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HEADER HYDROLASE 22-APR-16 5JIB
TITLE CRYSTAL STRUCTURE OF THE THERMOTOGA MARITIMA ACETYL ESTERASE (TM0077)
TITLE 2 COMPLEX WITH A SUBSTRATE ANALOG
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CEPHALOSPORIN-C DEACETYLASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 SYNONYM: ACETYLXYLAN ESTERASE;
COMPND 5 EC: 3.1.1.41,3.1.1.72;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA (STRAIN ATCC 43589 / MSB8 /
SOURCE 3 DSM 3109 / JCM 10099);
SOURCE 4 ORGANISM_TAXID: 243274;
SOURCE 5 STRAIN: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099;
SOURCE 6 GENE: AXEA, TM_0077;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 10 EXPRESSION_SYSTEM_VARIANT: RIL;
SOURCE 11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PMH1
KEYWDS HYDROLASE, CARBOHYDRATE METABOLISM, CEPHALOSPORIN DEACETYLASE,
KEYWDS 2 ROSSMANN FOLD
EXPDTA X-RAY DIFFRACTION
AUTHOR N.MANOJ
REVDAT 1 01-MAR-17 5JIB 0
JRNL AUTH M.K.SINGH,N.MANOJ
JRNL TITL CRYSTAL STRUCTURE OF THERMOTOGA MARITIMA ACETYL ESTERASE
JRNL TITL 2 COMPLEX WITH A SUBSTRATE ANALOG: INSIGHTS INTO THE
JRNL TITL 3 DISTINCTIVE SUBSTRATE SPECIFICITY IN THE CE7 CARBOHYDRATE
JRNL TITL 4 ESTERASE FAMILY
JRNL REF BIOCHEM. BIOPHYS. RES. V. 476 63 2016
JRNL REF 2 COMMUN.
JRNL REFN ESSN 1090-2104
JRNL PMID 27181355
JRNL DOI 10.1016/J.BBRC.2016.05.061
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH M.K.SINGH,N.MANOJ
REMARK 1 TITL AN EXTENDED LOOP IN CE7 CARBOHYDRATE ESTERASE FAMILY IS
REMARK 1 TITL 2 DISPENSABLE FOR OLIGOMERIZATION BUT REQUIRED FOR ACTIVITY
REMARK 1 TITL 3 AND THERMOSTABILITY.
REMARK 1 REF J. STRUCT. BIOL. 2016
REMARK 1 REFN ESSN 1095-8657
REMARK 1 PMID 27085421
REMARK 1 DOI 10.1016/J.JSB.2016.04.008
REMARK 2
REMARK 2 RESOLUTION. 1.86 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0103
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 94.8
REMARK 3 NUMBER OF REFLECTIONS : 148760
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) : 0.157
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.192
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 7863
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) : 1.86
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.91
REMARK 3 REFLECTION IN BIN (WORKING SET) : 10040
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 86.39
REMARK 3 BIN R VALUE (WORKING SET) : 0.1840
REMARK 3 BIN FREE R VALUE SET COUNT : 516
REMARK 3 BIN FREE R VALUE : 0.2280
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15120
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 84
REMARK 3 SOLVENT ATOMS : 1039
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.21000
REMARK 3 B22 (A**2) : 0.30000
REMARK 3 B33 (A**2) : -0.54000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.23000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.132
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.122
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.076
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.508
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.961
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 15686 ; 0.019 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 14419 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 21339 ; 1.845 ; 1.955
REMARK 3 BOND ANGLES OTHERS (DEGREES): 33108 ; 1.110 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1908 ; 6.525 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 738 ;29.654 ;22.846
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2291 ;11.899 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 105 ;16.851 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2208 ; 0.117 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 17939 ; 0.011 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 3898 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): 7656 ; 1.787 ; 1.771
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 7655 ; 1.784 ; 1.770
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 9553 ; 2.557 ; 2.643
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 RIDING
REMARK 3 POSITIONS U VALUES : REFINED INDIVIDUALLY
REMARK 4
REMARK 4 5JIB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-APR-16.
