| content |
HEADER HYDROLASE 17-MAR-10 3M82
TITLE CRYSTAL STRUCTURE OF ACETYL XYLAN ESTERASE (TM0077) FROM THERMOTOGA
TITLE 2 MARITIMA AT 2.40 A RESOLUTION (PMSF INHIBITOR COMPLEX STRUCTURE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ACETYL XYLAN ESTERASE;
COMPND 3 CHAIN: A, B, C, D, E, F;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: THERMOTOGA MARITIMA;
SOURCE 3 ORGANISM_TAXID: 2336;
SOURCE 4 GENE: TM0077, TM_0077;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: DL41;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: MH1
KEYWDS STRUCTURAL GENOMICS, JOINT CENTER FOR STRUCTURAL GENOMICS, JCSG,
KEYWDS 2 PROTEIN STRUCTURE INITIATIVE, PSI-2, AXE1, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
REVDAT 1 26-MAY-10 3M82 0
JRNL AUTH JOINT CENTER FOR STRUCTURAL GENOMICS (JCSG)
JRNL TITL CRYSTAL STRUCTURE OF ACETYL XYLAN ESTERASE (TM0077) FROM
JRNL TITL 2 THERMOTOGA MARITIMA AT 2.40 A RESOLUTION (PMSF INHIBITOR
JRNL TITL 3 COMPLEX STRUCTURE)
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.97
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 94680
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) : 0.162
REMARK 3 R VALUE (WORKING SET) : 0.160
REMARK 3 FREE R VALUE : 0.208
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 4742
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) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.46
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6549
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.93
REMARK 3 BIN R VALUE (WORKING SET) : 0.2030
REMARK 3 BIN FREE R VALUE SET COUNT : 366
REMARK 3 BIN FREE R VALUE : 0.2980
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 15616
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 44
REMARK 3 SOLVENT ATOMS : 946
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 34.88
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.24
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.32000
REMARK 3 B22 (A**2) : 0.12000
REMARK 3 B33 (A**2) : 1.20000
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): 0.332
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.219
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.150
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.401
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.926
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 16255 ; 0.017 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 11377 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 22055 ; 1.532 ; 1.962
REMARK 3 BOND ANGLES OTHERS (DEGREES): 27413 ; 1.018 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1946 ; 6.380 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 804 ;31.775 ;23.109
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2553 ;14.558 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 115 ;16.887 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 2233 ; 0.088 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 18279 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 3702 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 2927 ; 0.199 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 11551 ; 0.194 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 7584 ; 0.181 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 7883 ; 0.086 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 811 ; 0.162 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): 2 ; 0.124 ; 0.200
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): 7 ; 0.099 ; 0.200
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 13 ; 0.268 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 33 ; 0.301 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.213 ; 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): 10099 ; 1.803 ; 3.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3896 ; 0.260 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 15617 ; 2.593 ; 5.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 7350 ; 4.646 ; 8.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 6438 ; 5.807 ;11.000
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C D E F
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 3 A 323 2
REMARK 3 1 B 3 B 323 2
REMARK 3 1 C 3 C 323 2
REMARK 3 1 D 3 D 323 2
REMARK 3 1 E 3 E 323 2
REMARK 3 1 F 3 F 323 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT POSITIONAL 1 A (A): 1853 ; 0.040 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 B (A): 1853 ; 0.040 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 C (A): 1853 ; 0.050 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 D (A): 1853 ; 0.040 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 E (A): 1853 ; 0.040 ; 0.050
REMARK 3 TIGHT POSITIONAL 1 F (A): 1853 ; 0.040 ; 0.050
