASN ALA PRO PHE TYR GLY ILE ASN LYS GLY GLN
SEQRES 14 E 271 VAL VAL SER GLN GLY VAL GLN THR GLN THR LEU GLN ILE
SEQRES 15 E 271 ALA LEU LEU ALA SER LEU LYS ALA THR VAL ASP CYS VAL
SEQRES 16 E 271 THR ALA PHE ALA GLU THR ASP PHE ARG PRO ASP MET ALA
SEQRES 17 E 271 LYS ILE ASP VAL PRO THR LEU VAL ILE HIS GLY ASP GLY
SEQRES 18 E 271 ASP GLN ILE VAL PRO PHE GLU THR THR GLY LYS VAL ALA
SEQRES 19 E 271 ALA GLU LEU ILE LYS GLY ALA GLU LEU LYS VAL TYR LYS
SEQRES 20 E 271 ASP ALA PRO HIS GLY PHE ALA VAL THR HIS ALA GLN GLN
SEQRES 21 E 271 LEU ASN GLU ASP LEU LEU ALA PHE LEU LYS ARG
SEQRES 1 F 271 SER THR PHE VAL ALA LYS ASP GLY THR GLN ILE TYR PHE
SEQRES 2 F 271 LYS ASP TRP GLY SER GLY LYS PRO VAL LEU PHE SER HIS
SEQRES 3 F 271 GLY TRP PRO LEU ASP ALA ASP MET TRP GLU TYR GLN MET
SEQRES 4 F 271 GLU TYR LEU SER SER ARG GLY TYR ARG THR ILE ALA PHE
SEQRES 5 F 271 ASP ARG ARG GLY PHE GLY ARG SER ASP GLN PRO TRP THR
SEQRES 6 F 271 GLY ASN ASP TYR ASP THR PHE ALA ASP ASP ILE ALA GLN
SEQRES 7 F 271 LEU ILE GLU HIS LEU ASP LEU LYS GLU VAL THR LEU VAL
SEQRES 8 F 271 GLY PHE SER MET GLY GLY GLY ASP VAL ALA ARG TYR ILE
SEQRES 9 F 271 ALA ARG HIS GLY SER ALA ARG VAL ALA GLY LEU VAL LEU
SEQRES 10 F 271 LEU GLY ALA VAL THR PRO LEU PHE GLY GLN LYS PRO ASP
SEQRES 11 F 271 TYR PRO GLN GLY VAL PRO LEU ASP VAL PHE ALA ARG PHE
SEQRES 12 F 271 LYS THR GLU LEU LEU LYS ASP ARG ALA GLN PHE ILE SER
SEQRES 13 F 271 ASP PHE ASN ALA PRO PHE TYR GLY ILE ASN LYS GLY GLN
SEQRES 14 F 271 VAL VAL SER GLN GLY VAL GLN THR GLN THR LEU GLN ILE
SEQRES 15 F 271 ALA LEU LEU ALA SER LEU LYS ALA THR VAL ASP CYS VAL
SEQRES 16 F 271 THR ALA PHE ALA GLU THR ASP PHE ARG PRO ASP MET ALA
SEQRES 17 F 271 LYS ILE ASP VAL PRO THR LEU VAL ILE HIS GLY ASP GLY
SEQRES 18 F 271 ASP GLN ILE VAL PRO PHE GLU THR THR GLY LYS VAL ALA
SEQRES 19 F 271 ALA GLU LEU ILE LYS GLY ALA GLU LEU LYS VAL TYR LYS
SEQRES 20 F 271 ASP ALA PRO HIS GLY PHE ALA VAL THR HIS ALA GLN GLN
SEQRES 21 F 271 LEU ASN GLU ASP LEU LEU ALA PHE LEU LYS ARG
HET ACT A 272 4
HET SO4 A 273 5
HET GOL A 274 6
HET GOL A 275 6
HET GOL A 276 6
HET ACT B 272 4
HET SO4 B 273 5
HET GOL B 274 6
HET GOL B 275 6
HET GOL B 276 6
HET ACT C 272 4
HET SO4 C 273 5
HET ACT C 274 4
HET GOL C 275 6
HET GOL C 276 6
