HEADER CHAPERONE 12-AUG-11 3TEE
TITLE CRYSTAL STRUCTURE OF SALMONELLA FLGA IN OPEN FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLAGELLA BASAL BODY P-RING FORMATION PROTEIN FLGA;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: FLAGELLAR FLGA PROTEIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;
SOURCE 3 ORGANISM_TAXID: 90371;
SOURCE 4 STRAIN: SJW1103;
SOURCE 5 GENE: FLGA;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET22B
KEYWDS CHAPERONE, FLAGELLAR P-RING FORMATION, FLAGELLAR FLGI PROTEIN,
KEYWDS 2 PERIPLASMIC PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR H.MATSUNAMI,F.A.SAMATEY,K.NAMBA
REVDAT 2 06-JUL-16 3TEE 1 JRNL
REVDAT 1 15-AUG-12 3TEE 0
JRNL AUTH H.MATSUNAMI,Y.H.YOON,V.A.MESHCHERYAKOV,K.NAMBA,F.A.SAMATEY
JRNL TITL STRUCTURAL FLEXIBILITY OF THE PERIPLASMIC PROTEIN, FLGA,
JRNL TITL 2 REGULATES FLAGELLAR P-RING ASSEMBLY IN SALMONELLA ENTERICA
JRNL REF SCI REP V. 6 27399 2016
JRNL REFN ESSN 2045-2322
JRNL PMID 27273476
JRNL DOI 10.1038/SREP27399
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.8.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 25665
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) : 0.201
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.070
REMARK 3 FREE R VALUE TEST SET COUNT : 1302
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 13
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.03
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2864
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2096
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2725
REMARK 3 BIN R VALUE (WORKING SET) : 0.2091
REMARK 3 BIN FREE R VALUE : 0.2184
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.85
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 139
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1555
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 31
REMARK 3 SOLVENT ATOMS : 166
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 38.42
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 50.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -9.21120
REMARK 3 B22 (A**2) : 5.90510
REMARK 3 B33 (A**2) : 3.30620
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.255
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.924
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 1599 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 2162 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 564 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 47 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 227 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 1599 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 211 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 1908 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.06
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.19
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.75
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 14.6614 36.0775 15.3626
REMARK 3 T TENSOR
REMARK 3 T11: -0.2565 T22: -0.2856
REMARK 3 T33: -0.2787 T12: 0.0377
REMARK 3 T13: -0.0783 T23: -0.0599
REMARK 3 L TENSOR
REMARK 3 L11: 0.4791 L22: 0.5702
REMARK 3 L33: 0.1765 L12: -0.3443
REMARK 3 L13: 0.0878 L23: -0.2655
REMARK 3 S TENSOR
REMARK 3 S11: 0.0410 S12: 0.0282 S13: -0.1577
REMARK 3 S21: -0.0199 S22: 0.1098 S23: -0.0633
REMARK 3 S31: 0.1035 S32: 0.0295 S33: -0.1508
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3TEE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-AUG-11.
