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HEADER HYDROLASE 16-MAY-17 5XMW
TITLE SELENOMETHIONINE-DERIVATED ZHD
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ZEARALENONE LACTONASE;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: BIONECTRIA OCHROLEUCA;
SOURCE 3 ORGANISM_TAXID: 29856;
SOURCE 4 GENE: ZHD101;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS LACTONASE, HYDROLASE, ALPHA-BETA FOLD, ZEARALENONE DEGRADE
EXPDTA X-RAY DIFFRACTION
AUTHOR X.J.HU
REVDAT 1 25-APR-18 5XMW 0
JRNL AUTH Q.QI,W.J.YANG,H.J.ZHOU,D.M.MING,K.L.SUN,T.Y.XU,X.J.HU,H.LV
JRNL TITL THE STRUCTURE OF A COMPLEX OF THE LACTONOHYDROLASE
JRNL TITL 2 ZEARALENONE HYDROLASE WITH THE HYDROLYSIS PRODUCT OF
JRNL TITL 3 ZEARALENONE AT 1.60 ANGSTROM RESOLUTION
JRNL REF ACTA CRYSTALLOGR F STRUCT V. 73 376 2017
JRNL REF 2 BIOL COMMUN
JRNL REFN ESSN 2053-230X
JRNL PMID 28695844
JRNL DOI 10.1107/S2053230X17007713
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 14839
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) : 0.209
REMARK 3 R VALUE (WORKING SET) : 0.208
REMARK 3 FREE R VALUE : 0.236
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 805
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) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.08
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1072
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.34
REMARK 3 BIN R VALUE (WORKING SET) : 0.3010
REMARK 3 BIN FREE R VALUE SET COUNT : 52
REMARK 3 BIN FREE R VALUE : 0.4420
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4117
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 5
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 73.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 75.03
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -7.97000
REMARK 3 B22 (A**2) : 7.57000
REMARK 3 B33 (A**2) : 0.39000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.381
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.277
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.380
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.919
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.923
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4245 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3851 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5808 ; 1.343 ; 1.956
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8946 ; 0.920 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 540 ; 5.408 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 174 ;33.014 ;24.138
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 615 ;12.226 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 20 ;15.215 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 665 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4752 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 836 ; 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): 2160 ; 6.037 ; 7.469
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 2159 ; 6.037 ; 7.467
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2700 ; 8.516 ;11.228
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2701 ; 8.514 ;11.231
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2085 ; 6.856 ; 7.842
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 2085 ; 6.856 ; 7.842
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 3109 ; 9.573 ;11.576
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 17507 ;13.156 ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 17508 ;13.155 ; 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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 1
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 1 267 B 1 267 17046 0.06 0.05
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
REMARK 4
REMARK 4 5XMW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 18-MAY-17.
REMARK 100 THE DEPOSITION ID IS D_1300003798.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-SEP-14
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97869
REMARK 200 MONOCHROMATOR : 0.990
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : AREA DETECTOR
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 V1.0
REMARK 200 DATA SCALING SOFTWARE : HKL-2000 V1.0
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14839
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.010
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 13.60
REMARK 200 R MERGE (I) : 0.13100
REMARK 200 R SYM (I) : NULL
REMARK 200 FOR THE DATA SET : 9.3100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.08
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 14.50
REMARK 200 R MERGE FOR SHELL (I) : 0.51200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHENIX V 1.9
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.07
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.01
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.2 M AMMONIUM DIBASIC PHOSPHATE, 200
REMARK 280 MM KCL, 100 MM IMIDAZOLE, PH 7.4, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
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 36.96200
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 56.52800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 45.08450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 56.52800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.96200
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 45.08450
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 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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1290 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21560 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 ASP A 271
REMARK 465 LYS A 272
REMARK 465 LEU A 273
REMARK 465 ALA A 274
REMARK 465 ALA A 275
REMARK 465 ALA A 276
REMARK 465 LEU A 277
REMARK 465 GLU A 278
REMARK 465 HIS A 279
REMARK 465 HIS A 280
REMARK 465 HIS A 281
REMARK 465 HIS A 282
REMARK 465 HIS A 283
REMARK 465 HIS A 284
REMARK 465 SER B 269
REMARK 465 VAL B 270
REMARK 465 ASP B 271
REMARK 465 LYS B 272
REMARK 465 LEU B 273
REMARK 465 ALA B 274
REMARK 465 ALA B 275
REMARK 465 ALA B 276
REMARK 465 LEU B 277
REMARK 465 GLU B 278
REMARK 465 HIS B 279
REMARK 465 HIS B 280
REMARK 465 HIS B 281
REMARK 465 HIS B 282
REMARK 465 HIS B 283
REMARK 465 HIS B 284
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 OD1 ASP B 31 OH TYR B 245 2.13
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 ARG B 185 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 SER A 62 -129.35 53.07
REMARK 500 SER A 102 -125.97 60.36
REMARK 500 MSE A 241 -117.38 -117.19
REMARK 500 SER A 267 81.02 -69.51
REMARK 500 SER B 62 -123.38 54.96
REMARK 500 LYS B 66 89.42 -69.47
REMARK 500 SER B 102 -125.74 60.62
REMARK 500 LEU B 155 -70.59 -63.44
REMARK 500 MSE B 241 -111.06 -113.11
REMARK 500 SER B 267 89.18 -68.58
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5C8Z RELATED DB: PDB
REMARK 900 5C8Z CONTAINS THE SAME PROTEIN COMPLEXED WITH ZGR
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE STRAIN OF CLONOSTACHYS ROSEA IS DIFFERENT FROM UNP A0A0N9XBU7.