HET GOL C 277 6
HET GOL C 278 6
HET ACT D 272 4
HET SO4 D 273 5
HET GOL D 274 6
HET GOL D 275 6
HET GOL D 276 6
HET ACT E 272 4
HET SO4 E 273 5
HET ACT E 274 4
HET GOL E 275 6
HET GOL E 276 6
HET GOL E 277 6
HET ACT F 272 4
HET ACT F 273 4
HET ACT F 274 4
HET GOL F 275 6
HET GOL F 276 6
HET GOL F 277 6
HET GOL F 278 6
HETNAM ACT ACETATE ION
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
FORMUL 7 ACT 10(C2 H3 O2 1-)
FORMUL 8 SO4 5(O4 S 2-)
FORMUL 9 GOL 20(C3 H8 O3)
FORMUL 42 HOH *1036(H2 O)
HELIX 1 1 ASP A 31 MET A 34 5 4
HELIX 2 2 TRP A 35 SER A 44 1 10
HELIX 3 3 ASP A 68 ASP A 84 1 17
HELIX 4 4 MET A 95 GLY A 108 1 14
HELIX 5 5 PRO A 136 GLY A 164 1 29
HELIX 6 6 ILE A 165 GLY A 168 5 4
HELIX 7 7 SER A 172 ALA A 186 1 15
HELIX 8 8 SER A 187 THR A 201 1 15
HELIX 9 9 PHE A 203 ILE A 210 1 8
HELIX 10 10 PRO A 226 THR A 229 5 4
HELIX 11 11 THR A 230 ILE A 238 1 9
HELIX 12 12 GLY A 252 HIS A 257 1 6
HELIX 13 13 HIS A 257 ARG A 271 1 15
HELIX 14 14 ASP B 31 MET B 34 5 4
HELIX 15 15 TRP B 35 SER B 44 1 10
HELIX 16 16 ASP B 68 ASP B 84 1 17
HELIX 17 17 MET B 95 GLY B 108 1 14
HELIX 18 18 PRO B 136 GLY B 164 1 29
HELIX 19 19 ILE B 165 GLY B 168 5 4
HELIX 20 20 SER B 172 ALA B 186 1 15
HELIX 21 21 SER B 187 THR B 201 1 15
HELIX 22 22 PHE B 203 ILE B 210 1 8
HELIX 23 23 PRO B 226 THR B 229 5 4
HELIX 24 24 THR B 230 ILE B 238 1 9
HELIX 25 25 GLY B 252 HIS B 257 1 6
HELIX 26 26 HIS B 257 ARG B 271 1 15
HELIX 27 27 ASP C 31 MET C 34 5 4
HELIX 28 28 TRP C 35 SER C 44 1 10
HELIX 29 29 ASP C 68 ASP C 84 1 17
HELIX 30 30 MET C 95 GLY C 108 1 14
HELIX 31 31 PRO C 136 GLY C 164 1 29
HELIX 32 32 ILE C 165 GLY C 168 5 4
HELIX 33 33 SER C 172 ALA C 186 1 15
HELIX 34 34 SER C 187 THR C 201 1 15
HELIX 35 35 PHE C 203 ILE C 210 1 8
HELIX 36 36 PRO C 226 THR C 229 5 4
HELIX 37 37 THR C 230 ILE C 238 1 9
HELIX 38 38 GLY C 252 HIS C 257 1 6
HELIX 39 39 HIS C 257 LYS C 270 1 14
HELIX 40 40 ASP D 31 MET D 34 5 4
HELIX 41 41 TRP D 35 SER D 44 1 10
HELIX 42 42 ASP D 68 LEU D 83 1 16
HELIX 43 43 MET D 95 GLY D 108 1 14
HELIX 44 44 PRO D 136 TYR D 163 1 28
HELIX 45 45 GLY D 164 GLY D 168 5 5
HELIX 46 46 SER D 172 LEU D 185 1 14
HELIX 47 47 SER D 187 THR D 201 1 15
HELIX 48 48 PHE D 203 ILE D 210 1 8
HELIX 49 49 PRO D 226 THR D 229 5 4
