HEADER VIRAL PROTEIN 30-AUG-07 2Z83
TITLE CRYSTAL STRUCTURE OF CATALYTIC DOMAIN OF JAPANESE ENCEPHALITIS VIRUS
TITLE 2 NS3 HELICASE/NUCLEOSIDE TRIPHOSPHATASE AT A RESOLUTION 1.8
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HELICASE/NUCLEOSIDE TRIPHOSPHATASE;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 167-624;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: JAPANESE ENCEPHALITIS VIRUS;
SOURCE 3 ORGANISM_TAXID: 11072;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET21A
KEYWDS HELICASE, HYDROLASE, MEMBRANE, NUCLEOTIDE-BINDING, RNA REPLICATION,
KEYWDS 2 TRANSMEMBRANE, VIRAL PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR T.YAMASHITA
REVDAT 3 01-NOV-23 2Z83 1 SEQADV
REVDAT 2 24-FEB-09 2Z83 1 VERSN
REVDAT 1 04-MAR-08 2Z83 0
JRNL AUTH T.YAMASHITA,H.UNNO,Y.MORI,H.TANI,K.MORIISHI,A.TAKAMIZAWA,
JRNL AUTH 2 M.AGOH,T.TSUKIHARA,Y.MATSUURA
JRNL TITL CRYSTAL STRUCTURE OF CATALYTIC DOMAIN OF JAPANESE
JRNL TITL 2 ENCEPHALITIS VIRUS NS3 HELICASE/NUCLEOSIDE TRIPHOSPHATASE AT
JRNL TITL 3 A RESOLUTION 1.8
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.41
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 40575
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.249
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2154
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2981
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.56
REMARK 3 BIN R VALUE (WORKING SET) : 0.2320
REMARK 3 BIN FREE R VALUE SET COUNT : 152
REMARK 3 BIN FREE R VALUE : 0.2770
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3364
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 411
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 41.90
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.39
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.01000
REMARK 3 B22 (A**2) : 0.01000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.03000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.141
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.139
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.095
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.955
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.960
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3437 ; 0.016 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4655 ; 1.592 ; 1.952
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 422 ; 6.354 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 161 ;38.176 ;23.540
