HEADER MEMBRANE PROTEIN 09-JUN-08 2ZOV
TITLE STRUCTURE OF THE PERIPLASMIC DOMAIN OF MOTB FROM SALMONELLA
TITLE 2 (CRYSTAL FORM I)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CHEMOTAXIS PROTEIN MOTB;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: C-TERMINAL FRAGMENT 1, UNP RESIDUES 88-291;
COMPND 5 SYNONYM: MOTILITY PROTEIN B;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 3 ORGANISM_TAXID: 602;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: PET19B
KEYWDS 2-LAYER SANDWICH, BACTERIAL FLAGELLUM, CELL PROJECTION,
KEYWDS 2 CHEMOTAXIS, FLAGELLAR ROTATION, INNER MEMBRANE, MEMBRANE,
KEYWDS 3 TRANSMEMBRANE, MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR K.IMADA,S.KOJIMA,K.NAMBA,M.HOMMA
REVDAT 2 01-SEP-09 2ZOV 1 JRNL
REVDAT 1 09-JUN-09 2ZOV 0
JRNL AUTH S.KOJIMA,K.IMADA,M.SAKUMA,Y.SUDO,C.KOJIMA,
JRNL AUTH 2 T.MINAMINO,M.HOMMA,K.NAMBA
JRNL TITL STATOR ASSEMBLY AND ACTIVATION MECHANISM OF THE
JRNL TITL 2 FLAGELLAR MOTOR BY THE PERIPLASMIC REGION OF MOTB
JRNL REF MOL.MICROBIOL. V. 73 710 2009
JRNL REFN ISSN 0950-382X
JRNL PMID 19627504
JRNL DOI 10.1111/J.1365-2958.2009.06802.X
REMARK 1
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.1
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.65
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : 1429599.590
REMARK 3 DATA CUTOFF LOW (ABS(F)) : 0.0000
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 99.2
REMARK 3 NUMBER OF REFLECTIONS : 17140
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 SET) : 0.233
REMARK 3 FREE R VALUE : 0.265
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 866
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.009
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.20
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2669
REMARK 3 BIN R VALUE (WORKING SET) : 0.2510
REMARK 3 BIN FREE R VALUE : 0.3140
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.10
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 142
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.026
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1304
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 204
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 20.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 37.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.65000
REMARK 3 B22 (A**2) : -0.65000
REMARK 3 B33 (A**2) : 1.30000
REMARK 3 B12 (A**2) : 2.08000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.25
REMARK 3 ESD FROM SIGMAA (A) : 0.17
REMARK 3 LOW RESOLUTION CUTOFF (A) : 5.00
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : 0.30
REMARK 3 ESD FROM C-V SIGMAA (A) : 0.20
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.006
REMARK 3 BOND ANGLES (DEGREES) : 1.30
REMARK 3 DIHEDRAL ANGLES (DEGREES) : 24.20
REMARK 3 IMPROPER ANGLES (DEGREES) : 0.77
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : RESTRAINED
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : 1.710 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE (A**2) : 2.830 ; 2.000
REMARK 3 SIDE-CHAIN BOND (A**2) : 2.420 ; 2.000
REMARK 3 SIDE-CHAIN ANGLE (A**2) : 3.560 ; 2.500
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : FLAT MODEL
REMARK 3 KSOL : 0.34
REMARK 3 BSOL : 65.91
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 1 : PROTEIN.TOP
REMARK 3 TOPOLOGY FILE 2 : WATER.TOP
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 2ZOV COMPLIES WITH FORMAT V. 3.20, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-JUN-08.
