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HEADER HYDROLASE 17-SEP-09 2WTM
TITLE EST1E FROM BUTYRIVIBRIO PROTEOCLASTICUS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EST1E;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: CLOSTRIDIUM PROTEOCLASTICUM;
SOURCE 3 ORGANISM_TAXID: 43305;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS ESTERASE, HYDROLASE, FERULIC ACID ESTERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.C.GOLDSTONE,V.L.ARCUS
REVDAT 1 19-JAN-10 2WTM 0
JRNL AUTH D.C.GOLDSTONE,S.G.VILLAS-BOAS,M.TILL,W.J.KELLY,
JRNL AUTH 2 G.T.ATTWOOD,V.L.ARCUS
JRNL TITL STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF A
JRNL TITL 2 PROMISCUOUS FERULOYL ESTERASE (EST1E) FROM THE
JRNL TITL 3 RUMEN BACTERIUM BUTYRIVIBRIO PROTEOCLASTICUS.
JRNL REF PROTEINS 2009
JRNL REFN ESSN 1097-0134
JRNL PMID 20058325
JRNL DOI 10.1002/PROT.22662
REMARK 2
REMARK 2 RESOLUTION. 1.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 89.44
REMARK 3 DATA CUTOFF (SIGMA(F)) : NONE
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.42
REMARK 3 NUMBER OF REFLECTIONS : 124101
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) : 0.15793
REMARK 3 R VALUE (WORKING SET) : 0.15604
REMARK 3 FREE R VALUE : 0.19410
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.0
REMARK 3 FREE R VALUE TEST SET COUNT : 6580
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.600
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.642
REMARK 3 REFLECTION IN BIN (WORKING SET) : 9181
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.63
REMARK 3 BIN R VALUE (WORKING SET) : 0.206
REMARK 3 BIN FREE R VALUE SET COUNT : 508
REMARK 3 BIN FREE R VALUE : 0.257
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7757
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 66
REMARK 3 SOLVENT ATOMS : 886
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 16.4
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 15.150
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.57
REMARK 3 B22 (A**2) : -0.32
REMARK 3 B33 (A**2) : -0.60
REMARK 3 B12 (A**2) : 0.00
REMARK 3 B13 (A**2) : -0.82
REMARK 3 B23 (A**2) : 0.00
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.079
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.084
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.054
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.506
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.971
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.954
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7992 ; 0.022 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 7263 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10866 ; 1.905 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16941 ; 0.957 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1011 ; 6.157 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 355 ;33.258 ;25.099
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1354 ;12.210 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 27 ;16.571 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1227 ; 0.127 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8854 ; 0.010 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1501 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1670 ; 0.236 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 7624 ; 0.185 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3973 ; 0.184 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 4619 ; 0.088 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 689 ; 0.199 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 32 ; 0.195 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 91 ; 0.225 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 36 ; 0.264 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 6341 ; 1.647 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2017 ; 0.390 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 8004 ; 1.920 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3496 ; 3.333 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 2847 ; 4.569 ; 4.500
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS.
REMARK 4
REMARK 4 2WTM COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-SEP-09.