DBREF1 5XMW A 1 264 UNP A0A0N9XBU7_BIOOC
DBREF2 5XMW A A0A0N9XBU7 1 264
DBREF1 5XMW B 1 264 UNP A0A0N9XBU7_BIOOC
DBREF2 5XMW B A0A0N9XBU7 1 264
SEQADV 5XMW ILE A 26 UNP A0A0N9XBU VAL 26 SEE SEQUENCE DETAILS
SEQADV 5XMW ALA A 69 UNP A0A0N9XBU PRO 69 SEE SEQUENCE DETAILS
SEQADV 5XMW ASN A 148 UNP A0A0N9XBU LYS 148 SEE SEQUENCE DETAILS
SEQADV 5XMW LEU A 168 UNP A0A0N9XBU MET 168 SEE SEQUENCE DETAILS
SEQADV 5XMW VAL A 170 UNP A0A0N9XBU ASP 170 SEE SEQUENCE DETAILS
SEQADV 5XMW GLN A 198 UNP A0A0N9XBU LYS 198 SEE SEQUENCE DETAILS
SEQADV 5XMW VAL A 200 UNP A0A0N9XBU LEU 200 SEE SEQUENCE DETAILS
SEQADV 5XMW TRP A 265 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW ASN A 266 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW SER A 267 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW SER A 268 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW SER A 269 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW VAL A 270 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW ASP A 271 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW LYS A 272 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW LEU A 273 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW ALA A 274 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW ALA A 275 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW ALA A 276 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW LEU A 277 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW GLU A 278 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW HIS A 279 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW HIS A 280 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW HIS A 281 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW HIS A 282 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW HIS A 283 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW HIS A 284 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW ILE B 26 UNP A0A0N9XBU VAL 26 SEE SEQUENCE DETAILS
SEQADV 5XMW ALA B 69 UNP A0A0N9XBU PRO 69 SEE SEQUENCE DETAILS
SEQADV 5XMW ASN B 148 UNP A0A0N9XBU LYS 148 SEE SEQUENCE DETAILS
SEQADV 5XMW LEU B 168 UNP A0A0N9XBU MET 168 SEE SEQUENCE DETAILS
SEQADV 5XMW VAL B 170 UNP A0A0N9XBU ASP 170 SEE SEQUENCE DETAILS
SEQADV 5XMW GLN B 198 UNP A0A0N9XBU LYS 198 SEE SEQUENCE DETAILS
SEQADV 5XMW VAL B 200 UNP A0A0N9XBU LEU 200 SEE SEQUENCE DETAILS