REMARK 100 THE DEPOSITION ID IS D_1000220649.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-SEP-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
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 : BRUKER AXS MICROSTAR
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : IMOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS 0.1.30
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 156655
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.860
REMARK 200 RESOLUTION RANGE LOW (A) : 45.970
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 94.3
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.07200
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 19.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 70.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : 0.36000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 5.100
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: 5FDF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.41
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05 M AMMONIUM SULFATE, 0.1 M BIS
REMARK 280 -TRIS PH 6.5 AND 30% (V/V) PENTAERYTHRITOLETHOXYLATE (15/4 EO/OH)
REMARK 280 , VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
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 57.89000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 17740 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 60300 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -119.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 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 -11
REMARK 465 GLY A -10
REMARK 465 SER A -9
REMARK 465 ASP A -8
REMARK 465 LYS A -7
REMARK 465 ILE A -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 ALA A 2
REMARK 465 PHE A 3
REMARK 465 GLU A 134
REMARK 465 LYS A 324
REMARK 465 GLY A 325
REMARK 465 MET B -11
REMARK 465 GLY B -10
REMARK 465 SER B -9
REMARK 465 ASP B -8
REMARK 465 LYS B -7
REMARK 465 ILE B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
REMARK 465 ALA B 2
REMARK 465 PHE B 3
REMARK 465 GLU B 134
REMARK 465 LYS B 324
REMARK 465 GLY B 325
REMARK 465 MET C -11
REMARK 465 GLY C -10
REMARK 465 SER C -9
REMARK 465 ASP C -8
REMARK 465 LYS C -7
REMARK 465 ILE C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 HIS C -1
REMARK 465 HIS C 0
REMARK 465 MET C 1
REMARK 465 ALA C 2
REMARK 465 PHE C 3
REMARK 465 LYS C 324
REMARK 465 GLY C 325
REMARK 465 MET D -11
REMARK 465 GLY D -10
REMARK 465 SER D -9
REMARK 465 ASP D -8
REMARK 465 LYS D -7
REMARK 465 ILE D -6
REMARK 465 HIS D -5
REMARK 465 HIS D -4
REMARK 465 HIS D -3
REMARK 465 HIS D -2
REMARK 465 HIS D -1
REMARK 465 HIS D 0
REMARK 465 MET D 1
REMARK 465 ALA D 2
REMARK 465 PHE D 3
REMARK 465 GLU D 134
REMARK 465 LYS D 324
REMARK 465 GLY D 325
REMARK 465 MET E -11
REMARK 465 GLY E -10
REMARK 465 SER E -9
REMARK 465 ASP E -8
REMARK 465 LYS E -7
REMARK 465 ILE E -6
REMARK 465 HIS E -5
REMARK 465 HIS E -4
REMARK 465 HIS E -3
REMARK 465 HIS E -2
REMARK 465 HIS E -1
REMARK 465 HIS E 0
REMARK 465 MET E 1
REMARK 465 ALA E 2
REMARK 465 PHE E 3
REMARK 465 GLY E 135
REMARK 465 LYS E 324
REMARK 465 GLY E 325
REMARK 465 MET F -11
REMARK 465 GLY F -10
REMARK 465 SER F -9
REMARK 465 ASP F -8
REMARK 465 LYS F -7
REMARK 465 ILE F -6
REMARK 465 HIS F -5
REMARK 465 HIS F -4
REMARK 465 HIS F -3
REMARK 465 HIS F -2
REMARK 465 HIS F -1
REMARK 465 HIS F 0
REMARK 465 MET F 1
REMARK 465 ALA F 2
REMARK 465 PHE F 3
REMARK 465 LYS F 324
REMARK 465 GLY F 325
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 GLU A 9 CG CD OE1 OE2
REMARK 470 LYS A 13 CG CD CE NZ
REMARK 470 LYS A 22 CG CD CE NZ
REMARK 470 GLU A 26 CG CD OE1 OE2
REMARK 470 GLU A 34 CG CD OE1 OE2
REMARK 470 GLU A 36 CG CD OE1 OE2
REMARK 470 LYS A 37 CG CD CE NZ
REMARK 470 GLU A 48 CG CD OE1 OE2
REMARK 470 GLU A 79 CB CG CD OE1 OE2
REMARK 470 ARG A 153 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 169 CG CD OE1 OE2
REMARK 470 GLN A 179 CG CD OE1 NE2
REMARK 470 LYS A 202 CG CD CE NZ
REMARK 470 LYS A 203 CG CD CE NZ
REMARK 470 LYS A 205 CG CD CE NZ
REMARK 470 ARG A 218 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 248 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 263 CD CE NZ
REMARK 470 LYS A 320 CG CD CE NZ
REMARK 470 GLU A 323 CG CD OE1 OE2
REMARK 470 GLU B 9 CG CD OE1 OE2
REMARK 470 LYS B 13 CG CD CE NZ
REMARK 470 LYS B 22 CG CD CE NZ
REMARK 470 GLU B 29 CG CD OE1 OE2
REMARK 470 GLU B 48 CG CD OE1 OE2
REMARK 470 GLU B 79 CG CD OE1 OE2
REMARK 470 GLU B 80 CG CD OE1 OE2
REMARK 470 GLU B 81 CG CD OE1 OE2
REMARK 470 LYS B 82 CG CD CE NZ
REMARK 470 GLU B 169 CG CD OE1 OE2
REMARK 470 GLU B 244 CG CD OE1 OE2
REMARK 470 LYS B 320 CG CD CE NZ
REMARK 470 GLU B 323 CG CD OE1 OE2
REMARK 470 GLU C 9 CG CD OE1 OE2
REMARK 470 LYS C 13 CG CD CE NZ
REMARK 470 ARG C 15 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 17 CG CD OE1 OE2
REMARK 470 LYS C 22 CG CD CE NZ