REMARK 100 THE PDBE ID CODE IS EBI-41175.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : NULL
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 124101
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.60
REMARK 200 RESOLUTION RANGE LOW (A) : 50.00
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.0
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 200 DATA REDUNDANCY : 2.8
REMARK 200 R MERGE (I) : 0.08
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 13.70
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) : 1.65
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 2.8
REMARK 200 R MERGE FOR SHELL (I) : 0.35
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 4.80
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 40.54
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y+1/2,-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 54.53350
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3910 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18450 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.97 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
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: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3930 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 18280 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.62 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D
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 SER A -2
REMARK 465 HIS B 64
REMARK 465 GLY B 65
REMARK 465 LYS B 66
REMARK 465 SER B 67
REMARK 465 ASP B 68
REMARK 465 GLY B 69
REMARK 465 LYS B 70
REMARK 465 PHE B 71
REMARK 465 GLU B 72
REMARK 465 LYS C 248
REMARK 465 GLY D 65
REMARK 465 LYS D 66
REMARK 465 SER D 67
REMARK 465 ASP D 68
REMARK 465 GLY D 69
REMARK 465 LYS D 70
REMARK 465 PHE D 71
REMARK 465 GLU D 72
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 LYS A 18 CG CD CE NZ
REMARK 470 ASN A 20 CG OD1 ND2
REMARK 470 GLU A 22 CD OE1 OE2
REMARK 470 LYS A 70 NZ
REMARK 470 LYS A 248 CG CD CE NZ
REMARK 470 LYS B 18 CG CD CE NZ
REMARK 470 ARG B 163 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 164 CG CD CE NZ
REMARK 470 LYS B 213 CE NZ
REMARK 470 LYS C 9 NZ
REMARK 470 LYS C 18 CG CD CE NZ
REMARK 470 GLU C 22 CG CD OE1 OE2
REMARK 470 LYS C 216 NZ
REMARK 470 LYS D 9 CD CE NZ
REMARK 470 LYS D 18 CG CD CE NZ
REMARK 470 ASN D 19 CG OD1 ND2
REMARK 470 ASN D 20 CG OD1 ND2
REMARK 470 GLU D 22 CG CD OE1 OE2
REMARK 470 HIS D 64 CG ND1 CD2 CE1 NE2
REMARK 470 ASP D 94 CG OD1 OD2
REMARK 470 LYS D 164 CE NZ
REMARK 470 LYS D 184 CE NZ
REMARK 470 GLU D 198 CD OE1 OE2
REMARK 470 LYS D 248 CG CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O ARG A 119 O HOH A 2111 1.97
REMARK 500 OE1 GLU A 203 O HOH A 2183 2.13
REMARK 500 OE1 GLU B 47 O HOH B 2044 2.20
REMARK 500 OE1 GLU C 47 O HOH C 2059 2.05