SEQADV 5XMW TRP B 265 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW ASN B 266 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW SER B 267 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW SER B 268 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW SER B 269 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW VAL B 270 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW ASP B 271 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW LYS B 272 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW LEU B 273 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW ALA B 274 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW ALA B 275 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW ALA B 276 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW LEU B 277 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW GLU B 278 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW HIS B 279 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW HIS B 280 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW HIS B 281 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW HIS B 282 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW HIS B 283 UNP A0A0N9XBU EXPRESSION TAG
SEQADV 5XMW HIS B 284 UNP A0A0N9XBU EXPRESSION TAG
SEQRES 1 A 284 MSE ARG THR ARG SER THR ILE SER THR PRO ASN GLY ILE
SEQRES 2 A 284 THR TRP TYR TYR GLU GLN GLU GLY THR GLY PRO ASP ILE
SEQRES 3 A 284 VAL LEU VAL PRO ASP GLY LEU GLY GLU CYS GLN MSE PHE
SEQRES 4 A 284 ASP SER SER VAL SER GLN ILE ALA ALA GLN GLY PHE ARG
SEQRES 5 A 284 VAL THR THR PHE ASP MSE PRO GLY MSE SER ARG SER ALA
SEQRES 6 A 284 LYS ALA PRO ALA GLU THR TYR THR GLU VAL THR ALA GLN
SEQRES 7 A 284 LYS LEU ALA SER TYR VAL ILE SER ILE LEU ASP ALA LEU
SEQRES 8 A 284 ASP ILE LYS HIS ALA THR VAL TRP GLY CYS SER SER GLY
SEQRES 9 A 284 ALA SER THR VAL VAL ALA LEU LEU LEU GLY TYR PRO ASP
SEQRES 10 A 284 ARG ILE ARG ASN ALA MSE CYS HIS GLU LEU PRO THR LYS
SEQRES 11 A 284 LEU LEU ASP HIS LEU SER ASN THR ALA VAL LEU GLU ASP
SEQRES 12 A 284 GLU GLU ILE SER ASN ILE LEU ALA ASN VAL MSE LEU ASN
SEQRES 13 A 284 ASP VAL SER GLY GLY SER GLU ALA TRP GLN ALA LEU GLY
SEQRES 14 A 284 VAL GLU VAL HIS ALA ARG LEU HIS LYS ASN TYR PRO VAL
SEQRES 15 A 284 TRP ALA ARG GLY TYR PRO ARG THR ILE PRO PRO SER ALA
SEQRES 16 A 284 PRO VAL GLN ASP VAL GLU ALA LEU ARG GLY LYS PRO LEU
SEQRES 17 A 284 ASP TRP THR VAL GLY ALA ALA THR PRO THR GLU SER PHE
SEQRES 18 A 284 PHE ASP ASN ILE VAL THR ALA THR LYS ALA GLY VAL ASN
SEQRES 19 A 284 ILE GLY LEU LEU PRO GLY MSE HIS PHE PRO TYR VAL SER
SEQRES 20 A 284 HIS PRO ASP VAL PHE ALA LYS TYR VAL VAL GLU THR THR
SEQRES 21 A 284 GLN LYS HIS LEU TRP ASN SER SER SER VAL ASP LYS LEU
SEQRES 22 A 284 ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
SEQRES 1 B 284 MSE ARG THR ARG SER THR ILE SER THR PRO ASN GLY ILE
SEQRES 2 B 284 THR TRP TYR TYR GLU GLN GLU GLY THR GLY PRO ASP ILE
SEQRES 3 B 284 VAL LEU VAL PRO ASP GLY LEU GLY GLU CYS GLN MSE PHE
SEQRES 4 B 284 ASP SER SER VAL SER GLN ILE ALA ALA GLN GLY PHE ARG
SEQRES 5 B 284 VAL THR THR PHE ASP MSE PRO GLY MSE SER ARG SER ALA