REMARK 100 THE RCSB ID CODE IS RCSB028239.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-APR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SPRING-8
REMARK 200 BEAMLINE : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979101,0.979397,0.9730,
REMARK 200 0.9860
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17162
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 33.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 9.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06500
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 22.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.4
REMARK 200 DATA REDUNDANCY IN SHELL : 9.60
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.26000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 8.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: MAD
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD
REMARK 200 SOFTWARE USED: SOLVE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.27
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 6% PEG 4000, 0.1M ACETATE, 0.22M
REMARK 280 ZN(OAC)2, PH 4.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE
REMARK 280 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 29.30667
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 14.65333
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 14.65333
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 29.30667
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: 2960 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15910 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 KCAL/MOL
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 350 BIOMT1 2 -0.500000 0.866025 0.000000 0.00000
REMARK 350 BIOMT2 2 0.866025 0.500000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 43.96000
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 GLY A 88
REMARK 465 ASP A 89
REMARK 465 ASP A 90
REMARK 465 TYR A 91
REMARK 465 THR A 92
REMARK 465 GLN A 93
REMARK 465 GLN A 94
REMARK 465 GLN A 95
REMARK 465 GLY A 96
REMARK 465 GLU A 97
REMARK 465 VAL A 98
REMARK 465 GLU A 99
REMARK 465 LYS A 100
REMARK 465 GLN A 101
REMARK 465 PRO A 102
REMARK 465 ASN A 103
REMARK 465 ILE A 104
REMARK 465 ASP A 105
REMARK 465 GLU A 106
REMARK 465 LEU A 107
REMARK 465 MSE A 246
REMARK 465 ARG A 247
REMARK 465 LEU A 248
REMARK 465 SER A 249
REMARK 465 ASP A 250
REMARK 465 ARG A 251
REMARK 465 GLY A 252
REMARK 465 PRO A 253
REMARK 465 ASP A 254
REMARK 465 ASN A 283
REMARK 465 GLU A 284
REMARK 465 PRO A 285
REMARK 465 VAL A 286
REMARK 465 SER A 287
REMARK 465 VAL A 288
REMARK 465 LEU A 289
REMARK 465 GLN A 290
REMARK 465 GLN A 291
REMARK 465 HIS A 292
REMARK 465 HIS A 293
REMARK 465 HIS A 294
REMARK 465 HIS A 295
REMARK 465 HIS A 296
REMARK 465 HIS A 297
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH A 298 O HOH A 355 2.07
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 368 O HOH A 368 4555 1.36
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 PRO A 201 130.26 -38.55
REMARK 500 ASN A 204 -150.51 71.15
REMARK 500 GLU A 206 115.00 -169.08
REMARK 500 LYS A 207 55.11 -109.17
REMARK 500 SER A 210 -169.26 -124.53
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 391 DISTANCE = 6.46 ANGSTROMS