REMARK 3 MEDIUM POSITIONAL 1 A (A): 2557 ; 0.260 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 B (A): 2557 ; 0.260 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 C (A): 2557 ; 0.290 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 D (A): 2557 ; 0.220 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 E (A): 2557 ; 0.240 ; 0.500
REMARK 3 MEDIUM POSITIONAL 1 F (A): 2557 ; 0.220 ; 0.500
REMARK 3 TIGHT THERMAL 1 A (A**2): 1853 ; 0.150 ; 0.500
REMARK 3 TIGHT THERMAL 1 B (A**2): 1853 ; 0.180 ; 0.500
REMARK 3 TIGHT THERMAL 1 C (A**2): 1853 ; 0.150 ; 0.500
REMARK 3 TIGHT THERMAL 1 D (A**2): 1853 ; 0.160 ; 0.500
REMARK 3 TIGHT THERMAL 1 E (A**2): 1853 ; 0.200 ; 0.500
REMARK 3 TIGHT THERMAL 1 F (A**2): 1853 ; 0.170 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 2557 ; 1.100 ; 2.000
REMARK 3 MEDIUM THERMAL 1 B (A**2): 2557 ; 1.120 ; 2.000
REMARK 3 MEDIUM THERMAL 1 C (A**2): 2557 ; 0.940 ; 2.000
REMARK 3 MEDIUM THERMAL 1 D (A**2): 2557 ; 1.080 ; 2.000
REMARK 3 MEDIUM THERMAL 1 E (A**2): 2557 ; 1.200 ; 2.000
REMARK 3 MEDIUM THERMAL 1 F (A**2): 2557 ; 1.140 ; 2.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
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: 1. HYDROGENS HAVE BEEN ADDED IN THE
REMARK 3 RIDING POSITIONS. 2. THE DIETHYL PHOSPHONATE (DEP) IS COVALENTALY
REMARK 3 BOUND TO THE SER 188 IN THE ACTIVE SITE OF A, B, C, D, E AND F
REMARK 3 CHAINS. 3. CALCIUM (CA) AND ACETATE (ACT) IONS FROM
REMARK 3 CRYSTALLIZATION CONDITIONS, AND ETHYLENE GLYCOL (EDO) MOLECULES
REMARK 3 FROM CRYO CONDITION ARE MODELLED.
REMARK 4
REMARK 4 3M82 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-MAR-10.
REMARK 100 THE RCSB ID CODE IS RCSB058225.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUN-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.3
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9765
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 94681
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 48.970
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.18000
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 11.5000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.46
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.67400
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MR
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1VLQ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.22
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2000M CAACETATE, 20.0000% PEG-3350,
REMARK 280 NO BUFFER PH 7.3, ADDITIVE: 0.004 M PHENYLMETHYLSULFONYL FLUORIDE
REMARK 280 (PMSF), NANODROP', VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-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 51.78500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 110.80500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.25000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 110.80500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 51.78500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.25000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 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 300 REMARK: AUTHORS STATE THAT SIZE EXCLUSION CHROMATOGRAPHY WITH
REMARK 300 STATIC LIGHT SCATTERING SUPPORTS THE ASSIGNMENT OF A HEXAMER AS A
REMARK 300 SIGNIFICANT OLIGOMERIZATION STATE IN SOLUTION FOR THE UNCOMPLEXED
REMARK 300 PROTEIN.
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: 20760 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 63050 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -165.0 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 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 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 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 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 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 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 22 NZ
REMARK 470 GLU A 81 CD OE1 OE2
REMARK 470 LYS A 126 CE NZ
REMARK 470 GLU B 9 CG CD OE1 OE2
REMARK 470 LYS B 22 NZ
REMARK 470 GLU B 81 CD OE1 OE2
REMARK 470 LYS B 126 CE NZ
REMARK 470 GLU C 9 CG CD OE1 OE2
REMARK 470 LYS C 22 NZ
REMARK 470 GLU C 81 CD OE1 OE2
REMARK 470 LYS C 126 CE NZ
REMARK 470 GLU D 9 CG CD OE1 OE2
REMARK 470 LYS D 22 NZ
REMARK 470 GLU D 81 CD OE1 OE2
REMARK 470 LYS D 126 CE NZ
REMARK 470 GLU E 9 CG CD OE1 OE2
REMARK 470 LYS E 22 NZ
REMARK 470 GLU E 79 CD OE1 OE2
REMARK 470 GLU E 81 CD OE1 OE2
REMARK 470 LYS E 126 CE NZ
REMARK 470 GLU F 9 CG CD OE1 OE2
REMARK 470 LYS F 22 NZ
REMARK 470 GLU F 81 CD OE1 OE2
REMARK 470 LYS F 126 NZ
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 131 CB - CG - OD1 ANGL. DEV. = 5.5 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 GLU A 80 129.85 -38.43
REMARK 500 GLN A 120 -117.64 -97.42
REMARK 500 SEB A 188 -124.09 59.35
REMARK 500 VAL A 211 53.03 34.63