SEQRES 6 B 284 LYS ALA PRO ALA GLU THR TYR THR GLU VAL THR ALA GLN
SEQRES 7 B 284 LYS LEU ALA SER TYR VAL ILE SER ILE LEU ASP ALA LEU
SEQRES 8 B 284 ASP ILE LYS HIS ALA THR VAL TRP GLY CYS SER SER GLY
SEQRES 9 B 284 ALA SER THR VAL VAL ALA LEU LEU LEU GLY TYR PRO ASP
SEQRES 10 B 284 ARG ILE ARG ASN ALA MSE CYS HIS GLU LEU PRO THR LYS
SEQRES 11 B 284 LEU LEU ASP HIS LEU SER ASN THR ALA VAL LEU GLU ASP
SEQRES 12 B 284 GLU GLU ILE SER ASN ILE LEU ALA ASN VAL MSE LEU ASN
SEQRES 13 B 284 ASP VAL SER GLY GLY SER GLU ALA TRP GLN ALA LEU GLY
SEQRES 14 B 284 VAL GLU VAL HIS ALA ARG LEU HIS LYS ASN TYR PRO VAL
SEQRES 15 B 284 TRP ALA ARG GLY TYR PRO ARG THR ILE PRO PRO SER ALA
SEQRES 16 B 284 PRO VAL GLN ASP VAL GLU ALA LEU ARG GLY LYS PRO LEU
SEQRES 17 B 284 ASP TRP THR VAL GLY ALA ALA THR PRO THR GLU SER PHE
SEQRES 18 B 284 PHE ASP ASN ILE VAL THR ALA THR LYS ALA GLY VAL ASN
SEQRES 19 B 284 ILE GLY LEU LEU PRO GLY MSE HIS PHE PRO TYR VAL SER
SEQRES 20 B 284 HIS PRO ASP VAL PHE ALA LYS TYR VAL VAL GLU THR THR
SEQRES 21 B 284 GLN LYS HIS LEU TRP ASN SER SER SER VAL ASP LYS LEU
SEQRES 22 B 284 ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 5XMW MSE A 1 MET MODIFIED RESIDUE
MODRES 5XMW MSE A 38 MET MODIFIED RESIDUE
MODRES 5XMW MSE A 58 MET MODIFIED RESIDUE
MODRES 5XMW MSE A 61 MET MODIFIED RESIDUE
MODRES 5XMW MSE A 123 MET MODIFIED RESIDUE
MODRES 5XMW MSE A 154 MET MODIFIED RESIDUE
MODRES 5XMW MSE A 241 MET MODIFIED RESIDUE
MODRES 5XMW MSE B 1 MET MODIFIED RESIDUE
MODRES 5XMW MSE B 38 MET MODIFIED RESIDUE
MODRES 5XMW MSE B 58 MET MODIFIED RESIDUE
MODRES 5XMW MSE B 61 MET MODIFIED RESIDUE
MODRES 5XMW MSE B 123 MET MODIFIED RESIDUE
MODRES 5XMW MSE B 154 MET MODIFIED RESIDUE
MODRES 5XMW MSE B 241 MET MODIFIED RESIDUE
HET MSE A 1 8
HET MSE A 38 8
HET MSE A 58 8
HET MSE A 61 8
HET MSE A 123 8
HET MSE A 154 8
HET MSE A 241 8
HET MSE B 1 8
HET MSE B 38 8
HET MSE B 58 8
HET MSE B 61 8
HET MSE B 123 8
HET MSE B 154 8
HET MSE B 241 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 14(C5 H11 N O2 SE)
FORMUL 3 HOH *5(H2 O)
HELIX 1 AA1 GLU A 35 MSE A 38 5 4
HELIX 2 AA2 PHE A 39 ALA A 48 1 10
HELIX 3 AA3 MSE A 61 ALA A 65 5 5
HELIX 4 AA4 PRO A 68 THR A 73 5 6
HELIX 5 AA5 THR A 76 LEU A 91 1 16
HELIX 6 AA6 SER A 102 TYR A 115 1 14
HELIX 7 AA7 LEU A 132 ASN A 137 1 6
HELIX 8 AA8 GLU A 142 ASP A 157 1 16
HELIX 9 AA9 GLY A 161 ALA A 167 1 7
HELIX 10 AB1 GLY A 169 TYR A 187 1 19
HELIX 11 AB2 ILE A 191 ALA A 195 5 5
HELIX 12 AB3 ASP A 199 ARG A 204 1 6
HELIX 13 AB4 PHE A 221 GLY A 232 1 12
HELIX 14 AB5 PHE A 243 HIS A 248 1 6
HELIX 15 AB6 HIS A 248 SER A 267 1 20
HELIX 16 AB7 GLU B 35 MSE B 38 5 4
HELIX 17 AB8 PHE B 39 ALA B 48 1 10
HELIX 18 AB9 MSE B 61 ALA B 65 5 5
HELIX 19 AC1 PRO B 68 THR B 73 5 6