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 589 ;15.446 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;16.151 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 507 ; 0.114 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2618 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1738 ; 0.232 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2353 ; 0.314 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 384 ; 0.210 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 51 ; 0.204 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 23 ; 0.168 ; 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): 2173 ; 1.269 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3417 ; 2.128 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1441 ; 3.022 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1238 ; 4.860 ; 4.500
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 : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 2Z83 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-SEP-07.
REMARK 100 THE DEPOSITION ID IS D_1000027639.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-OCT-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL44XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : BRUKER DIP-6040
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40575
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 32.410
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
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: 2BHR
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.60
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15 % ETHANOL, 100MM TRIS-HCL PH 7.0,
REMARK 280 4% PENTAERYTHRITOL ETOXYLATE (3/4 EO/OH), VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
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 34.01200
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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
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 167
REMARK 465 ALA A 168
REMARK 465 SER A 169
REMARK 465 MET A 170
REMARK 465 THR A 171
REMARK 465 GLY A 172
REMARK 465 GLY A 173
REMARK 465 GLN A 174
REMARK 465 GLN A 175
REMARK 465 MET A 176
REMARK 465 GLY A 177
REMARK 465 ARG A 178
REMARK 465 GLY A 179
REMARK 465 SER A 180
REMARK 465 SER A 246
REMARK 465 ALA A 247
REMARK 465 VAL A 248
REMARK 465 GLN A 249
REMARK 465 ARG A 250
REMARK 465 GLU A 251
REMARK 465 HIS A 252
REMARK 465 GLN A 253
REMARK 465 ARG A 275
REMARK 465 GLU A 413
REMARK 465 MET A 414
REMARK 465 GLY A 415
REMARK 465 ARG A 619
REMARK 465 HIS A 620
REMARK 465 HIS A 621
REMARK 465 HIS A 622
REMARK 465 HIS A 623
REMARK 465 HIS A 624
REMARK 465 HIS A 625
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 NH1 ARG A 427 OH TYR A 473 1.45
REMARK 500 O THR A 225 O HOH A 1034 1.62
REMARK 500 O HOH A 686 O HOH A 780 1.89
REMARK 500 OD2 ASP A 291 O HOH A 1027 2.03
REMARK 500 OG1 THR A 323 O HOH A 731 2.14
REMARK 500 O PRO A 327 NH2 ARG A 459 2.16
REMARK 500 O HOH A 661 O HOH A 1005 2.17
REMARK 500 O LEU A 505 O HOH A 992 2.17
REMARK 500 O HOH A 761 O HOH A 987 2.17
REMARK 500 O HOH A 708 O HOH A 792 2.18
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 A 459 NE - CZ - NH1 ANGL. DEV. = 8.2 DEGREES
REMARK 500 ARG A 459 NE - CZ - NH2 ANGL. DEV. = -8.6 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 LYS A 186 152.61 -49.33