REMARK 500 LEU A 214 36.42 71.80
REMARK 500 ASN A 302 -142.77 -86.47
REMARK 500 GLN B 120 -118.37 -96.88
REMARK 500 PRO B 139 132.19 -38.95
REMARK 500 SEB B 188 -126.09 63.06
REMARK 500 VAL B 211 53.30 36.49
REMARK 500 LEU B 214 35.89 73.19
REMARK 500 ASN B 302 -140.86 -85.13
REMARK 500 ASP C 5 -169.86 -107.57
REMARK 500 GLN C 120 -116.62 -96.37
REMARK 500 SEB C 188 -121.89 61.88
REMARK 500 VAL C 211 52.74 33.18
REMARK 500 LEU C 214 38.15 70.43
REMARK 500 ASN C 302 -143.49 -87.74
REMARK 500 GLN D 120 -117.36 -99.22
REMARK 500 PRO D 142 126.62 -39.98
REMARK 500 SEB D 188 -122.28 61.83
REMARK 500 VAL D 211 51.18 37.85
REMARK 500 LEU D 214 37.41 72.40
REMARK 500 ASN D 302 -141.44 -86.43
REMARK 500 GLN E 120 -118.90 -100.51
REMARK 500 SEB E 188 -126.35 63.29
REMARK 500 VAL E 211 57.05 34.94
REMARK 500 LEU E 214 36.21 73.27
REMARK 500 ASN E 302 -143.55 -87.67
REMARK 500 GLN F 120 -115.51 -97.97
REMARK 500 PRO F 142 124.99 -39.24
REMARK 500 SEB F 188 -124.89 61.69
REMARK 500 VAL F 211 53.74 33.56
REMARK 500 ASN F 302 -139.91 -87.88
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA F 406 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU F 26 OE1
REMARK 620 2 LYS F 22 O 98.7
REMARK 620 3 HOH F 741 O 95.8 73.4
REMARK 620 4 GLU F 26 OE2 48.7 88.4 137.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 404 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU A 26 OE1
REMARK 620 2 LYS A 22 O 97.8
REMARK 620 3 HOH A 576 O 89.6 76.2
REMARK 620 4 GLU A 26 OE2 49.1 85.5 132.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA E 407 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU E 26 OE1
REMARK 620 2 LYS E 22 O 98.6
REMARK 620 3 GLU E 26 OE2 50.2 91.9
REMARK 620 4 HOH E 711 O 80.9 74.7 127.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA A 401 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 448 O
REMARK 620 2 HOH A 477 O 166.1
REMARK 620 3 ASP A 58 OD2 81.8 86.8
REMARK 620 4 GLU A 45 OE1 101.0 88.0 95.7
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 402 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 45 OE1
REMARK 620 2 HOH D 673 O 175.6
REMARK 620 3 ASP D 58 OD2 95.8 85.9
REMARK 620 4 HOH D 712 O 107.4 76.9 81.0
REMARK 620 5 HOH D 520 O 91.9 84.2 82.7 155.8
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA D 405 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 GLU D 26 OE1
REMARK 620 2 LYS D 22 O 83.1
REMARK 620 3 HOH D 582 O 81.4 63.2
REMARK 620 4 GLU D 26 OE2 47.3 128.4 112.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA C 403 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS C 22 O
REMARK 620 2 GLU C 26 OE1 84.3
REMARK 620 3 HOH C 499 O 76.8 84.6
REMARK 620 4 GLU C 26 OE2 125.1 50.5 119.9
REMARK 620 5 HOH C1195 O 77.9 161.9 88.0 145.6
REMARK 620 6 HOH C 885 O 157.8 99.6 81.8 71.3 95.7
REMARK 620 7 HOH C1727 O 67.0 76.8 140.5 72.8 99.0 135.2
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 CA B 408 CA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 LYS B 22 O
REMARK 620 2 HOH B 586 O 72.7
REMARK 620 3 GLU B 26 OE2 110.0 115.0
REMARK 620 4 GLU B 26 OE1 83.5 73.0 44.8
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 404
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 410
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 412
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 413
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 408
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 409
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 414
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 415
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 405
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 407
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT E 411
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 416
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA F 406
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 417
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 281958 RELATED DB: TARGETDB
REMARK 900 RELATED ID: 1VLQ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYL XYLAN ESTERASE (TM0077) FROM
REMARK 900 THERMOTOGA MARITIMA AT 2.10 A RESOLUTION (SELENOMETHIONINE
REMARK 900 SUBSTITUTED STRUCTURE, MONOCLINIC CRYSTAL FORM)
REMARK 900 RELATED ID: 3M81 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYL XYLAN ESTERASE (TM0077) FROM
REMARK 900 THERMOTOGA MARITIMA AT 2.50 A RESOLUTION (NATIVE APO
REMARK 900 STRUCTURE, ORTHORHOMBIC CRYSTAL FORM)
REMARK 900 RELATED ID: 3M83 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF ACETYL XYLAN ESTERASE (TM0077) FROM
REMARK 900 THERMOTOGA MARITIMA AT 2.12 A RESOLUTION (PARAOXON
REMARK 900 INHIBITOR COMPLEX STRUCTURE, ORTHORHOMBIC CRYSTAL FORM)
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHH
REMARK 999 FOLLOWED BY THE TARGET SEQUENCE.