REMARK 500 N ASP D 73 O HOH D 2054 1.78
REMARK 500 OE1 GLU D 151 O HOH D 2117 2.06
REMARK 500 O1 GOL A 1250 O HOH A 2215 2.15
REMARK 500 O HOH A 2007 O HOH A 2016 2.17
REMARK 500 O HOH B 2009 O HOH A 2038 2.06
REMARK 500 O HOH B 2063 O HOH A 2096 2.20
REMARK 500 O HOH B 2169 O HOH B 2170 2.12
REMARK 500 O HOH B 2212 O HOH B 2213 2.13
REMARK 500 O HOH C 2043 O HOH C 2122 1.97
REMARK 500 O HOH C 2081 O HOH C 2087 2.19
REMARK 500 O HOH C 2092 O HOH C 2095 2.16
REMARK 500 O HOH C 2163 O HOH C 2166 2.07
REMARK 500 O HOH D 2023 O HOH D 2189 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 2091 O HOH C 2212 1457 2.13
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 CYS B 215 CB CYS B 215 SG -0.099
REMARK 500 GLU C 198 CB GLU C 198 CG 0.118
REMARK 500 GLU D 203 CG GLU D 203 CD 0.092
REMARK 500 CYS D 215 CB CYS D 215 SG -0.102
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 PRO A 21 C - N - CD ANGL. DEV. = -14.1 DEGREES
REMARK 500 ASP A 195 CB - CG - OD2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG B 40 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG B 40 NE - CZ - NH2 ANGL. DEV. = -4.2 DEGREES
REMARK 500 ASP B 180 CB - CG - OD2 ANGL. DEV. = -7.4 DEGREES
REMARK 500 PHE C 77 CB - CG - CD1 ANGL. DEV. = 4.7 DEGREES
REMARK 500 PHE C 77 CB - CG - CD2 ANGL. DEV. = -5.5 DEGREES
REMARK 500 PRO C 127 C - N - CD ANGL. DEV. = -13.9 DEGREES
REMARK 500 PRO D 127 C - N - CD ANGL. DEV. = -13.3 DEGREES
REMARK 500 ARG D 139 NE - CZ - NH2 ANGL. DEV. = -4.8 DEGREES
REMARK 500 ASP D 155 CB - CG - OD1 ANGL. DEV. = 6.1 DEGREES
REMARK 500 ARG D 177 NE - CZ - NH1 ANGL. DEV. = 3.7 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 ASP A 6 -123.84 46.59
REMARK 500 THR A 34 -5.59 75.82
REMARK 500 THR A 97 -92.25 -91.41
REMARK 500 SER A 105 -117.67 59.36
REMARK 500 ALA A 159 -169.38 -166.98
REMARK 500 TRP A 160 62.64 60.68
REMARK 500 HIS A 230 50.41 -140.99
REMARK 500 THR B 97 -86.01 -95.14
REMARK 500 SER B 105 -117.04 62.25
REMARK 500 LEU B 143 114.72 -161.33
REMARK 500 LEU B 144 -119.44 47.52
REMARK 500 TRP B 160 129.54 -36.41
REMARK 500 THR C 34 -6.77 73.17
REMARK 500 THR C 97 -89.99 -95.77
REMARK 500 SER C 105 -117.11 62.40
REMARK 500 ALA C 159 -168.39 -168.33
REMARK 500 HIS C 230 50.63 -147.30
REMARK 500 ASN D 19 -11.68 103.62
REMARK 500 THR D 97 -90.81 -97.85
REMARK 500 SER D 105 -117.08 60.54
REMARK 500 HIS D 230 50.43 -140.80
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 111 24.5 L L OUTSIDE RANGE
REMARK 500 SER C -2 23.1 L L OUTSIDE RANGE
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D1249
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B1249
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 D1250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C1248