HELIX 50 50 THR D 230 ILE D 238 1 9
HELIX 51 51 GLY D 252 HIS D 257 1 6
HELIX 52 52 HIS D 257 ARG D 271 1 15
HELIX 53 53 ASP E 31 MET E 34 5 4
HELIX 54 54 TRP E 35 SER E 44 1 10
HELIX 55 55 ASP E 68 LEU E 83 1 16
HELIX 56 56 MET E 95 GLY E 108 1 14
HELIX 57 57 PRO E 136 GLY E 164 1 29
HELIX 58 58 ILE E 165 GLY E 168 5 4
HELIX 59 59 SER E 172 ALA E 186 1 15
HELIX 60 60 SER E 187 THR E 201 1 15
HELIX 61 61 PHE E 203 LYS E 209 1 7
HELIX 62 62 PRO E 226 THR E 229 5 4
HELIX 63 63 THR E 230 ILE E 238 1 9
HELIX 64 64 GLY E 252 HIS E 257 1 6
HELIX 65 65 HIS E 257 ARG E 271 1 15
HELIX 66 66 ASP F 31 MET F 34 5 4
HELIX 67 67 TRP F 35 SER F 44 1 10
HELIX 68 68 ASP F 68 ASP F 84 1 17
HELIX 69 69 MET F 95 GLY F 108 1 14
HELIX 70 70 PRO F 136 TYR F 163 1 28
HELIX 71 71 GLY F 164 GLY F 168 5 5
HELIX 72 72 SER F 172 ALA F 186 1 15
HELIX 73 73 SER F 187 THR F 201 1 15
HELIX 74 74 PHE F 203 ALA F 208 1 6
HELIX 75 75 PRO F 226 THR F 229 5 4
HELIX 76 76 THR F 230 ILE F 238 1 9
HELIX 77 77 GLY F 252 HIS F 257 1 6
HELIX 78 78 HIS F 257 LYS F 270 1 14
SHEET 1 A 8 THR A 2 VAL A 4 0
SHEET 2 A 8 GLN A 10 TRP A 16 -1 O ILE A 11 N PHE A 3
SHEET 3 A 8 TYR A 47 PHE A 52 -1 O THR A 49 N TRP A 16
SHEET 4 A 8 LYS A 20 SER A 25 1 N PHE A 24 O ILE A 50
SHEET 5 A 8 VAL A 88 PHE A 93 1 O THR A 89 N LEU A 23
SHEET 6 A 8 VAL A 112 LEU A 118 1 O LEU A 118 N GLY A 92
SHEET 7 A 8 THR A 214 GLY A 219 1 O ILE A 217 N LEU A 117
SHEET 8 A 8 GLU A 242 TYR A 246 1 O GLU A 242 N VAL A 216
SHEET 1 B 8 THR B 2 VAL B 4 0
SHEET 2 B 8 GLN B 10 TRP B 16 -1 O ILE B 11 N PHE B 3
SHEET 3 B 8 ARG B 48 PHE B 52 -1 O THR B 49 N TRP B 16
SHEET 4 B 8 PRO B 21 SER B 25 1 N PHE B 24 O ILE B 50
SHEET 5 B 8 VAL B 88 PHE B 93 1 O VAL B 91 N LEU B 23
SHEET 6 B 8 VAL B 112 LEU B 118 1 O VAL B 116 N LEU B 90
SHEET 7 B 8 THR B 214 GLY B 219 1 O ILE B 217 N LEU B 117
SHEET 8 B 8 GLU B 242 TYR B 246 1 O LYS B 244 N VAL B 216
SHEET 1 C 8 THR C 2 VAL C 4 0
SHEET 2 C 8 GLN C 10 TRP C 16 -1 O ILE C 11 N PHE C 3
SHEET 3 C 8 TYR C 47 PHE C 52 -1 O THR C 49 N TRP C 16
SHEET 4 C 8 LYS C 20 SER C 25 1 N PHE C 24 O ILE C 50
SHEET 5 C 8 VAL C 88 PHE C 93 1 O VAL C 91 N SER C 25
SHEET 6 C 8 VAL C 112 LEU C 118 1 O LEU C 118 N GLY C 92
SHEET 7 C 8 THR C 214 GLY C 219 1 O ILE C 217 N LEU C 117