DBREF 3M82 A 1 325 UNP Q9WXT2 Q9WXT2_THEMA 1 325
DBREF 3M82 B 1 325 UNP Q9WXT2 Q9WXT2_THEMA 1 325
DBREF 3M82 C 1 325 UNP Q9WXT2 Q9WXT2_THEMA 1 325
DBREF 3M82 D 1 325 UNP Q9WXT2 Q9WXT2_THEMA 1 325
DBREF 3M82 E 1 325 UNP Q9WXT2 Q9WXT2_THEMA 1 325
DBREF 3M82 F 1 325 UNP Q9WXT2 Q9WXT2_THEMA 1 325
SEQADV 3M82 MET A -11 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 GLY A -10 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 SER A -9 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 ASP A -8 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 LYS A -7 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 ILE A -6 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS A -5 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS A -4 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS A -3 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS A -2 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS A -1 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS A 0 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 MET B -11 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 GLY B -10 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 SER B -9 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 ASP B -8 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 LYS B -7 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 ILE B -6 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS B -5 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS B -4 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS B -3 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS B -2 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS B -1 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS B 0 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 MET C -11 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 GLY C -10 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 SER C -9 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 ASP C -8 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 LYS C -7 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 ILE C -6 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS C -5 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS C -4 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS C -3 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS C -2 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS C -1 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS C 0 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 MET D -11 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 GLY D -10 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 SER D -9 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 ASP D -8 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 LYS D -7 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 ILE D -6 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS D -5 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS D -4 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS D -3 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS D -2 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS D -1 