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B1250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A1249
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1250
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C1249
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D1251
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1251
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D1252
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B1252
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2WTN RELATED DB: PDB
REMARK 900 FERULIC ACID BOUND TO EST1E FROM
REMARK 900 BUTYRIVIBRIO PROTEOCLASTICUS
DBREF 2WTM A -2 248 PDB 2WTM 2WTM -2 248
DBREF 2WTM B -2 248 PDB 2WTM 2WTM -2 248
DBREF 2WTM C -2 248 PDB 2WTM 2WTM -2 248
DBREF 2WTM D -2 248 PDB 2WTM 2WTM -2 248
SEQRES 1 A 251 SER GLY ALA MET TYR ILE ASP CYS ASP GLY ILE LYS LEU
SEQRES 2 A 251 ASN ALA TYR LEU ASP MET PRO LYS ASN ASN PRO GLU LYS
SEQRES 3 A 251 CYS PRO LEU CYS ILE ILE ILE HIS GLY PHE THR GLY HIS
SEQRES 4 A 251 SER GLU GLU ARG HIS ILE VAL ALA VAL GLN GLU THR LEU
SEQRES 5 A 251 ASN GLU ILE GLY VAL ALA THR LEU ARG ALA ASP MET TYR
SEQRES 6 A 251 GLY HIS GLY LYS SER ASP GLY LYS PHE GLU ASP HIS THR
SEQRES 7 A 251 LEU PHE LYS TRP LEU THR ASN ILE LEU ALA VAL VAL ASP
SEQRES 8 A 251 TYR ALA LYS LYS LEU ASP PHE VAL THR ASP ILE TYR MET
SEQRES 9 A 251 ALA GLY HIS SER GLN GLY GLY LEU SER VAL MET LEU ALA
SEQRES 10 A 251 ALA ALA MET GLU ARG ASP ILE ILE LYS ALA LEU ILE PRO
SEQRES 11 A 251 LEU SER PRO ALA ALA MET ILE PRO GLU ILE ALA ARG THR
SEQRES 12 A 251 GLY GLU LEU LEU GLY LEU LYS PHE ASP PRO GLU ASN ILE
SEQRES 13 A 251 PRO ASP GLU LEU ASP ALA TRP ASP GLY ARG LYS LEU LYS
SEQRES 14 A 251 GLY ASN TYR VAL ARG VAL ALA GLN THR ILE ARG VAL GLU
SEQRES 15 A 251 ASP PHE VAL ASP LYS TYR THR LYS PRO VAL LEU ILE VAL
SEQRES 16 A 251 HIS GLY ASP GLN ASP GLU ALA VAL PRO TYR GLU ALA SER
SEQRES 17 A 251 VAL ALA PHE SER LYS GLN TYR LYS ASN CYS LYS LEU VAL
SEQRES 18 A 251 THR ILE PRO GLY ASP THR HIS CYS TYR ASP HIS HIS LEU
SEQRES 19 A 251 GLU LEU VAL THR GLU ALA VAL LYS GLU PHE MET LEU GLU
SEQRES 20 A 251 GLN ILE ALA LYS
SEQRES 1 B 251 SER GLY ALA MET TYR ILE ASP CYS ASP GLY ILE LYS LEU
SEQRES 2 B 251 ASN ALA TYR LEU ASP MET PRO LYS ASN ASN PRO GLU LYS
SEQRES 3 B 251 CYS PRO LEU CYS ILE ILE ILE HIS GLY PHE THR GLY HIS
SEQRES 4 B 251 SER GLU GLU ARG HIS ILE VAL ALA VAL GLN GLU THR LEU
SEQRES 5 B 251 ASN GLU ILE GLY VAL ALA THR LEU ARG ALA ASP MET TYR
SEQRES 6 B 251 GLY HIS GLY LYS SER ASP GLY LYS PHE GLU ASP HIS THR
SEQRES 7 B 251 LEU PHE LYS TRP LEU THR ASN ILE LEU ALA VAL VAL ASP
SEQRES 8 B 251 TYR ALA LYS LYS LEU ASP PHE VAL THR ASP ILE TYR MET
SEQRES 9 B 251 ALA GLY HIS SER GLN GLY GLY LEU SER VAL MET LEU ALA
SEQRES 10 B 251 ALA ALA MET GLU ARG ASP ILE ILE LYS ALA LEU ILE PRO
SEQRES 11 B 251 LEU SER PRO ALA ALA MET ILE PRO GLU ILE ALA ARG THR