REMARK 470 GLU C 34 CG CD OE1 OE2
REMARK 470 GLU C 48 CG CD OE1 OE2
REMARK 470 ARG C 65 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 77 CG CD CE NZ
REMARK 470 GLU C 79 CG CD OE1 OE2
REMARK 470 GLU C 81 CG CD OE1 OE2
REMARK 470 GLU C 169 CG CD OE1 OE2
REMARK 470 GLN C 179 CG CD OE1 NE2
REMARK 470 LYS C 202 CG CD CE NZ
REMARK 470 LYS C 203 CG CD CE NZ
REMARK 470 LYS C 205 CG CD CE NZ
REMARK 470 ARG C 218 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 263 CG CD CE NZ
REMARK 470 LYS C 320 CG CD CE NZ
REMARK 470 GLU D 9 CG CD OE1 OE2
REMARK 470 ARG D 15 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 17 CG CD OE1 OE2
REMARK 470 LYS D 22 CG CD CE NZ
REMARK 470 GLU D 34 CG CD OE1 OE2
REMARK 470 GLU D 48 CG CD OE1 OE2
REMARK 470 GLU D 79 CG CD OE1 OE2
REMARK 470 GLU D 81 CG CD OE1 OE2
REMARK 470 LYS D 202 CG CD CE NZ
REMARK 470 LYS D 205 CG CD CE NZ
REMARK 470 ARG D 218 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 237 CG CD CE NZ
REMARK 470 GLU D 244 CG CD OE1 OE2
REMARK 470 LYS D 263 CG CD CE NZ
REMARK 470 LYS D 320 CG CD CE NZ
REMARK 470 GLU D 323 CG CD OE1 OE2
REMARK 470 GLU E 9 CG CD OE1 OE2
REMARK 470 LYS E 22 CG CD CE NZ
REMARK 470 GLU E 30 CG CD OE1 OE2
REMARK 470 GLU E 45 CG CD OE1 OE2
REMARK 470 GLU E 48 CG CD OE1 OE2
REMARK 470 GLU E 79 CG CD OE1 OE2
REMARK 470 GLU E 244 CG CD OE1 OE2
REMARK 470 LYS E 263 CG CD CE NZ
REMARK 470 LYS E 320 CG CD CE NZ
REMARK 470 GLU E 323 CG CD OE1 OE2
REMARK 470 GLU F 9 CG CD OE1 OE2
REMARK 470 LYS F 13 CG CD CE NZ
REMARK 470 LYS F 22 CG CD CE NZ
REMARK 470 GLU F 30 CG CD OE1 OE2
REMARK 470 LYS F 37 CG CD CE NZ
REMARK 470 GLU F 48 CG CD OE1 OE2
REMARK 470 GLU F 79 CB CG CD OE1 OE2
REMARK 470 GLU F 80 CB CG CD OE1 OE2
REMARK 470 GLU F 81 CB CG CD OE1 OE2
REMARK 470 LYS F 82 CG CD CE NZ
REMARK 470 ARG F 153 CG CD NE CZ NH1 NH2
REMARK 470 LYS F 202 CG CD CE NZ
REMARK 470 LYS F 203 CG CD CE NZ
REMARK 470 LYS F 205 CG CD CE NZ
REMARK 470 GLU F 244 CG CD OE1 OE2
REMARK 470 LYS F 320 CG CD CE NZ
REMARK 470 GLU F 323 CG CD OE1 OE2
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 OE1 GLU B 55 O HOH B 501 2.12
REMARK 500 O HOH C 513 O HOH C 535 2.19
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 GLU E 243 CD GLU E 243 OE1 -0.067
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 163 CB - CG - OD1 ANGL. DEV. = 5.4 DEGREES
REMARK 500 ARG A 219 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG A 219 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ARG A 240 NE - CZ - NH1 ANGL. DEV. = 3.3 DEGREES
REMARK 500 ASP A 241 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ARG B 18 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ASP B 151 CB - CG - OD1 ANGL. DEV. = 5.9 DEGREES
REMARK 500 ASP B 151 CB - CG - OD2 ANGL. DEV. = -5.8 DEGREES
REMARK 500 PHE B 161 CB - CG - CD1 ANGL. DEV. = 4.4 DEGREES
REMARK 500 ARG B 240 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ASP B 241 CB - CG - OD1 ANGL. DEV. = 7.3 DEGREES
REMARK 500 ARG C 18 NE - CZ - NH1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 ARG C 18 NE - CZ - NH2 ANGL. DEV. = -3.8 DEGREES
REMARK 500 ARG C 68 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG C 118 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP C 151 CB - CG - OD1 ANGL. DEV. = 7.0 DEGREES
REMARK 500 ASP C 163 CB - CG - OD1 ANGL. DEV. = 5.8 DEGREES
REMARK 500 ARG C 219 NE - CZ - NH2 ANGL. DEV. = -3.5 DEGREES
REMARK 500 ARG C 240 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ASP C 241 CB - CG - OD1 ANGL. DEV. = 7.4 DEGREES
REMARK 500 ASP D 25 CB - CG - OD1 ANGL. DEV. = 5.6 DEGREES
REMARK 500 ASP D 163 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP D 241 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ARG D 248 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG D 261 NE - CZ - NH1 ANGL. DEV. = 3.6 DEGREES
REMARK 500 ARG E 15 NE - CZ - NH1 ANGL. DEV. = 3.2 DEGREES
REMARK 500 ARG E 118 NE - CZ - NH1 ANGL. DEV. = 4.2 DEGREES
REMARK 500 ARG E 118 NE - CZ - NH2 ANGL. DEV. = -3.9 DEGREES
REMARK 500 ASP E 151 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP E 163 CB - CG - OD1 ANGL. DEV. = 5.5 DEGREES
REMARK 500 ASP E 241 CB - CG - OD1 ANGL. DEV. = 8.7 DEGREES
REMARK 500 ARG E 248 NE - CZ - NH1 ANGL. DEV. = 3.4 DEGREES
REMARK 500 ARG E 261 NE - CZ - NH1 ANGL. DEV. = 3.7 DEGREES
REMARK 500 ARG F 46 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG F 65 NE - CZ - NH1 ANGL. DEV. = 3.0 DEGREES
REMARK 500 ASP F 151 CB - CG - OD1 ANGL. DEV. = 6.5 DEGREES
REMARK 500 ASP F 241 CB - CG - OD1 ANGL. DEV. = 6.3 DEGREES
REMARK 500 ARG F 248 NE - CZ - NH1 ANGL. DEV. = 3.4 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 5 -166.56 -102.95
REMARK 500 GLN A 120 -121.92 -96.16
REMARK 500 SER A 122 12.32 -141.84
REMARK 500 PRO A 139 127.48 -38.08
REMARK 500 SER A 188 -115.74 58.90
REMARK 500 VAL A 211 56.82 30.04
REMARK 500 ASN A 302 -144.47 -91.45