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS D 0 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 MET E -11 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 GLY E -10 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 SER E -9 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 ASP E -8 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 LYS E -7 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 ILE E -6 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS E -5 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS E -4 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS E -3 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS E -2 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS E -1 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS E 0 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 MET F -11 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 GLY F -10 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 SER F -9 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 ASP F -8 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 LYS F -7 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 ILE F -6 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS F -5 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS F -4 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS F -3 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS F -2 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS F -1 UNP Q9WXT2 LEADER SEQUENCE
SEQADV 3M82 HIS F 0 UNP Q9WXT2 LEADER SEQUENCE
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 SEB 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 SEB 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 SEB 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 SEB 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 SEB 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 SEB 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
MODRES 3M82 SEB A 188 SER O-BENZYLSULFONYL-SERINE
MODRES 3M82 SEB B 188 SER O-BENZYLSULFONYL-SERINE
MODRES 3M82 SEB C 188 SER O-BENZYLSULFONYL-SERINE
MODRES 3M82 SEB D 188 SER O-BENZYLSULFONYL-SERINE
MODRES 3M82 SEB E 188 SER O-BENZYLSULFONYL-SERINE
MODRES 3M82 SEB F 188 SER O-BENZYLSULFONYL-SERINE
HET SEB A 188 16
HET SEB B 188 16
HET SEB C 188 16
HET SEB D 188 16
HET SEB E 188 16
HET SEB F 188 16
HET CA A 401 1
HET CA A 404 1
HET ACT A 410 4
HET EDO A 412 4
HET EDO A 413 4
HET CA B 408 1
HET ACT B 409 4
HET EDO B 414 4
HET CA C 403 1
HET EDO C 415 4
HET CA D 402 1
HET CA D 405 1
HET CA E 407 1
HET ACT E 411 4
HET EDO E 416 4
HET CA F 406 1
HET EDO F 417 4
HETNAM SEB O-BENZYLSULFONYL-SERINE
HETNAM CA CALCIUM ION
HETNAM ACT ACETATE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 SEB 6(C10 H13 N O5 S)
FORMUL 7 CA 8(CA 2+)
FORMUL 9 ACT 3(C2 H3 O2 1-)
FORMUL 10 EDO 6(C2 H6 O2)
FORMUL 24 HOH *946(H2 O)
HELIX 1 1 PRO A 7 LYS A 12 1 6
HELIX 2 2 ASP A 23 LYS A 37 1 15
HELIX 3 3 TYR A 64 GLY A 66 5 3
HELIX 4 4 PHE A 98 TRP A 102 5 5
HELIX 5 5 LEU A 103 MET A 108 1 6
HELIX 6 6 TYR A 155 PHE A 174 1 20
HELIX 7 7 SEB A 188 SER A 201 1 14
HELIX 8 8 HIS A 216 VAL A 224 1 9
HELIX 9 9 TYR A 229 HIS A 239 1 11