SEQRES 12 B 251 GLY GLU LEU LEU GLY LEU LYS PHE ASP PRO GLU ASN ILE
SEQRES 13 B 251 PRO ASP GLU LEU ASP ALA TRP ASP GLY ARG LYS LEU LYS
SEQRES 14 B 251 GLY ASN TYR VAL ARG VAL ALA GLN THR ILE ARG VAL GLU
SEQRES 15 B 251 ASP PHE VAL ASP LYS TYR THR LYS PRO VAL LEU ILE VAL
SEQRES 16 B 251 HIS GLY ASP GLN ASP GLU ALA VAL PRO TYR GLU ALA SER
SEQRES 17 B 251 VAL ALA PHE SER LYS GLN TYR LYS ASN CYS LYS LEU VAL
SEQRES 18 B 251 THR ILE PRO GLY ASP THR HIS CYS TYR ASP HIS HIS LEU
SEQRES 19 B 251 GLU LEU VAL THR GLU ALA VAL LYS GLU PHE MET LEU GLU
SEQRES 20 B 251 GLN ILE ALA LYS
SEQRES 1 C 251 SER GLY ALA MET TYR ILE ASP CYS ASP GLY ILE LYS LEU
SEQRES 2 C 251 ASN ALA TYR LEU ASP MET PRO LYS ASN ASN PRO GLU LYS
SEQRES 3 C 251 CYS PRO LEU CYS ILE ILE ILE HIS GLY PHE THR GLY HIS
SEQRES 4 C 251 SER GLU GLU ARG HIS ILE VAL ALA VAL GLN GLU THR LEU
SEQRES 5 C 251 ASN GLU ILE GLY VAL ALA THR LEU ARG ALA ASP MET TYR
SEQRES 6 C 251 GLY HIS GLY LYS SER ASP GLY LYS PHE GLU ASP HIS THR
SEQRES 7 C 251 LEU PHE LYS TRP LEU THR ASN ILE LEU ALA VAL VAL ASP
SEQRES 8 C 251 TYR ALA LYS LYS LEU ASP PHE VAL THR ASP ILE TYR MET
SEQRES 9 C 251 ALA GLY HIS SER GLN GLY GLY LEU SER VAL MET LEU ALA
SEQRES 10 C 251 ALA ALA MET GLU ARG ASP ILE ILE LYS ALA LEU ILE PRO
SEQRES 11 C 251 LEU SER PRO ALA ALA MET ILE PRO GLU ILE ALA ARG THR
SEQRES 12 C 251 GLY GLU LEU LEU GLY LEU LYS PHE ASP PRO GLU ASN ILE
SEQRES 13 C 251 PRO ASP GLU LEU ASP ALA TRP ASP GLY ARG LYS LEU LYS
SEQRES 14 C 251 GLY ASN TYR VAL ARG VAL ALA GLN THR ILE ARG VAL GLU
SEQRES 15 C 251 ASP PHE VAL ASP LYS TYR THR LYS PRO VAL LEU ILE VAL
SEQRES 16 C 251 HIS GLY ASP GLN ASP GLU ALA VAL PRO TYR GLU ALA SER
SEQRES 17 C 251 VAL ALA PHE SER LYS GLN TYR LYS ASN CYS LYS LEU VAL
SEQRES 18 C 251 THR ILE PRO GLY ASP THR HIS CYS TYR ASP HIS HIS LEU
SEQRES 19 C 251 GLU LEU VAL THR GLU ALA VAL LYS GLU PHE MET LEU GLU
SEQRES 20 C 251 GLN ILE ALA LYS
SEQRES 1 D 251 SER GLY ALA MET TYR ILE ASP CYS ASP GLY ILE LYS LEU
SEQRES 2 D 251 ASN ALA TYR LEU ASP MET PRO LYS ASN ASN PRO GLU LYS
SEQRES 3 D 251 CYS PRO LEU CYS ILE ILE ILE HIS GLY PHE THR GLY HIS
SEQRES 4 D 251 SER GLU GLU ARG HIS ILE VAL ALA VAL GLN GLU THR LEU
SEQRES 5 D 251 ASN GLU ILE GLY VAL ALA THR LEU ARG ALA ASP MET TYR
SEQRES 6 D 251 GLY HIS GLY LYS SER ASP GLY LYS PHE GLU ASP HIS THR
SEQRES 7 D 251 LEU PHE LYS TRP LEU THR ASN ILE LEU ALA VAL VAL ASP
SEQRES 8 D 251 TYR ALA LYS LYS LEU ASP PHE VAL THR ASP ILE TYR MET
SEQRES 9 D 251 ALA GLY HIS SER GLN GLY GLY LEU SER VAL MET LEU ALA
SEQRES 10 D 251 ALA ALA MET GLU ARG ASP ILE ILE LYS ALA LEU ILE PRO
SEQRES 11 D 251 LEU SER PRO ALA ALA MET ILE PRO GLU ILE ALA ARG THR
SEQRES 12 D 251 GLY GLU LEU LEU GLY LEU LYS PHE ASP PRO GLU ASN ILE
SEQRES 13 D 251 PRO ASP GLU LEU ASP ALA TRP ASP GLY ARG LYS LEU LYS
SEQRES 14 D 251 GLY ASN TYR VAL ARG VAL ALA GLN THR ILE ARG VAL GLU