HELIX 20 AC2 THR B 76 LEU B 91 1 16
HELIX 21 AC3 SER B 102 TYR B 115 1 14
HELIX 22 AC4 LEU B 132 ASN B 137 1 6
HELIX 23 AC5 GLU B 142 ASP B 157 1 16
HELIX 24 AC6 GLY B 161 ALA B 167 1 7
HELIX 25 AC7 GLY B 169 ILE B 191 1 23
HELIX 26 AC8 PRO B 192 ALA B 195 5 4
HELIX 27 AC9 ASP B 199 ARG B 204 1 6
HELIX 28 AD1 PHE B 221 GLY B 232 1 12
HELIX 29 AD2 PHE B 243 HIS B 248 1 6
HELIX 30 AD3 HIS B 248 SER B 267 1 20
SHEET 1 AA1 8 ARG A 2 SER A 8 0
SHEET 2 AA1 8 THR A 14 GLU A 20 -1 O GLN A 19 N THR A 3
SHEET 3 AA1 8 ARG A 52 PHE A 56 -1 O THR A 55 N GLU A 18
SHEET 4 AA1 8 ASP A 25 LEU A 28 1 N LEU A 28 O THR A 54
SHEET 5 AA1 8 ALA A 96 CYS A 101 1 O THR A 97 N VAL A 27
SHEET 6 AA1 8 ILE A 119 HIS A 125 1 O ARG A 120 N ALA A 96
SHEET 7 AA1 8 LEU A 208 GLY A 213 1 O ASP A 209 N ALA A 122
SHEET 8 AA1 8 ASN A 234 LEU A 238 1 O ASN A 234 N TRP A 210
SHEET 1 AA2 8 THR B 3 SER B 8 0
SHEET 2 AA2 8 THR B 14 GLU B 20 -1 O GLN B 19 N THR B 3
SHEET 3 AA2 8 ARG B 52 PHE B 56 -1 O THR B 55 N GLU B 18
SHEET 4 AA2 8 ASP B 25 LEU B 28 1 N LEU B 28 O THR B 54
SHEET 5 AA2 8 ALA B 96 CYS B 101 1 O THR B 97 N VAL B 27
SHEET 6 AA2 8 ILE B 119 HIS B 125 1 O ARG B 120 N ALA B 96
SHEET 7 AA2 8 LEU B 208 GLY B 213 1 O ASP B 209 N ALA B 122
SHEET 8 AA2 8 ASN B 234 LEU B 238 1 O ASN B 234 N TRP B 210
LINK C MSE A 1 N ARG A 2 1555 1555 1.32
LINK C GLN A 37 N MSE A 38 1555 1555 1.33
LINK C MSE A 38 N PHE A 39 1555 1555 1.34
LINK C ASP A 57 N MSE A 58 1555 1555 1.32
LINK C MSE A 58 N PRO A 59 1555 1555 1.33
LINK C GLY A 60 N MSE A 61 1555 1555 1.32
LINK C MSE A 61 N SER A 62 1555 1555 1.32
LINK C ALA A 122 N MSE A 123 1555 1555 1.33
LINK C MSE A 123 N CYS A 124 1555 1555 1.34
LINK C VAL A 153 N MSE A 154 1555 1555 1.32
LINK C MSE A 154 N LEU A 155 1555 1555 1.33
LINK C GLY A 240 N MSE A 241 1555 1555 1.32
LINK C MSE A 241 N HIS A 242 1555 1555 1.31
LINK C MSE B 1 N ARG B 2 1555 1555 1.32
LINK C GLN B 37 N MSE B 38 1555 1555 1.33
LINK C MSE B 38 N PHE B 39 1555 1555 1.33
LINK C ASP B 57 N MSE B 58 1555 1555 1.31
LINK C MSE B 58 N PRO B 59 1555 1555 1.33
LINK C GLY B 60 N MSE B 61 1555 1555 1.32
LINK C MSE B 61 N SER B 62 1555 1555 1.32
LINK C ALA B 122 N MSE B 123 1555 1555 1.33
LINK C MSE B 123 N CYS B 124 1555 1555 1.34
LINK C VAL B 153 N MSE B 154 1555 1555 1.33
LINK C MSE B 154 N LEU B 155 1555 1555 1.33
LINK C GLY B 240 N MSE B 241 1555 1555 1.32
LINK C MSE B 241 N HIS B 242 1555 1555 1.32
CRYST1 73.924 90.169 113.056 90.00 90.00 90.00 P 21 21 21 8
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.013527 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011090 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008845 0.00000
TER 2076 VAL A 270
TER 4139 SER B 268
MASTER 343 0 14 30 16 0 0 6 4122 2 138 44
END |