HELIX 10 10 LYS A 242 TYR A 252 1 11
HELIX 11 11 ASP A 254 ALA A 260 1 7
HELIX 12 12 PRO A 278 TYR A 289 1 12
HELIX 13 13 GLY A 306 GLU A 323 1 18
HELIX 14 14 PRO B 7 LYS B 12 1 6
HELIX 15 15 ASP B 23 LYS B 37 1 15
HELIX 16 16 TYR B 64 GLY B 66 5 3
HELIX 17 17 PHE B 98 TRP B 102 5 5
HELIX 18 18 LEU B 103 MET B 108 1 6
HELIX 19 19 TYR B 155 PHE B 174 1 20
HELIX 20 20 SEB B 188 SER B 201 1 14
HELIX 21 21 HIS B 216 VAL B 224 1 9
HELIX 22 22 TYR B 229 HIS B 239 1 11
HELIX 23 23 LYS B 242 TYR B 252 1 11
HELIX 24 24 ASP B 254 ALA B 260 1 7
HELIX 25 25 PRO B 278 TYR B 289 1 12
HELIX 26 26 GLY B 306 GLU B 323 1 18
HELIX 27 27 PRO C 7 LYS C 12 1 6
HELIX 28 28 ASP C 23 LYS C 37 1 15
HELIX 29 29 TYR C 64 GLY C 66 5 3
HELIX 30 30 PHE C 98 TRP C 102 5 5
HELIX 31 31 LEU C 103 MET C 108 1 6
HELIX 32 32 TYR C 155 PHE C 174 1 20
HELIX 33 33 SEB C 188 SER C 201 1 14
HELIX 34 34 HIS C 216 VAL C 224 1 9
HELIX 35 35 TYR C 229 HIS C 239 1 11
HELIX 36 36 LYS C 242 TYR C 252 1 11
HELIX 37 37 ASP C 254 ALA C 260 1 7
HELIX 38 38 PRO C 278 TYR C 289 1 12
HELIX 39 39 GLY C 306 GLU C 323 1 18
HELIX 40 40 PRO D 7 LYS D 12 1 6
HELIX 41 41 ASP D 23 LYS D 37 1 15
HELIX 42 42 TYR D 64 GLY D 66 5 3
HELIX 43 43 PHE D 98 TRP D 102 5 5
HELIX 44 44 LEU D 103 MET D 108 1 6
HELIX 45 45 TYR D 155 SER D 173 1 19
HELIX 46 46 SEB D 188 SER D 201 1 14
HELIX 47 47 HIS D 216 VAL D 224 1 9
HELIX 48 48 TYR D 229 HIS D 239 1 11
HELIX 49 49 LYS D 242 TYR D 252 1 11
HELIX 50 50 ASP D 254 ALA D 260 1 7
HELIX 51 51 PRO D 278 TYR D 289 1 12
HELIX 52 52 GLY D 306 GLU D 323 1 18
HELIX 53 53 PRO E 7 LYS E 12 1 6
HELIX 54 54 ASP E 23 LYS E 37 1 15
HELIX 55 55 TYR E 64 GLY E 66 5 3
HELIX 56 56 PHE E 98 TRP E 102 5 5
HELIX 57 57 LEU E 103 MET E 108 1 6
HELIX 58 58 TYR E 155 PHE E 174 1 20
HELIX 59 59 SEB E 188 SER E 201 1 14
HELIX 60 60 HIS E 216 VAL E 224 1 9
HELIX 61 61 TYR E 229 HIS E 239 1 11
HELIX 62 62 LYS E 242 TYR E 252 1 11
HELIX 63 63 ASP E 254 ALA E 260 1 7
HELIX 64 64 PRO E 278 TYR E 289 1 12
HELIX 65 65 GLY E 306 GLU E 323 1 18
HELIX 66 66 PRO F 7 LYS F 12 1 6
HELIX 67 67 ASP F 23 LYS F 37 1 15
HELIX 68 68 TYR F 64 GLY F 66 5 3
HELIX 69 69 PHE F 98 TRP F 102 5 5
HELIX 70 70 LEU F 103 MET F 108 1 6
HELIX 71 71 TYR F 155 SER F 173 1 19
HELIX 72 72 SEB F 188 SER F 201 1 14
HELIX 73 73 HIS F 216 VAL F 224 1 9
HELIX 74 74 TYR F 229 HIS F 239 1 11
HELIX 75 75 LYS F 242 TYR F 252 1 11
HELIX 76 76 ASP F 254 ALA F 260 1 7
HELIX 77 77 PRO F 278 TYR F 289 1 12
HELIX 78 78 GLY F 306 PHE F 322 1 17
SHEET 1 A 9 VAL A 43 ARG A 46 0
SHEET 2 A 9 VAL A 54 SER A 62 -1 O ASP A 58 N GLU A 45
SHEET 3 A 9 ARG A 68 PRO A 76 -1 O VAL A 75 N GLU A 55
SHEET 4 A 9 ILE A 111 MET A 115 -1 O VAL A 114 N TRP A 72
SHEET 5 A 9 LEU A 83 GLN A 88 1 N GLN A 88 O PHE A 113
SHEET 6 A 9 VAL A 177 GLY A 187 1 O ASP A 178 N LEU A 83
SHEET 7 A 9 ALA A 206 ASP A 210 1 O ALA A 206 N ILE A 184
SHEET 8 A 9 ALA A 266 GLY A 271 1 O LEU A 267 N CYS A 209
SHEET 9 A 9 LYS A 293 TYR A 298 1 O GLU A 294 N PHE A 268
SHEET 1 B 9 VAL B 43 ARG B 46 0
SHEET 2 B 9 VAL B 54 SER B 62 -1 O ASP B 58 N GLU B 45
SHEET 3 B 9 ARG B 68 PRO B 76 -1 O VAL B 75 N GLU B 55
SHEET 4 B 9 ILE B 111 MET B 115 -1 O VAL B 114 N TRP B 72