SHEET 8 C 8 GLU C 242 TYR C 246 1 O GLU C 242 N VAL C 216
SHEET 1 D 8 THR D 2 VAL D 4 0
SHEET 2 D 8 GLN D 10 TRP D 16 -1 O ILE D 11 N PHE D 3
SHEET 3 D 8 TYR D 47 PHE D 52 -1 O THR D 49 N TRP D 16
SHEET 4 D 8 LYS D 20 SER D 25 1 N PHE D 24 O ILE D 50
SHEET 5 D 8 VAL D 88 PHE D 93 1 O VAL D 91 N SER D 25
SHEET 6 D 8 VAL D 112 LEU D 118 1 O LEU D 118 N GLY D 92
SHEET 7 D 8 THR D 214 GLY D 219 1 O ILE D 217 N LEU D 117
SHEET 8 D 8 GLU D 242 TYR D 246 1 O GLU D 242 N VAL D 216
SHEET 1 E 8 THR E 2 VAL E 4 0
SHEET 2 E 8 GLN E 10 TRP E 16 -1 O ILE E 11 N PHE E 3
SHEET 3 E 8 ARG E 48 PHE E 52 -1 O THR E 49 N TRP E 16
SHEET 4 E 8 PRO E 21 SER E 25 1 N PHE E 24 O ILE E 50
SHEET 5 E 8 VAL E 88 PHE E 93 1 O VAL E 91 N SER E 25
SHEET 6 E 8 VAL E 112 LEU E 118 1 O LEU E 118 N GLY E 92
SHEET 7 E 8 THR E 214 GLY E 219 1 O LEU E 215 N LEU E 117
SHEET 8 E 8 GLU E 242 TYR E 246 1 O LYS E 244 N VAL E 216
SHEET 1 F 8 THR F 2 VAL F 4 0
SHEET 2 F 8 GLN F 10 GLY F 17 -1 O ILE F 11 N PHE F 3
SHEET 3 F 8 TYR F 47 PHE F 52 -1 O THR F 49 N TRP F 16
SHEET 4 F 8 LYS F 20 SER F 25 1 N PHE F 24 O ILE F 50
SHEET 5 F 8 VAL F 88 PHE F 93 1 O VAL F 91 N SER F 25
SHEET 6 F 8 VAL F 112 LEU F 118 1 O LEU F 118 N GLY F 92
SHEET 7 F 8 THR F 214 GLY F 219 1 O LEU F 215 N LEU F 117
SHEET 8 F 8 GLU F 242 TYR F 246 1 O GLU F 242 N THR F 214
CISPEP 1 TRP A 28 PRO A 29 0 -9.42
CISPEP 2 THR A 122 PRO A 123 0 6.96
CISPEP 3 TRP B 28 PRO B 29 0 -17.73
CISPEP 4 THR B 122 PRO B 123 0 3.03
CISPEP 5 TRP C 28 PRO C 29 0 -10.93
CISPEP 6 THR C 122 PRO C 123 0 6.27
CISPEP 7 TRP D 28 PRO D 29 0 -7.41
CISPEP 8 THR D 122 PRO D 123 0 8.80
CISPEP 9 TRP E 28 PRO E 29 0 -8.39
CISPEP 10 THR E 122 PRO E 123 0 4.91
CISPEP 11 TRP F 28 PRO F 29 0 -8.42
CISPEP 12 THR F 122 PRO F 123 0 8.68
SITE 1 AC1 5 TRP A 28 SER A 94 MET A 95 VAL A 121
SITE 2 AC1 5 HOH A 278
SITE 1 AC2 1 ARG A 106
SITE 1 AC3 8 SER A 1 TYR A 12 PHE A 13 LYS A 14
SITE 2 AC3 8 ASP A 15 ASP C 61 GLN C 62 HOH C 659
SITE 1 AC4 5 LEU A 137 ALA A 141 LYS A 144 GLU A 200
SITE 2 AC4 5 HOH A 289
SITE 1 AC5 6 LEU A 30 TYR A 163 VAL A 175 GLN A 178
SITE 2 AC5 6 THR A 179 HOH A 311
SITE 1 AC6 6 TRP B 28 SER B 94 MET B 95 VAL B 121
SITE 2 AC6 6 PHE B 198 HOH B 277
SITE 1 AC7 2 ARG B 106 HOH B 602