SEQRES 15 D 251 ASP PHE VAL ASP LYS TYR THR LYS PRO VAL LEU ILE VAL
SEQRES 16 D 251 HIS GLY ASP GLN ASP GLU ALA VAL PRO TYR GLU ALA SER
SEQRES 17 D 251 VAL ALA PHE SER LYS GLN TYR LYS ASN CYS LYS LEU VAL
SEQRES 18 D 251 THR ILE PRO GLY ASP THR HIS CYS TYR ASP HIS HIS LEU
SEQRES 19 D 251 GLU LEU VAL THR GLU ALA VAL LYS GLU PHE MET LEU GLU
SEQRES 20 D 251 GLN ILE ALA LYS
HET PO4 D1249 5
HET PO4 B1249 5
HET PO4 D1250 5
HET PO4 C1248 5
HET PO4 B1250 5
HET PO4 A1249 5
HET GOL A1250 6
HET GOL C1249 6
HET GOL D1251 6
HET GOL B1251 6
HET GOL D1252 6
HET GOL B1252 6
HETNAM PO4 PHOSPHATE ION
HETNAM GOL GLYCEROL
FORMUL 5 PO4 6(O4 P 3-)
FORMUL 6 GOL 6(C3 H8 O3)
FORMUL 7 HOH *886(H2 O)
HELIX 1 1 GLU A 39 ILE A 52 1 14
HELIX 2 2 LYS A 70 HIS A 74 5 5
HELIX 3 3 THR A 75 LYS A 91 1 17
HELIX 4 4 LEU A 109 GLU A 118 1 10
HELIX 5 5 MET A 133 THR A 140 1 8
HELIX 6 6 ASN A 168 GLN A 174 1 7
HELIX 7 7 ARG A 177 TYR A 185 1 9
HELIX 8 8 PRO A 201 TYR A 212 1 12
HELIX 9 9 HIS A 230 ALA A 247 1 18
HELIX 10 10 GLU B 39 ILE B 52 1 14
HELIX 11 11 THR B 75 LYS B 92 1 18
HELIX 12 12 LEU B 109 GLU B 118 1 10
HELIX 13 13 MET B 133 THR B 140 1 8
HELIX 14 14 ASN B 168 GLN B 174 1 7
HELIX 15 15 ARG B 177 TYR B 185 1 9
HELIX 16 16 PRO B 201 TYR B 212 1 12
HELIX 17 17 HIS B 230 ALA B 247 1 18
HELIX 18 18 GLU C 39 ILE C 52 1 14
HELIX 19 19 LYS C 70 HIS C 74 5 5
HELIX 20 20 THR C 75 LYS C 91 1 17
HELIX 21 21 LEU C 109 GLU C 118 1 10
HELIX 22 22 MET C 133 THR C 140 1 8
HELIX 23 23 ASN C 168 GLN C 174 1 7
HELIX 24 24 ARG C 177 TYR C 185 1 9
HELIX 25 25 PRO C 201 TYR C 212 1 12
HELIX 26 26 HIS C 230 ALA C 247 1 18
HELIX 27 27 GLU D 39 ILE D 52 1 14
HELIX 28 28 THR D 75 LYS D 91 1 17
HELIX 29 29 LEU D 109 GLU D 118 1 10
HELIX 30 30 MET D 133 THR D 140 1 8
HELIX 31 31 ASN D 168 GLN D 174 1 7
HELIX 32 32 ARG D 177 TYR D 185 1 9
HELIX 33 33 PRO D 201 TYR D 212 1 12
HELIX 34 34 HIS D 230 LYS D 248 1 19
SHEET 1 AA 6 MET A 1 ASP A 4 0
SHEET 2 AA 6 LYS A 9 ASP A 15 -1 O LEU A 10 N ILE A 3
SHEET 3 AA 6 ALA A 55 ALA A 59 -1 O THR A 56 N ASP A 15
SHEET 4 AA 6 CYS A 24 ILE A 30 1 O PRO A 25 N ALA A 55
SHEET 5 AA 6 VAL A 96 ALA A 102 1 N THR A 97 O CYS A 24
SHEET 6 AA 6 ILE A 122 LEU A 125 1 N LYS A 123 O ILE A 99
SHEET 1 AB 2 LEU A 157 ASP A 158 0
SHEET 2 AB 2 LYS A 164 LEU A 165 -1 O LEU A 165 N LEU A 157
SHEET 1 AC 2 VAL A 189 HIS A 193 0
SHEET 2 AC 2 CYS A 215 THR A 219 1 O LYS A 216 N ILE A 191
SHEET 1 BA 6 MET B 1 ASP B 4 0
SHEET 2 BA 6 LYS B 9 ASP B 15 -1 O LEU B 10 N ILE B 3
SHEET 3 BA 6 ALA B 55 ALA B 59 -1 O THR B 56 N ASP B 15
SHEET 4 BA 6 CYS B 24 ILE B 30 1 O PRO B 25 N ALA B 55
SHEET 5 BA 6 VAL B 96 ALA B 102 1 N THR B 97 O CYS B 24
SHEET 6 BA 6 ILE B 122 LEU B 125 1 N LYS B 123 O ILE B 99
SHEET 1 BB 3 LYS B 147 PHE B 148 0
SHEET 2 BB 3 LEU C 157 ASP C 158 1 N ASP C 158 O LYS B 147