SHEET 5 B 9 LEU B 83 GLN B 88 1 N GLN B 88 O PHE B 113
SHEET 6 B 9 VAL B 177 GLY B 187 1 O VAL B 183 N CYS B 85
SHEET 7 B 9 ALA B 206 ASP B 210 1 O ALA B 206 N ILE B 184
SHEET 8 B 9 ALA B 266 GLY B 271 1 O LEU B 267 N CYS B 209
SHEET 9 B 9 LYS B 293 TYR B 298 1 O GLU B 294 N PHE B 268
SHEET 1 C 9 VAL C 43 ARG C 46 0
SHEET 2 C 9 VAL C 54 SER C 62 -1 O ASP C 58 N GLU C 45
SHEET 3 C 9 ARG C 68 PRO C 76 -1 O ILE C 69 N PHE C 61
SHEET 4 C 9 ILE C 111 MET C 115 -1 O VAL C 114 N TRP C 72
SHEET 5 C 9 LEU C 83 GLN C 88 1 N GLN C 88 O PHE C 113
SHEET 6 C 9 VAL C 177 GLY C 187 1 O ASP C 178 N LEU C 83
SHEET 7 C 9 ALA C 206 ASP C 210 1 O ALA C 206 N ILE C 184
SHEET 8 C 9 ALA C 266 GLY C 271 1 O LEU C 267 N CYS C 209
SHEET 9 C 9 LYS C 293 TYR C 298 1 O GLU C 294 N PHE C 268
SHEET 1 D 9 VAL D 43 ARG D 46 0
SHEET 2 D 9 VAL D 54 SER D 62 -1 O ASP D 58 N GLU D 45
SHEET 3 D 9 ARG D 68 PRO D 76 -1 O ILE D 69 N PHE D 61
SHEET 4 D 9 ILE D 111 MET D 115 -1 O VAL D 114 N TRP D 72
SHEET 5 D 9 LEU D 83 GLN D 88 1 N GLN D 88 O PHE D 113
SHEET 6 D 9 VAL D 177 GLY D 187 1 O VAL D 183 N VAL D 87
SHEET 7 D 9 ALA D 206 ASP D 210 1 O ALA D 206 N ILE D 184
SHEET 8 D 9 ALA D 266 GLY D 271 1 O LEU D 267 N CYS D 209
SHEET 9 D 9 LYS D 293 TYR D 298 1 O GLU D 294 N PHE D 268
SHEET 1 E 9 VAL E 43 ARG E 46 0
SHEET 2 E 9 VAL E 54 SER E 62 -1 O ASP E 58 N GLU E 45
SHEET 3 E 9 ARG E 68 PRO E 76 -1 O VAL E 75 N GLU E 55
SHEET 4 E 9 ILE E 111 MET E 115 -1 O CYS E 112 N LEU E 74
SHEET 5 E 9 LEU E 83 GLN E 88 1 N VAL E 86 O ILE E 111
SHEET 6 E 9 VAL E 177 GLY E 187 1 O ASP E 178 N LEU E 83
SHEET 7 E 9 ALA E 206 ASP E 210 1 O ALA E 206 N ILE E 184
SHEET 8 E 9 ALA E 266 GLY E 271 1 O LEU E 267 N CYS E 209
SHEET 9 E 9 LYS E 293 TYR E 298 1 O GLU E 294 N PHE E 268
SHEET 1 F 9 VAL F 43 ARG F 46 0
SHEET 2 F 9 VAL F 54 SER F 62 -1 O ASP F 58 N GLU F 45
SHEET 3 F 9 ARG F 68 PRO F 76 -1 O VAL F 75 N GLU F 55
SHEET 4 F 9 ILE F 111 MET F 115 -1 O VAL F 114 N TRP F 72
SHEET 5 F 9 LEU F 83 GLN F 88 1 N GLN F 88 O PHE F 113
SHEET 6 F 9 VAL F 177 GLY F 187 1 O ASP F 178 N LEU F 83
SHEET 7 F 9 ALA F 206 ASP F 210 1 O LEU F 208 N ILE F 184
SHEET 8 F 9 ALA F 266 GLY F 271 1 O LEU F 267 N CYS F 209
SHEET 9 F 9 LYS F 293 TYR F 298 1 O GLU F 294 N PHE F 268
LINK C GLY A 187 N SEB A 188 1555 1555 1.33
LINK C SEB A 188 N GLN A 189 1555 1555 1.34
LINK C GLY B 187 N SEB B 188 1555 1555 1.34
LINK C SEB B 188 N GLN B 189 1555 1555 1.33
LINK C GLY C 187 N SEB C 188 1555 1555 1.34
LINK C SEB C 188 N GLN C 189 1555 1555 1.34
LINK C GLY D 187 N SEB D 188 1555 1555 1.35
LINK C SEB D 188 N GLN D 189 1555 1555 1.34
LINK C GLY E 187 N SEB E 188 1555 1555 1.33
LINK C SEB E 188 N GLN E 189 1555 1555 1.34
LINK C GLY F 187 N SEB F 188 1555 1555 1.34
LINK C SEB F 188 N GLN F 189 1555 1555 1.33
LINK OE1AGLU F 26 CA CA F 406 1555 1555 2.23
LINK OE1 GLU A 26 CA CA A 404 1555 1555 2.31
LINK OE1AGLU E 26 CA CA E 407 1555 1555 2.31
LINK CA CA A 401 O HOH A 448 1555 1555 2.34
LINK OE1 GLU D 45 CA CA D 402 1555 1555 2.37
LINK CA CA D 402 O HOH D 673 1555 1555 2.40
LINK OD2 ASP D 58 CA CA D 402 1555 1555 2.40
LINK CA CA A 401 O HOH A 477 1555 1555 2.43
LINK OE1 GLU D 26 CA CA D 405 1555 1555 2.43