REMARK 100 THE RCSB ID CODE IS RCSB067378.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-JUN-07; 27-JUN-07
REMARK 200 TEMPERATURE (KELVIN) : 100; 100
REMARK 200 PH : 5.4
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y; Y
REMARK 200 RADIATION SOURCE : SPRING-8; SPRING-8
REMARK 200 BEAMLINE : BL41XU; BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL; NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M; M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9830; 1.07153, 1.07188, 1.09074
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL MONOCHROMATOR;
REMARK 200 DOUBLE-CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL; NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD; CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315; ADSC QUANTUM
REMARK 200 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25669
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 34.580
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.37200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; 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 (%): 66.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.70
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 2000, 0.8M LITHIUM CHLORIDE,
REMARK 280 0.05M CITRIC ACID, 18% GLYCEROL, PH 5.4, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y+1/2,-Z
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 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 53.76000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 65.88500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 53.76000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 65.88500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 53.76000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 65.88500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 53.76000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 65.88500
REMARK 290 SMTRY3 8 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 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 THR A 44
REMARK 465 GLY A 45
REMARK 465 SER A 46
REMARK 465 ALA A 47
REMARK 465 ASP A 199
REMARK 465 PRO A 200
REMARK 465 ASN A 201
REMARK 465 HIS A 214
REMARK 465 HIS A 215
REMARK 465 HIS A 216
REMARK 465 HIS A 217
REMARK 465 HIS A 218
REMARK 465 HIS A 219
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CHIRAL CENTERS
REMARK 500
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)
REMARK 500
REMARK 500 M RES CSSEQI IMPROPER EXPECTED FOUND DETAILS
REMARK 500 ILE A 115 24.3 L L OUTSIDE RANGE
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 378 DISTANCE = 5.97 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 401
DBREF 3TEE A 1 198 UNP P40131 FLGA_SALTY 22 219
SEQADV 3TEE ASP A 199 UNP P40131 EXPRESSION TAG
SEQADV 3TEE PRO A 200 UNP P40131 EXPRESSION TAG
SEQADV 3TEE ASN A 201 UNP P40131 EXPRESSION TAG
SEQADV 3TEE SER A 202 UNP P40131 EXPRESSION TAG
SEQADV 3TEE SER A 203 UNP P40131 EXPRESSION TAG
SEQADV 3TEE SER A 204 UNP P40131 EXPRESSION TAG
SEQADV 3TEE VAL A 205 UNP P40131 EXPRESSION TAG
SEQADV 3TEE ASP A 206 UNP P40131 EXPRESSION TAG
SEQADV 3TEE LYS A 207 UNP P40131 EXPRESSION TAG
SEQADV 3TEE LEU A 208 UNP P40131 EXPRESSION TAG
SEQADV 3TEE ALA A 209 UNP P40131 EXPRESSION TAG
SEQADV 3TEE ALA A 210 UNP P40131 EXPRESSION TAG
SEQADV 3TEE ALA A 211 UNP P40131 EXPRESSION TAG
SEQADV 3TEE LEU A 212 UNP P40131 EXPRESSION TAG