REMARK 500 ASP B 5 -168.74 -105.67
REMARK 500 ASP B 41 61.52 38.62
REMARK 500 GLN B 120 -116.98 -101.93
REMARK 500 SER B 188 -120.56 63.63
REMARK 500 VAL B 211 52.55 38.91
REMARK 500 ASN B 302 -142.89 -88.34
REMARK 500 GLN C 120 -121.47 -93.06
REMARK 500 ASP C 138 151.34 -49.62
REMARK 500 PRO C 139 132.52 -38.91
REMARK 500 SER C 188 -119.05 58.91
REMARK 500 VAL C 211 56.21 37.09
REMARK 500 ASN C 302 -147.88 -88.63
REMARK 500 ASN C 302 -147.52 -88.59
REMARK 500 GLN D 120 -117.96 -96.85
REMARK 500 ASP D 138 154.24 -49.36
REMARK 500 PRO D 139 131.37 -39.35
REMARK 500 SER D 188 -120.61 56.35
REMARK 500 VAL D 211 56.60 32.51
REMARK 500 ASN D 302 -144.12 -81.65
REMARK 500 ASP E 5 -165.40 -111.87
REMARK 500 GLN E 120 -117.68 -96.87
REMARK 500 SER E 188 -123.59 63.00
REMARK 500 VAL E 211 54.90 34.67
REMARK 500 ASN E 302 -143.92 -89.90
REMARK 500 ASP F 5 -166.91 -101.09
REMARK 500 GLN F 120 -121.26 -98.26
REMARK 500 TRP F 124 -18.81 -154.74
REMARK 500 SER F 188 -114.11 62.87
REMARK 500 VAL F 211 53.19 39.63
REMARK 500 ASN F 302 -145.09 -91.20
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 B 681 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH F 669 DISTANCE = 6.34 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OIA A 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OIA B 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OIA C 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OIA D 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OIA E 400
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OIA F 400
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5FDF RELATED DB: PDB
REMARK 900 5FDF CONTAINS THE APO-FORM OF THE SAME PROTEIN
REMARK 900 RELATED ID: 5HFN RELATED DB: PDB
REMARK 900 5HFN CONTAINS A TRUNCATION VARIANT OF THE SAME PROTEIN
REMARK 900 RELATED ID: 3M82 RELATED DB: PDB
REMARK 900 3M82 CONTAINS A COVALENTLY MODIFIED INHIBITOR (PMSF) COMPLEX OF THE
REMARK 900 SAME PROTEIN
REMARK 900 RELATED ID: 3M83 RELATED DB: PDB
REMARK 900 3M83 CONTAINS A COVALENTLY MODIFIED INHIBITOR (PARAOXON)COMPLEX OF
REMARK 900 THE SAME PROTEIN
DBREF 5JIB A 1 325 UNP Q9WXT2 CAH_THEMA 1 325
DBREF 5JIB B 1 325 UNP Q9WXT2 CAH_THEMA 1 325
DBREF 5JIB C 1 325 UNP Q9WXT2 CAH_THEMA 1 325
DBREF 5JIB D 1 325 UNP Q9WXT2 CAH_THEMA 1 325
DBREF 5JIB E 1 325 UNP Q9WXT2 CAH_THEMA 1 325
DBREF 5JIB F 1 325 UNP Q9WXT2 CAH_THEMA 1 325
SEQADV 5JIB MET A -11 UNP Q9WXT2 INITIATING METHIONINE
SEQADV 5JIB GLY A -10 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB SER A -9 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB ASP A -8 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB LYS A -7 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB ILE A -6 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS A -5 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS A -4 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS A -3 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS A -2 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS A -1 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS A 0 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB MET B -11 UNP Q9WXT2 INITIATING METHIONINE
SEQADV 5JIB GLY B -10 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB SER B -9 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB ASP B -8 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB LYS B -7 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB ILE B -6 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS B -5 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS B -4 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS B -3 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS B -2 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS B -1 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS B 0 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB MET C -11 UNP Q9WXT2 INITIATING METHIONINE
SEQADV 5JIB GLY C -10 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB SER C -9 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB ASP C -8 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB LYS C -7 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB ILE C -6 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS C -5 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS C -4 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS C -3 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS C -2 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS C -1 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS C 0 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB MET D -11 UNP Q9WXT2 INITIATING METHIONINE