SHEET 3 BB 3 LYS C 164 LEU C 165 -1 O LEU C 165 N LEU C 157
SHEET 1 BC 2 LEU B 157 ASP B 158 0
SHEET 2 BC 2 LYS B 164 LEU B 165 -1 O LEU B 165 N LEU B 157
SHEET 1 BD 2 VAL B 189 HIS B 193 0
SHEET 2 BD 2 CYS B 215 THR B 219 1 O LYS B 216 N ILE B 191
SHEET 1 CA 6 MET C 1 ASP C 4 0
SHEET 2 CA 6 LYS C 9 ASP C 15 -1 O LEU C 10 N ILE C 3
SHEET 3 CA 6 ALA C 55 ALA C 59 -1 O THR C 56 N ASP C 15
SHEET 4 CA 6 CYS C 24 ILE C 30 1 O PRO C 25 N ALA C 55
SHEET 5 CA 6 VAL C 96 ALA C 102 1 N THR C 97 O CYS C 24
SHEET 6 CA 6 ILE C 122 LEU C 125 1 N LYS C 123 O ILE C 99
SHEET 1 CB 2 VAL C 189 HIS C 193 0
SHEET 2 CB 2 CYS C 215 THR C 219 1 O LYS C 216 N ILE C 191
SHEET 1 DA 6 MET D 1 ASP D 4 0
SHEET 2 DA 6 LYS D 9 ASP D 15 -1 O LEU D 10 N ILE D 3
SHEET 3 DA 6 ALA D 55 ALA D 59 -1 O THR D 56 N ASP D 15
SHEET 4 DA 6 CYS D 24 ILE D 30 1 O PRO D 25 N ALA D 55
SHEET 5 DA 6 VAL D 96 ALA D 102 1 N THR D 97 O CYS D 24
SHEET 6 DA 6 ILE D 122 LEU D 125 1 N LYS D 123 O ILE D 99
SHEET 1 DB 2 LEU D 157 ASP D 158 0
SHEET 2 DB 2 LYS D 164 LEU D 165 -1 O LEU D 165 N LEU D 157
SHEET 1 DC 2 VAL D 189 HIS D 193 0
SHEET 2 DC 2 CYS D 215 THR D 219 1 O LYS D 216 N ILE D 191
SITE 1 AC1 10 GLY D 32 PHE D 33 THR D 34 SER D 105
SITE 2 AC1 10 GLN D 106 ARG D 163 PO4 D1250 HOH D2191
SITE 3 AC1 10 HOH D2192 HOH D2193
SITE 1 AC2 9 GLY B 32 PHE B 33 THR B 34 SER B 105
SITE 2 AC2 9 GLN B 106 PO4 B1250 HOH B2208 HOH B2209
SITE 3 AC2 9 HOH B2210
SITE 1 AC3 12 HIS D 31 GLY D 32 PHE D 33 THR D 34
SITE 2 AC3 12 GLY D 35 GLU D 39 HIS D 41 HIS D 104
SITE 3 AC3 12 SER D 105 PO4 D1249 HOH D2193 HOH D2194
SITE 1 AC4 7 GLY C 32 PHE C 33 SER C 105 GLN C 106
SITE 2 AC4 7 HIS C 225 GOL C1249 HOH C2255
SITE 1 AC5 12 HIS B 31 GLY B 32 PHE B 33 THR B 34
SITE 2 AC5 12 GLY B 35 GLU B 39 HIS B 41 HIS B 104
SITE 3 AC5 12 SER B 105 PO4 B1249 HOH B2208 HOH B2211
SITE 1 AC6 6 GLY A 32 PHE A 33 SER A 105 GLN A 106
SITE 2 AC6 6 HIS A 225 HOH A2213
SITE 1 AC7 6 HOH A2214 HOH A2215 HOH A2216 GLU B 203
SITE 2 AC7 6 ALA B 207 HOH B2165
SITE 1 AC8 10 PHE C 33 THR C 34 GLY C 35 GLU C 39
SITE 2 AC8 10 HIS C 225 CYS C 226 PO4 C1248 HOH C2257
SITE 3 AC8 10 HOH C2258 HOH C2259
SITE 1 AC9 5 TYR D 13 GLU D 38 ARG D 58 HOH D2034
SITE 2 AC9 5 HOH D2195
SITE 1 BC1 6 TYR B 13 GLU B 38 ARG B 58 HOH B2043
SITE 2 BC1 6 HOH B2212 HOH B2213
SITE 1 BC2 7 HOH C2096 HOH C2104 CYS D 5 ASP D 6
SITE 2 BC2 7 HOH D2071 HOH D2196 HOH D2197
SITE 1 BC3 6 ARG A 119 LYS A 184 ARG B 139 GLU B 151
SITE 2 BC3 6 GLN B 174 HOH B2214
CRYST1 52.035 109.067 91.647 90.00 102.18 90.00 P 1 21 1 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 0.019218 0.000000 0.004148 0.00000
SCALE2 0.000000 0.009169 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011163 0.00000
TER 1973 LYS A 248
TER 3879 LYS B 248
TER 5859 ALA C 247
TER 7761 LYS D 248
MASTER 499 0 12 34 41 0 29 6 8709 4 66 80
END |