REMARK 500 THR A 316 144.43 -175.77
REMARK 500 ASN A 387 -117.96 -128.22
REMARK 500 SER A 390 -93.64 -47.89
REMARK 500 ASP A 392 -110.23 -103.21
REMARK 500 ILE A 411 105.61 23.34
REMARK 500 GLU A 437 -88.11 -47.14
REMARK 500 ASP A 483 33.17 -143.50
REMARK 500 LYS A 593 74.36 -150.55
REMARK 500
REMARK 500 REMARK: NULL
DBREF 2Z83 A 181 619 UNP Q5NT71 Q5NT71_9FLAV 1685 2123
SEQADV 2Z83 MET A 167 UNP Q5NT71 EXPRESSION TAG
SEQADV 2Z83 ALA A 168 UNP Q5NT71 EXPRESSION TAG
SEQADV 2Z83 SER A 169 UNP Q5NT71 EXPRESSION TAG
SEQADV 2Z83 MET A 170 UNP Q5NT71 EXPRESSION TAG
SEQADV 2Z83 THR A 171 UNP Q5NT71 EXPRESSION TAG
SEQADV 2Z83 GLY A 172 UNP Q5NT71 EXPRESSION TAG
SEQADV 2Z83 GLY A 173 UNP Q5NT71 EXPRESSION TAG
SEQADV 2Z83 GLN A 174 UNP Q5NT71 EXPRESSION TAG
SEQADV 2Z83 GLN A 175 UNP Q5NT71 EXPRESSION TAG
SEQADV 2Z83 MET A 176 UNP Q5NT71 EXPRESSION TAG
SEQADV 2Z83 GLY A 177 UNP Q5NT71 EXPRESSION TAG
SEQADV 2Z83 ARG A 178 UNP Q5NT71 EXPRESSION TAG
SEQADV 2Z83 GLY A 179 UNP Q5NT71 EXPRESSION TAG
SEQADV 2Z83 SER A 180 UNP Q5NT71 EXPRESSION TAG
SEQADV 2Z83 HIS A 620 UNP Q5NT71 EXPRESSION TAG
SEQADV 2Z83 HIS A 621 UNP Q5NT71 EXPRESSION TAG
SEQADV 2Z83 HIS A 622 UNP Q5NT71 EXPRESSION TAG
SEQADV 2Z83 HIS A 623 UNP Q5NT71 EXPRESSION TAG
SEQADV 2Z83 HIS A 624 UNP Q5NT71 EXPRESSION TAG
SEQADV 2Z83 HIS A 625 UNP Q5NT71 EXPRESSION TAG
SEQRES 1 A 459 MET ALA SER MET THR GLY GLY GLN GLN MET GLY ARG GLY
SEQRES 2 A 459 SER PRO ASN MET LEU ARG LYS ARG GLN MET THR VAL LEU
SEQRES 3 A 459 ASP LEU HIS PRO GLY SER GLY LYS THR ARG LYS ILE LEU
SEQRES 4 A 459 PRO GLN ILE ILE LYS ASP ALA ILE GLN GLN ARG LEU ARG
SEQRES 5 A 459 THR ALA VAL LEU ALA PRO THR ARG VAL VAL ALA ALA GLU
SEQRES 6 A 459 MET ALA GLU ALA LEU ARG GLY LEU PRO VAL ARG TYR GLN
SEQRES 7 A 459 THR SER ALA VAL GLN ARG GLU HIS GLN GLY ASN GLU ILE
SEQRES 8 A 459 VAL ASP VAL MET CYS HIS ALA THR LEU THR HIS ARG LEU
SEQRES 9 A 459 MET SER PRO ASN ARG VAL PRO ASN TYR ASN LEU PHE VAL
SEQRES 10 A 459 MET ASP GLU ALA HIS PHE THR ASP PRO ALA SER ILE ALA
SEQRES 11 A 459 ALA ARG GLY TYR ILE ALA THR LYS VAL GLU LEU GLY GLU
SEQRES 12 A 459 ALA ALA ALA ILE PHE MET THR ALA THR PRO PRO GLY THR
SEQRES 13 A 459 THR ASP PRO PHE PRO ASP SER ASN ALA PRO ILE HIS ASP
SEQRES 14 A 459 LEU GLN ASP GLU ILE PRO ASP ARG ALA TRP SER SER GLY
SEQRES 15 A 459 TYR GLU TRP ILE THR GLU TYR ALA GLY LYS THR VAL TRP
SEQRES 16 A 459 PHE VAL ALA SER VAL LYS MET GLY ASN GLU ILE ALA MET
SEQRES 17 A 459 CYS LEU GLN ARG ALA GLY LYS LYS VAL ILE GLN LEU ASN
SEQRES 18 A 459 ARG LYS SER TYR ASP THR GLU TYR PRO LYS CYS LYS ASN
SEQRES 19 A 459 GLY ASP TRP ASP PHE VAL ILE THR THR ASP ILE SER GLU
SEQRES 20 A 459 MET GLY ALA ASN PHE GLY ALA SER ARG VAL ILE ASP CYS
SEQRES 21 A 459 ARG LYS SER VAL LYS PRO THR ILE LEU GLU GLU GLY GLU
SEQRES 22 A 459 GLY ARG VAL ILE LEU GLY ASN PRO SER PRO ILE THR SER