REMARK 525 HOH A 395 DISTANCE = 7.40 ANGSTROMS
REMARK 525 HOH A 415 DISTANCE = 5.53 ANGSTROMS
REMARK 525 HOH A 461 DISTANCE = 7.55 ANGSTROMS
REMARK 525 HOH A 465 DISTANCE = 5.37 ANGSTROMS
REMARK 525 HOH A 492 DISTANCE = 6.33 ANGSTROMS
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2ZVY RELATED DB: PDB
REMARK 900 RELATED ID: 2ZVZ RELATED DB: PDB
DBREF 2ZOV A 88 291 UNP P55892 MOTB_SALTY 88 291
SEQADV 2ZOV HIS A 292 UNP P55892 EXPRESSION TAG
SEQADV 2ZOV HIS A 293 UNP P55892 EXPRESSION TAG
SEQADV 2ZOV HIS A 294 UNP P55892 EXPRESSION TAG
SEQADV 2ZOV HIS A 295 UNP P55892 EXPRESSION TAG
SEQADV 2ZOV HIS A 296 UNP P55892 EXPRESSION TAG
SEQADV 2ZOV HIS A 297 UNP P55892 EXPRESSION TAG
SEQRES 1 A 210 GLY ASP ASP TYR THR GLN GLN GLN GLY GLU VAL GLU LYS
SEQRES 2 A 210 GLN PRO ASN ILE ASP GLU LEU LYS LYS ARG MSE GLU GLN
SEQRES 3 A 210 SER ARG LEU ASN LYS LEU ARG GLY ASP LEU ASP GLN LEU
SEQRES 4 A 210 ILE GLU SER ASP PRO LYS LEU ARG ALA LEU ARG PRO HIS
SEQRES 5 A 210 LEU LYS ILE ASP LEU VAL GLN GLU GLY LEU ARG ILE GLN
SEQRES 6 A 210 ILE ILE ASP SER GLN ASN ARG PRO MSE PHE LYS THR GLY
SEQRES 7 A 210 SER ALA GLU VAL GLU PRO TYR MSE ARG ASP ILE LEU ARG
SEQRES 8 A 210 ALA ILE ALA PRO VAL LEU ASN GLY ILE PRO ASN ARG ILE
SEQRES 9 A 210 SER LEU ALA GLY HIS THR ASP ASP PHE PRO TYR ALA ASN
SEQRES 10 A 210 GLY GLU LYS GLY TYR SER ASN TRP GLU LEU SER ALA ASP
SEQRES 11 A 210 ARG ALA ASN ALA SER ARG ARG GLU LEU VAL ALA GLY GLY
SEQRES 12 A 210 LEU ASP ASN GLY LYS VAL LEU ARG VAL VAL GLY MSE ALA
SEQRES 13 A 210 ALA THR MSE ARG LEU SER ASP ARG GLY PRO ASP ASP ALA
SEQRES 14 A 210 ILE ASN ARG ARG ILE SER LEU LEU VAL LEU ASN LYS GLN
SEQRES 15 A 210 ALA GLU GLN ALA ILE LEU HIS GLU ASN ALA GLU SER GLN
SEQRES 16 A 210 ASN GLU PRO VAL SER VAL LEU GLN GLN HIS HIS HIS HIS
SEQRES 17 A 210 HIS HIS
MODRES 2ZOV MSE A 111 MET SELENOMETHIONINE
MODRES 2ZOV MSE A 161 MET SELENOMETHIONINE
MODRES 2ZOV MSE A 173 MET SELENOMETHIONINE
MODRES 2ZOV MSE A 242 MET SELENOMETHIONINE
HET MSE A 111 8
HET MSE A 161 8
HET MSE A 173 8
HET MSE A 242 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 4(C5 H11 N O2 SE)
FORMUL 2 HOH *204(H2 O)
HELIX 1 1 LYS A 108 ASP A 130 1 23
HELIX 2 2 ASP A 130 ARG A 137 1 8
HELIX 3 3 GLU A 170 ASN A 185 1 16
HELIX 4 4 SER A 210 GLY A 229 1 20
HELIX 5 5 ASN A 267 ALA A 279 1 13
SHEET 1 A 5 LEU A 140 VAL A 145 0
SHEET 2 A 5 GLY A 148 ILE A 154 -1 O GLY A 148 N VAL A 145
SHEET 3 A 5 ASN A 258 LEU A 266 -1 O VAL A 265 N LEU A 149
SHEET 4 A 5 ILE A 191 ASP A 198 -1 N ALA A 194 O SER A 262
SHEET 5 A 5 VAL A 236 MSE A 242 1 O VAL A 240 N GLY A 195
LINK C ARG A 110 N MSE A 111 1555 1555 1.33
LINK C MSE A 111 N GLU A 112 1555 1555 1.33
LINK C PRO A 160 N MSE A 161 1555 1555 1.33
LINK C MSE A 161 N PHE A 162 1555 1555 1.33
LINK C TYR A 172 N MSE A 173 1555 1555 1.33
LINK C MSE A 173 N ARG A 174 1555 1555 1.33
LINK C GLY A 241 N MSE A 242 1555 1555 1.33
LINK C MSE A 242 N ALA A 243 1555 1555 1.33
CRYST1 99.740 99.740 43.960 90.00 90.00 120.00 P 32 2 1 6
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 0.010026 0.005789 0.000000 0.00000
SCALE2 0.000000 0.011577 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022748 0.00000
(ATOM LINES ARE NOT SHOWN.)
END