LINK CA CA D 402 O HOH D 712 1555 1555 2.44
LINK O LYS A 22 CA CA A 404 1555 1555 2.44
LINK O LYS E 22 CA CA E 407 1555 1555 2.44
LINK O LYS C 22 CA CA C 403 1555 1555 2.45
LINK OE1 GLU C 26 CA CA C 403 1555 1555 2.49
LINK O LYS D 22 CA CA D 405 1555 1555 2.50
LINK CA CA D 402 O HOH D 520 1555 1555 2.50
LINK OD2 ASP A 58 CA CA A 401 1555 1555 2.50
LINK OE1 GLU A 45 CA CA A 401 1555 1555 2.54
LINK CA CA C 403 O HOH C 499 1555 1555 2.57
LINK OE2 GLU C 26 CA CA C 403 1555 1555 2.60
LINK O LYS B 22 CA CA B 408 1555 1555 2.63
LINK O LYS F 22 CA CA F 406 1555 1555 2.64
LINK CA CA B 408 O HOH B 586 1555 1555 2.64
LINK CA CA F 406 O HOH F 741 1555 1555 2.66
LINK CA CA C 403 O HOH C1195 1555 1555 2.68
LINK OE2 GLU B 26 CA CA B 408 1555 1555 2.76
LINK OE2AGLU E 26 CA CA E 407 1555 1555 2.79
LINK CA CA D 405 O HOH D 582 1555 1555 2.83
LINK CA CA A 404 O HOH A 576 1555 1555 2.87
LINK OE2 GLU A 26 CA CA A 404 1555 1555 2.89
LINK OE2AGLU F 26 CA CA F 406 1555 1555 2.90
LINK OE2 GLU D 26 CA CA D 405 1555 1555 2.90
LINK CA CA E 407 O HOH E 711 1555 1555 2.93
LINK OE1 GLU B 26 CA CA B 408 1555 1555 2.94
LINK CA CA C 403 O HOH C 885 1555 1555 3.06
LINK CA CA C 403 O HOH C1727 1555 1555 3.18
CISPEP 1 HIS A 227 PRO A 228 0 2.91
CISPEP 2 HIS B 227 PRO B 228 0 0.64
CISPEP 3 HIS C 227 PRO C 228 0 3.30
CISPEP 4 HIS D 227 PRO D 228 0 2.85
CISPEP 5 HIS E 227 PRO E 228 0 0.84
CISPEP 6 HIS F 227 PRO F 228 0 -0.50
SITE 1 AC1 5 GLU A 45 ASP A 58 HOH A 448 HOH A 477
SITE 2 AC1 5 GLU C 45
SITE 1 AC2 3 LYS A 22 GLU A 26 HOH A 576
SITE 1 AC3 9 GLN A 140 PRO A 142 GLY A 143 ARG A 147
SITE 2 AC3 9 GLN C 140 PRO C 142 GLY C 143 PHE C 144
SITE 3 AC3 9 ARG C 147
SITE 1 AC4 5 GLU A 34 TYR A 64 ARG A 65 GLU A 134
SITE 2 AC4 5 HOH A 722
SITE 1 AC5 7 GLN A 88 TRP A 105 GLY A 186 GLY A 187
SITE 2 AC5 7 ASP A 210 GLN A 314 HOH A 726
SITE 1 AC6 3 LYS B 22 GLU B 26 HOH B 586
SITE 1 AC7 10 GLN B 140 PRO B 142 GLY B 143 ARG B 147
SITE 2 AC7 10 HOH B1243 GLN D 140 PRO D 142 GLY D 143
SITE 3 AC7 10 PHE D 144 ARG D 147
SITE 1 AC8 6 GLN B 88 TRP B 105 GLY B 186 GLY B 187
SITE 2 AC8 6 ASP B 210 GLN B 314
SITE 1 AC9 5 LYS C 22 GLU C 26 HOH C 499 HOH C 885
SITE 2 AC9 5 HOH C1195
SITE 1 BC1 6 GLN C 88 TRP C 105 GLY C 186 GLY C 187
SITE 2 BC1 6 ASP C 210 GLN C 314
SITE 1 BC2 6 GLU B 45 GLU D 45 ASP D 58 HOH D 520
SITE 2 BC2 6 HOH D 673 HOH D 712
SITE 1 BC3 3 LYS D 22 GLU D 26 HOH D 582
SITE 1 BC4 3 LYS E 22 GLU E 26 HOH E 711
SITE 1 BC5 9 GLN E 140 PRO E 142 GLY E 143 PHE E 144
SITE 2 BC5 9 ARG E 147 HOH E1544 GLN F 140 GLY F 143
SITE 3 BC5 9 ARG F 147
SITE 1 BC6 6 GLN E 88 TRP E 105 GLY E 186 GLY E 187
SITE 2 BC6 6 ASP E 210 GLN E 314
SITE 1 BC7 3 LYS F 22 GLU F 26 HOH F 741
SITE 1 BC8 7 GLN F 88 TRP F 105 ALA F 185 GLY F 186
SITE 2 BC8 7 GLY F 187 ASP F 210 GLN F 314
CRYST1 103.570 104.500 221.610 90.00 90.00 90.00 P 21 21 21 24
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 0.009655 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009569 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004512 0.00000
TER 2621 GLU A 323
TER 5253 GLU B 323
TER 7865 GLU C 323
TER 10477 GLU D 323
TER 13113 GLU E 323
TER 15735 GLU F 323
MASTER 650 0 23 78 54 0 32 616606 6 190 156
END |