SEQADV 5JIB GLY D -10 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB SER D -9 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB ASP D -8 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB LYS D -7 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB ILE D -6 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS D -5 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS D -4 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS D -3 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS D -2 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS D -1 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS D 0 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB MET E -11 UNP Q9WXT2 INITIATING METHIONINE
SEQADV 5JIB GLY E -10 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB SER E -9 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB ASP E -8 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB LYS E -7 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB ILE E -6 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS E -5 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS E -4 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS E -3 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS E -2 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS E -1 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS E 0 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB MET F -11 UNP Q9WXT2 INITIATING METHIONINE
SEQADV 5JIB GLY F -10 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB SER F -9 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB ASP F -8 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB LYS F -7 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB ILE F -6 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS F -5 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS F -4 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS F -3 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS F -2 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS F -1 UNP Q9WXT2 EXPRESSION TAG
SEQADV 5JIB HIS F 0 UNP Q9WXT2 EXPRESSION TAG
SEQRES 1 A 337 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 A 337 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 A 337 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 A 337 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 A 337 ASP PRO VAL PHE GLU ARG MET GLU SER HIS LEU LYS THR
SEQRES 6 A 337 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 A 337 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 A 337 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 A 337 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 A 337 PRO SER MET GLY TYR ILE CYS PHE VAL MET ASP THR ARG
SEQRES 11 A 337 GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP
SEQRES 12 A 337 TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE
SEQRES 13 A 337 MET THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 14 A 337 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 15 A 337 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 16 A 337 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 17 A 337 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 18 A 337 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 19 A 337 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 20 A 337 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 21 A 337 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 22 A 337 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MET ASP
SEQRES 23 A 337 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 24 A 337 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 25 A 337 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 26 A 337 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
SEQRES 1 B 337 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 B 337 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 B 337 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 B 337 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 B 337 ASP PRO VAL PHE GLU ARG MET GLU SER HIS LEU LYS THR
SEQRES 6 B 337 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 B 337 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 B 337 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 B 337 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 B 337 PRO SER MET GLY TYR ILE CYS PHE VAL MET ASP THR ARG
SEQRES 11 B 337 GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP
SEQRES 12 B 337 TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE
SEQRES 13 B 337 MET THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 14 B 337 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 15 B 337 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 16 B 337 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 17 B 337 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 18 B 337 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 19 B 337 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 20 B 337 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 21 B 337 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 22 B 337 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MET ASP