SITE 1 AC8 6 LEU B 137 LYS B 144 THR B 196 GLU B 200
SITE 2 AC8 6 HOH B 535 HOH B 548
SITE 1 AC9 6 ASP A 61 GLN A 62 SER B 1 TYR B 12
SITE 2 AC9 6 LYS B 14 ASP B 15
SITE 1 BC1 5 TYR B 163 GLN B 178 THR B 179 ILE B 182
SITE 2 BC1 5 HOH B 291
SITE 1 BC2 5 TRP C 28 SER C 94 MET C 95 VAL C 121
SITE 2 BC2 5 HOH C 279
SITE 1 BC3 1 ARG C 106
SITE 1 BC4 1 ILE C 224
SITE 1 BC5 8 ASP B 61 GLN B 62 SER C 1 TYR C 12
SITE 2 BC5 8 PHE C 13 LYS C 14 ASP C 15 HOH C 913
SITE 1 BC6 4 LEU C 137 LYS C 144 GLU C 200 HOH C 752
SITE 1 BC7 5 LEU C 30 TYR C 163 GLN C 178 THR C 179
SITE 2 BC7 5 ILE C 182
SITE 1 BC8 2 ASN A 166 GLY C 19
SITE 1 BC9 6 TRP D 28 SER D 94 MET D 95 VAL D 121
SITE 2 BC9 6 PHE D 198 HOH D 277
SITE 1 CC1 1 ARG D 106
SITE 1 CC2 5 LEU D 137 ALA D 141 LYS D 144 THR D 196
SITE 2 CC2 5 GLU D 200
SITE 1 CC3 6 SER D 1 TYR D 12 LYS D 14 ASP D 15
SITE 2 CC3 6 ASP E 61 GLN E 62
SITE 1 CC4 7 TYR D 163 VAL D 175 GLN D 178 THR D 179
SITE 2 CC4 7 ILE D 182 HOH D 293 HOH D 419
SITE 1 CC5 5 TRP E 28 SER E 94 MET E 95 VAL E 121
SITE 2 CC5 5 HOH E 278
SITE 1 CC6 1 ARG E 106
SITE 1 CC7 1 ILE E 224
SITE 1 CC8 5 SER E 1 TYR E 12 ASP E 15 ASP F 61
SITE 2 CC8 5 GLN F 62
SITE 1 CC9 6 LEU E 137 ALA E 141 LYS E 144 THR E 196
SITE 2 CC9 6 GLU E 200 HOH E 284
SITE 1 DC1 6 TYR E 163 GLN E 178 THR E 179 ILE E 182
SITE 2 DC1 6 HOH E 332 HOH E 481
SITE 1 DC2 6 TRP F 28 SER F 94 MET F 95 VAL F 121
SITE 2 DC2 6 PHE F 198 HOH F 279
SITE 1 DC3 4 VAL F 245 LYS F 247 GLN F 260 HOH F 590
SITE 1 DC4 2 GLN F 223 ILE F 224
SITE 1 DC5 8 ASP D 61 GLN D 62 SER F 1 TYR F 12
SITE 2 DC5 8 PHE F 13 LYS F 14 ASP F 15 HOH F 294
SITE 1 DC6 5 LEU F 137 ALA F 141 LYS F 144 THR F 196
SITE 2 DC6 5 GLU F 200
SITE 1 DC7 5 SER F 156 ASN F 159 GLN F 176 HOH F 418
SITE 2 DC7 5 HOH F1034
SITE 1 DC8 5 TYR F 163 GLN F 178 ILE F 182 HOH F 330
SITE 2 DC8 5 HOH F 982
CRYST1 145.490 145.490 129.990 90.00 90.00 120.00 P 32 18
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 0.006873 0.003968 0.000000 0.00000
SCALE2 0.000000 0.007937 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007693 0.00000
TER 2133 ARG A 271
TER 4266 ARG B 271
TER 6404 ARG C 271
TER 8537 ARG D 271
TER 10675 ARG E 271
TER 12808 ARG F 271
MASTER 506 0 35 78 48 0 59 614023 6 185 126
END |