SEQADV 3TEE GLU A 213 UNP P40131 EXPRESSION TAG
SEQADV 3TEE HIS A 214 UNP P40131 EXPRESSION TAG
SEQADV 3TEE HIS A 215 UNP P40131 EXPRESSION TAG
SEQADV 3TEE HIS A 216 UNP P40131 EXPRESSION TAG
SEQADV 3TEE HIS A 217 UNP P40131 EXPRESSION TAG
SEQADV 3TEE HIS A 218 UNP P40131 EXPRESSION TAG
SEQADV 3TEE HIS A 219 UNP P40131 EXPRESSION TAG
SEQRES 1 A 219 GLN ASP ILE ASN ALA GLN LEU THR THR TRP PHE SER GLN
SEQRES 2 A 219 ARG LEU ALA GLY PHE SER ASP GLU VAL VAL VAL THR LEU
SEQRES 3 A 219 ARG SER SER PRO ASN LEU LEU PRO SER CYS GLU GLN PRO
SEQRES 4 A 219 ALA PHE SER MET THR GLY SER ALA LYS LEU TRP GLY ASN
SEQRES 5 A 219 VAL ASN VAL VAL ALA ARG CYS ALA ASN GLU LYS ARG TYR
SEQRES 6 A 219 LEU GLN VAL ASN VAL GLN ALA THR GLY ASN TYR VAL ALA
SEQRES 7 A 219 VAL ALA ALA PRO ILE ALA ARG GLY GLY LYS LEU THR PRO
SEQRES 8 A 219 ALA ASN VAL THR LEU LYS ARG GLY ARG LEU ASP GLN LEU
SEQRES 9 A 219 PRO PRO ARG THR VAL LEU ASP ILE ARG GLN ILE GLN ASP
SEQRES 10 A 219 ALA VAL SER LEU ARG ASP LEU ALA PRO GLY GLN PRO VAL
SEQRES 11 A 219 GLN LEU THR MET ILE ARG GLN ALA TRP ARG VAL LYS ALA
SEQRES 12 A 219 GLY GLN ARG VAL GLN VAL ILE ALA ASN GLY GLU GLY PHE
SEQRES 13 A 219 SER VAL ASN ALA GLU GLY GLN ALA MET ASN ASN ALA ALA
SEQRES 14 A 219 VAL ALA GLN ASN ALA ARG VAL ARG MET THR SER GLY GLN
SEQRES 15 A 219 ILE VAL SER GLY THR VAL ASP SER ASP GLY ASN ILE LEU
SEQRES 16 A 219 ILE ASN LEU ASP PRO ASN SER SER SER VAL ASP LYS LEU
SEQRES 17 A 219 ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
HET GOL A 301 6
HET GOL A 302 6
HET GOL A 303 6
HET GOL A 304 6
HET GOL A 305 6
HET CL A 401 1
HETNAM GOL GLYCEROL
HETNAM CL CHLORIDE ION
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL 5(C3 H8 O3)
FORMUL 7 CL CL 1-
FORMUL 8 HOH *166(H2 O)
HELIX 1 1 GLN A 1 LEU A 15 1 15
HELIX 2 2 SER A 29 LEU A 33 5 5
HELIX 3 3 ASP A 102 LEU A 104 5 3
HELIX 4 4 ASP A 111 GLN A 116 5 6
HELIX 5 5 GLN A 131 THR A 133 5 3
HELIX 6 6 SER A 203 LEU A 212 1 10
SHEET 1 A 4 GLU A 21 LEU A 26 0
SHEET 2 A 4 GLU A 62 VAL A 79 -1 O GLN A 71 N VAL A 23
SHEET 3 A 4 GLY A 51 CYS A 59 -1 N VAL A 55 O LEU A 66
SHEET 4 A 4 ALA A 40 SER A 42 -1 N SER A 42 O VAL A 56
SHEET 1 B 3 GLU A 21 LEU A 26 0
SHEET 2 B 3 GLU A 62 VAL A 79 -1 O GLN A 71 N VAL A 23
SHEET 3 B 3 VAL A 94 ARG A 100 -1 O THR A 95 N ALA A 78
SHEET 1 C 2 ALA A 118 SER A 120 0
SHEET 2 C 2 ILE A 135 GLN A 137 -1 O ARG A 136 N VAL A 119
SHEET 1 D 6 ARG A 146 ASN A 152 0
SHEET 2 D 6 SER A 157 ALA A 164 -1 O ALA A 160 N VAL A 149
SHEET 3 D 6 ASN A 173 MET A 178 -1 O ARG A 177 N GLN A 163
SHEET 4 D 6 ILE A 183 VAL A 188 -1 O VAL A 184 N VAL A 176
SHEET 5 D 6 ILE A 194 ASN A 197 -1 O LEU A 195 N THR A 187
SHEET 6 D 6 ARG A 146 ASN A 152 1 N GLN A 148 O ILE A 194
SSBOND 1 CYS A 36 CYS A 59 1555 1555 2.05
SITE 1 AC1 7 TRP A 50 LEU A 101 LEU A 104 PRO A 105
SITE 2 AC1 7 ARG A 107 THR A 108 GOL A 304
SITE 1 AC2 6 SER A 42 MET A 43 VAL A 56 ARG A 58
SITE 2 AC2 6 LYS A 63 ASP A 123
SITE 1 AC3 5 GLY A 51 ASN A 69 ARG A 100 ASP A 102
SITE 2 AC3 5 HOH A 274
SITE 1 AC4 4 LYS A 48 LEU A 49 GOL A 301 HOH A 368
SITE 1 AC5 5 ARG A 85 GLY A 86 LEU A 121 ARG A 136
SITE 2 AC5 5 HOH A 358
SITE 1 AC6 2 ARG A 136 TRP A 139
CRYST1 107.520 131.770 49.360 90.00 90.00 90.00 C 2 2 2 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 0.009301 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007589 0.000000 0.00000
SCALE3 0.000000 0.000000 0.020259 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