SEQRES 23 B 337 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 24 B 337 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 25 B 337 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 26 B 337 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
SEQRES 1 C 337 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 C 337 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 C 337 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 C 337 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 C 337 ASP PRO VAL PHE GLU ARG MET GLU SER HIS LEU LYS THR
SEQRES 6 C 337 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 C 337 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 C 337 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 C 337 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 C 337 PRO SER MET GLY TYR ILE CYS PHE VAL MET ASP THR ARG
SEQRES 11 C 337 GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP
SEQRES 12 C 337 TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE
SEQRES 13 C 337 MET THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 14 C 337 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 15 C 337 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 16 C 337 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 17 C 337 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 18 C 337 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 19 C 337 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 20 C 337 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 21 C 337 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 22 C 337 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MET ASP
SEQRES 23 C 337 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 24 C 337 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 25 C 337 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 26 C 337 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
SEQRES 1 D 337 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 D 337 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 D 337 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 D 337 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 D 337 ASP PRO VAL PHE GLU ARG MET GLU SER HIS LEU LYS THR
SEQRES 6 D 337 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 D 337 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 D 337 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 D 337 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 D 337 PRO SER MET GLY TYR ILE CYS PHE VAL MET ASP THR ARG
SEQRES 11 D 337 GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP
SEQRES 12 D 337 TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE
SEQRES 13 D 337 MET THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 14 D 337 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 15 D 337 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 16 D 337 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 17 D 337 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 18 D 337 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 19 D 337 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 20 D 337 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 21 D 337 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 22 D 337 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MET ASP
SEQRES 23 D 337 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 24 D 337 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 25 D 337 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 26 D 337 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
SEQRES 1 E 337 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 E 337 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 E 337 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 E 337 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 E 337 ASP PRO VAL PHE GLU ARG MET GLU SER HIS LEU LYS THR
SEQRES 6 E 337 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 E 337 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 E 337 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 E 337 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 E 337 PRO SER MET GLY TYR ILE CYS PHE VAL MET ASP THR ARG
SEQRES 11 E 337 GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP
SEQRES 12 E 337 TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE
SEQRES 13 E 337 MET THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 14 E 337 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 15 E 337 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 16 E 337 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 17 E 337 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 18 E 337 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 19 E 337 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 20 E 337 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 21 E 337 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 22 E 337 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MET ASP