SEQRES 23 A 459 ALA SER ALA ALA GLN ARG ARG GLY ARG VAL GLY ARG ASN
SEQRES 24 A 459 PRO ASN GLN VAL GLY ASP GLU TYR HIS TYR GLY GLY ALA
SEQRES 25 A 459 THR SER GLU ASP ASP SER ASN LEU ALA HIS TRP THR GLU
SEQRES 26 A 459 ALA LYS ILE MET LEU ASP ASN ILE HIS MET PRO ASN GLY
SEQRES 27 A 459 LEU VAL ALA GLN LEU TYR GLY PRO GLU ARG GLU LYS ALA
SEQRES 28 A 459 PHE THR MET ASP GLY GLU TYR ARG LEU ARG GLY GLU GLU
SEQRES 29 A 459 LYS LYS ASN PHE LEU GLU LEU LEU ARG THR ALA ASP LEU
SEQRES 30 A 459 PRO VAL TRP LEU ALA TYR LYS VAL ALA SER ASN GLY ILE
SEQRES 31 A 459 GLN TYR THR ASP ARG LYS TRP CYS PHE ASP GLY PRO ARG
SEQRES 32 A 459 THR ASN ALA ILE LEU GLU ASP ASN ILE GLU VAL GLU ILE
SEQRES 33 A 459 VAL THR ARG MET GLY GLU ARG LYS ILE LEU LYS PRO ARG
SEQRES 34 A 459 TRP LEU ASP ALA ARG VAL TYR ALA ASP HIS GLN ALA LEU
SEQRES 35 A 459 LYS TRP PHE LYS ASP PHE ALA ALA GLY LYS ARG HIS HIS
SEQRES 36 A 459 HIS HIS HIS HIS
FORMUL 2 HOH *411(H2 O)
HELIX 1 1 PRO A 181 ARG A 185 5 5
HELIX 2 2 LYS A 203 GLN A 215 1 13
HELIX 3 3 THR A 225 LEU A 236 1 12
HELIX 4 4 HIS A 263 SER A 272 1 10
HELIX 5 5 ASP A 291 LEU A 307 1 17
HELIX 6 6 TYR A 349 TYR A 355 1 7
HELIX 7 7 SER A 365 ALA A 379 1 15
HELIX 8 8 GLU A 394 CYS A 398 5 5
HELIX 9 9 THR A 451 GLY A 460 1 10
HELIX 10 10 LEU A 486 ASN A 498 1 13
HELIX 11 11 TYR A 510 ALA A 517 5 8
HELIX 12 12 ARG A 527 THR A 540 1 14
HELIX 13 13 PRO A 544 ASN A 554 1 11
HELIX 14 14 ARG A 561 PHE A 565 5 5
HELIX 15 15 PRO A 568 ALA A 572 5 5
HELIX 16 16 ARG A 600 ALA A 603 5 4
HELIX 17 17 ASP A 604 GLY A 617 1 14
SHEET 1 A 6 MET A 189 LEU A 192 0
SHEET 2 A 6 ALA A 311 MET A 315 1 O ALA A 312 N THR A 190
SHEET 3 A 6 LEU A 281 MET A 284 1 N MET A 284 O MET A 315
SHEET 4 A 6 THR A 219 ALA A 223 1 N LEU A 222 O VAL A 283
SHEET 5 A 6 VAL A 258 CYS A 262 1 O ASP A 259 N VAL A 221
SHEET 6 A 6 VAL A 241 TYR A 243 1 N ARG A 242 O VAL A 258
SHEET 1 B 6 ILE A 333 GLN A 337 0
SHEET 2 B 6 ASP A 471 TYR A 475 1 O TYR A 473 N LEU A 336
SHEET 3 B 6 ARG A 422 ASP A 425 1 N VAL A 423 O HIS A 474
SHEET 4 B 6 THR A 359 PHE A 362 1 N PHE A 362 O ILE A 424
SHEET 5 B 6 PHE A 405 THR A 408 1 O VAL A 406 N TRP A 361
SHEET 6 B 6 VAL A 383 LEU A 386 1 N ILE A 384 O ILE A 407
SHEET 1 C 2 LYS A 428 SER A 429 0
SHEET 2 C 2 SER A 448 PRO A 449 -1 O SER A 448 N SER A 429
SHEET 1 D 3 PRO A 432 LEU A 435 0
SHEET 2 D 3 ARG A 441 LEU A 444 -1 O ARG A 441 N LEU A 435
SHEET 3 D 3 LEU A 597 ASP A 598 1 O LEU A 597 N VAL A 442
SHEET 1 E 2 LEU A 574 GLU A 575 0
SHEET 2 E 2 ILE A 578 GLU A 579 -1 O ILE A 578 N GLU A 575
SHEET 1 F 2 GLU A 581 VAL A 583 0
SHEET 2 F 2 ARG A 589 ILE A 591 -1 O LYS A 590 N ILE A 582
CRYST1 59.062 68.024 65.219 90.00 116.87 90.00 P 1 21 1 2
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 0.016931 0.000000 0.008579 0.00000
SCALE2 0.000000 0.014701 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017189 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