SEQRES 23 E 337 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 24 E 337 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 25 E 337 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 26 E 337 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
SEQRES 1 F 337 MET GLY SER ASP LYS ILE HIS HIS HIS HIS HIS HIS MET
SEQRES 2 F 337 ALA PHE PHE ASP LEU PRO LEU GLU GLU LEU LYS LYS TYR
SEQRES 3 F 337 ARG PRO GLU ARG TYR GLU GLU LYS ASP PHE ASP GLU PHE
SEQRES 4 F 337 TRP GLU GLU THR LEU ALA GLU SER GLU LYS PHE PRO LEU
SEQRES 5 F 337 ASP PRO VAL PHE GLU ARG MET GLU SER HIS LEU LYS THR
SEQRES 6 F 337 VAL GLU ALA TYR ASP VAL THR PHE SER GLY TYR ARG GLY
SEQRES 7 F 337 GLN ARG ILE LYS GLY TRP LEU LEU VAL PRO LYS LEU GLU
SEQRES 8 F 337 GLU GLU LYS LEU PRO CYS VAL VAL GLN TYR ILE GLY TYR
SEQRES 9 F 337 ASN GLY GLY ARG GLY PHE PRO HIS ASP TRP LEU PHE TRP
SEQRES 10 F 337 PRO SER MET GLY TYR ILE CYS PHE VAL MET ASP THR ARG
SEQRES 11 F 337 GLY GLN GLY SER GLY TRP LEU LYS GLY ASP THR PRO ASP
SEQRES 12 F 337 TYR PRO GLU GLY PRO VAL ASP PRO GLN TYR PRO GLY PHE
SEQRES 13 F 337 MET THR ARG GLY ILE LEU ASP PRO ARG THR TYR TYR TYR
SEQRES 14 F 337 ARG ARG VAL PHE THR ASP ALA VAL ARG ALA VAL GLU ALA
SEQRES 15 F 337 ALA ALA SER PHE PRO GLN VAL ASP GLN GLU ARG ILE VAL
SEQRES 16 F 337 ILE ALA GLY GLY SER GLN GLY GLY GLY ILE ALA LEU ALA
SEQRES 17 F 337 VAL SER ALA LEU SER LYS LYS ALA LYS ALA LEU LEU CYS
SEQRES 18 F 337 ASP VAL PRO PHE LEU CYS HIS PHE ARG ARG ALA VAL GLN
SEQRES 19 F 337 LEU VAL ASP THR HIS PRO TYR ALA GLU ILE THR ASN PHE
SEQRES 20 F 337 LEU LYS THR HIS ARG ASP LYS GLU GLU ILE VAL PHE ARG
SEQRES 21 F 337 THR LEU SER TYR PHE ASP GLY VAL ASN PHE ALA ALA ARG
SEQRES 22 F 337 ALA LYS ILE PRO ALA LEU PHE SER VAL GLY LEU MET ASP
SEQRES 23 F 337 ASN ILE CYS PRO PRO SER THR VAL PHE ALA ALA TYR ASN
SEQRES 24 F 337 TYR TYR ALA GLY PRO LYS GLU ILE ARG ILE TYR PRO TYR
SEQRES 25 F 337 ASN ASN HIS GLU GLY GLY GLY SER PHE GLN ALA VAL GLU
SEQRES 26 F 337 GLN VAL LYS PHE LEU LYS LYS LEU PHE GLU LYS GLY
HET OIA A 400 14
HET OIA B 400 14
HET OIA C 400 14
HET OIA D 400 14
HET OIA E 400 14
HET OIA F 400 14
HETNAM OIA [(3S)-2-OXO-2,3-DIHYDRO-1H-INDOL-3-YL]ACETIC ACID
FORMUL 7 OIA 6(C10 H9 N O3)
FORMUL 13 HOH *1039(H2 O)
HELIX 1 AA1 PRO A 7 LYS A 12 1 6
HELIX 2 AA2 ASP A 23 LYS A 37 1 15
HELIX 3 AA3 TYR A 64 GLY A 66 5 3
HELIX 4 AA4 PHE A 98 TRP A 102 5 5
HELIX 5 AA5 LEU A 103 MET A 108 1 6
HELIX 6 AA6 ASP A 151 THR A 154 5 4
HELIX 7 AA7 TYR A 155 PHE A 174 1 20
HELIX 8 AA8 SER A 188 SER A 201 1 14
HELIX 9 AA9 HIS A 216 VAL A 224 1 9
HELIX 10 AB1 PRO A 228 HIS A 239 1 12
HELIX 11 AB2 LYS A 242 TYR A 252 1 11
HELIX 12 AB3 ASP A 254 ALA A 260 1 7
HELIX 13 AB4 PRO A 278 TYR A 289 1 12
HELIX 14 AB5 GLY A 306 GLU A 323 1 18
HELIX 15 AB6 PRO B 7 LYS B 12 1 6
HELIX 16 AB7 ASP B 23 LYS B 37 1 15
HELIX 17 AB8 TYR B 64 GLY B 66 5 3
HELIX 18 AB9 PHE B 98 TRP B 102 5 5
HELIX 19 AC1 LEU B 103 MET B 108 1 6
HELIX 20 AC2 ASP B 151 THR B 154 5 4
HELIX 21 AC3 TYR B 155 PHE B 174 1 20
HELIX 22 AC4 SER B 188 SER B 201 1 14
HELIX 23 AC5 HIS B 216 VAL B 224 1 9
HELIX 24 AC6 PRO B 228 HIS B 239 1 12
HELIX 25 AC7 LYS B 242 TYR B 252 1 11
HELIX 26 AC8 ASP B 254 ALA B 260 1 7
HELIX 27 AC9 PRO B 278 TYR B 289 1 12
HELIX 28 AD1 GLY B 306 PHE B 322 1 17
HELIX 29 AD2 PRO C 7 LYS C 12 1 6
HELIX 30 AD3 ASP C 23 LYS C 37 1 15
HELIX 31 AD4 TYR C 64 GLY C 66 5 3
HELIX 32 AD5 PHE C 98 TRP C 102 5 5
HELIX 33 AD6 LEU C 103 MET C 108 1 6
HELIX 34 AD7 ASP C 151 THR C 154 5 4
HELIX 35 AD8 TYR C 155 PHE C 174 1 20
HELIX 36 AD9 SER C 188 SER C 201 1 14
HELIX 37 AE1 HIS C 216 VAL C 224 1 9
HELIX 38 AE2 PRO C 228 HIS C 239 1 12
HELIX 39 AE3 LYS C 242 TYR C 252 1 11
HELIX 40 AE4 ASP C 254 ALA C 260 1 7
HELIX 41 AE5 PRO C 278 TYR C 289 1 12
HELIX 42 AE6 GLY C 306 GLU C 323 1 18
HELIX 43 AE7 PRO D 7 LYS D 12 1 6
HELIX 44 AE8 ASP D 23 LYS D 37 1 15
HELIX 45 AE9 TYR D 64 GLY D 66 5 3
HELIX 46 AF1 PHE D 98 TRP D 102 5 5
HELIX 47 AF2 LEU D 103 MET D 108 1 6
HELIX 48 AF3 ASP D 151 THR D 154 5 4
HELIX 49 AF4 TYR D 155 SER D 173 1 19
HELIX 50 AF5 SER D 188 SER D 201 1 14
HELIX 51 AF6 HIS D 216 VAL D 224 1 9
HELIX 52 AF7 TYR D 229 HIS D 239 1 11
HELIX 53 AF8 LYS D 242 TYR D 252 1 11
HELIX 54 AF9 ASP D 254 ALA D 260 1 7
HELIX 55 AG1 PRO D 278 TYR D 289 1 12
HELIX 56 AG2 GLY D 306 GLU D 323 1 18
HELIX 57 AG3 PRO E 7 LYS E 12 1 6
HELIX 58 AG4 ASP E 23 LYS E 37 1 15
HELIX 59 AG5 TYR E 64 GLY E 66 5 3
HELIX 60 AG6 PHE E 98 TRP E 102 5 5
HELIX 61 AG7 LEU E 103 MET E 108 1 6
HELIX 62 AG8 TYR E 155 SER E 173 1 19
HELIX 63 AG9 SER E 188 SER E 201 1 14
HELIX 64 AH1 HIS E 216 VAL E 224 1 9
HELIX 65 AH2 TYR E 229 HIS E 239 1 11
HELIX 66 AH3 LYS E 242 TYR E 252 1 11
HELIX 67 AH4 ASP E 254 ALA E 260 1 7
HELIX 68 AH5 PRO E 278 TYR E 289 1 12
HELIX 69 AH6 GLY E 306 GLU E 323 1 18
HELIX 70 AH7 PRO F 7 LYS F 13 1 7
HELIX 71 AH8 ASP F 23 LYS F 37 1 15
HELIX 72 AH9 TYR F 64 GLY F 66 5 3
HELIX 73 AI1 PHE F 98 TRP F 102 5 5
HELIX 74 AI2 LEU F 103 MET F 108 1 6
HELIX 75 AI3 TYR F 155 SER F 173 1 19
HELIX 76 AI4 SER F 188 SER F 201 1 14
HELIX 77 AI5 HIS F 216 VAL F 224 1 9
HELIX 78 AI6 TYR F 229 HIS F 239 1 11
HELIX 79 AI7 LYS F 242 TYR F 252 1 11
HELIX 80 AI8 ASP F 254 ALA F 260 1 7
HELIX 81 AI9 PRO F 278 TYR F 289 1 12
HELIX 82 AJ1 GLY F 306 GLU F 323 1 18
SHEET 1 AA1 9 VAL A 43 ARG A 46 0
SHEET 2 AA1 9 VAL A 54 SER A 62 -1 O THR A 60 N VAL A 43
SHEET 3 AA1 9 ARG A 68 PRO A 76 -1 O ILE A 69 N PHE A 61
SHEET 4 AA1 9 ILE A 111 MET A 115 -1 O VAL A 114 N TRP A 72
SHEET 5 AA1 9 LEU A 83 TYR A 89 1 N GLN A 88 O PHE A 113
SHEET 6 AA1 9 VAL A 177 GLY A 187 1 O VAL A 183 N VAL A 87
SHEET 7 AA1 9 ALA A 206 ASP A 210 1 O LEU A 208 N ILE A 184
SHEET 8 AA1 9 ALA A 266 GLY A 271 1 O LEU A 267 N CYS A 209
SHEET 9 AA1 9 LYS A 293 TYR A 298 1 O GLU A 294 N PHE A 268
SHEET 1 AA2 9 VAL B 43 ARG B 46 0
SHEET 2 AA2 9 VAL B 54 SER B 62 -1 O THR B 60 N VAL B 43
SHEET 3 AA2 9 ARG B 68 PRO B 76 -1 O VAL B 75 N GLU B 55
SHEET 4 AA2 9 ILE B 111 MET B 115 -1 O VAL B 114 N TRP B 72
SHEET 5 AA2 9 LEU B 83 GLN B 88 1 N GLN B 88 O PHE B 113
SHEET 6 AA2 9 VAL B 177 GLY B 187 1 O VAL B 183 N CYS B 85
SHEET 7 AA2 9 ALA B 206 ASP B 210 1 O ASP B 210 N GLY B 186
SHEET 8 AA2 9 ALA B 266 GLY B 271 1 O LEU B 267 N CYS B 209
SHEET 9 AA2 9 LYS B 293 TYR B 298 1 O GLU B 294 N PHE B 268
SHEET 1 AA3 9 VAL C 43 ARG C 46 0
SHEET 2 AA3 9 VAL C 54 SER C 62 -1 O ASP C 58 N GLU C 45
SHEET 3 AA3 9 ARG C 68 PRO C 76 -1 O ILE C 69 N PHE C 61
SHEET 4 AA3 9 ILE C 111 MET C 115 -1 O CYS C 112 N LEU C 74
SHEET 5 AA3 9 LEU C 83 GLN C 88 1 N GLN C 88 O PHE C 113
SHEET 6 AA3 9 VAL C 177 GLY C 187 1 O VAL C 183 N CYS C 85
SHEET 7 AA3 9 ALA C 206 ASP C 210 1 O LEU C 208 N ILE C 184
SHEET 8 AA3 9 ALA C 266 GLY C 271 1 O LEU C 267 N CYS C 209
SHEET 9 AA3 9 LYS C 293 TYR C 298 1 O GLU C 294 N PHE C 268
SHEET 1 AA4 9 VAL D 43 ARG D 46 0
SHEET 2 AA4 9 VAL D 54 SER D 62 -1 O ASP D 58 N GLU D 45
SHEET 3 AA4 9 ARG D 68 PRO D 76 -1 O VAL D 75 N GLU D 55
SHEET 4 AA4 9 ILE D 111 MET D 115 -1 O VAL D 114 N TRP D 72
SHEET 5 AA4 9 LEU D 83 GLN D 88 1 N PRO D 84 O ILE D 111
SHEET 6 AA4 9 VAL D 177 GLY D 187 1 O VAL D 183 N CYS D 85
SHEET 7 AA4 9 ALA D 206 ASP D 210 1 O ALA D 206 N ILE D 184
SHEET 8 AA4 9 ALA D 266 GLY D 271 1 O LEU D 267 N CYS D 209
SHEET 9 AA4 9 LYS D 293 TYR D 298 1 O GLU D 294 N PHE D 268
SHEET 1 AA5 9 VAL E 43 ARG E 46 0
SHEET 2 AA5 9 VAL E 54 SER E 62 -1 O THR E 60 N VAL E 43
SHEET 3 AA5 9 ARG E 68 PRO E 76 -1 O ILE E 69 N PHE E 61
SHEET 4 AA5 9 ILE E 111 MET E 115 -1 O VAL E 114 N TRP E 72
SHEET 5 AA5 9 LEU E 83 GLN E 88 1 N GLN E 88 O PHE E 113
SHEET 6 AA5 9 VAL E 177 GLY E 187 1 O VAL E 183 N CYS E 85
SHEET 7 AA5 9 ALA E 206 ASP E 210 1 O ALA E 206 N ILE E 184
SHEET 8 AA5 9 ALA E 266 GLY E 271 1 O LEU E 267 N LEU E 207
SHEET 9 AA5 9 LYS E 293 TYR E 298 1 O TYR E 298 N VAL E 270
SHEET 1 AA6 9 VAL F 43 ARG F 46 0
SHEET 2 AA6 9 VAL F 54 SER F 62 -1 O ASP F 58 N GLU F 45
SHEET 3 AA6 9 ARG F 68 PRO F 76 -1 O ILE F 69 N PHE F 61
SHEET 4 AA6 9 ILE F 111 MET F 115 -1 O VAL F 114 N TRP F 72
SHEET 5 AA6 9 LEU F 83 GLN F 88 1 N GLN F 88 O PHE F 113
SHEET 6 AA6 9 VAL F 177 GLY F 187 1 O VAL F 183 N CYS F 85
SHEET 7 AA6 9 ALA F 206 ASP F 210 1 O LEU F 208 N ILE F 184
SHEET 8 AA6 9 ALA F 266 GLY F 271 1 O LEU F 267 N LEU F 207
SHEET 9 AA6 9 LYS F 293 TYR F 298 1 O GLU F 294 N PHE F 268
CISPEP 1 HIS A 227 PRO A 228 0 7.58
CISPEP 2 HIS B 227 PRO B 228 0 10.74
CISPEP 3 HIS C 227 PRO C 228 0 11.56
CISPEP 4 HIS D 227 PRO D 228 0 11.81
CISPEP 5 HIS E 227 PRO E 228 0 10.09
CISPEP 6 HIS F 227 PRO F 228 0 10.91
SITE 1 AC1 7 GLY A 91 TYR A 92 SER A 188 GLN A 189
SITE 2 AC1 7 HIS A 227 HIS A 303 HOH A 603
SITE 1 AC2 7 GLY B 91 TYR B 92 SER B 188 GLN B 189
SITE 2 AC2 7 HIS B 227 HIS B 303 HOH B 517
SITE 1 AC3 7 GLY C 91 TYR C 92 SER C 188 GLN C 189
SITE 2 AC3 7 HIS C 227 HIS C 303 HOH C 501
SITE 1 AC4 7 GLY D 91 TYR D 92 SER D 188 GLN D 189
SITE 2 AC4 7 HIS D 227 HIS D 303 HOH D 519
SITE 1 AC5 7 GLY E 91 TYR E 92 SER E 188 GLN E 189
SITE 2 AC5 7 HIS E 227 HIS E 303 HOH E 548
SITE 1 AC6 7 GLY F 91 TYR F 92 SER F 188 GLN F 189
SITE 2 AC6 7 HIS F 227 HIS F 303 HOH F 556
CRYST1 89.810 115.780 103.200 90.00 109.98 90.00 P 1 21 1 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 0.011135 0.000000 0.004048 0.00000
SCALE2 0.000000 0.008637 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010310 0.00000
TER 2498 GLU A 323
TER 5030 GLU B 323
TER 7546 GLU C 323
TER 10062 GLU D 323
TER 12611 GLU E 323
TER 15131 GLU F 323
MASTER 646 0 6 82 54 0 12 616243 6 84 156
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