HEADER CHAPERONE 27-OCT-11 3VJP
TITLE ORTHORHOMBIC CRYSTAL STRUCTURE OF SALMONELLA FLGA IN CLOSED FORM
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FLAGELLA BASAL BODY P-RING FORMATION PROTEIN FLGA;
COMPND 3 CHAIN: A, B;
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 BACTERIAL FLAGELLUM, SECRETION, DISULFIDE BOND, CHAPERONE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.MATSUNAMI,F.A.SAMATEY,K.NAMBA
REVDAT 2 06-JUL-16 3VJP 1 JRNL
REVDAT 1 31-OCT-12 3VJP 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. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.2_869)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.55
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 12402
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.245
REMARK 3 R VALUE (WORKING SET) : 0.244
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.850
REMARK 3 FREE R VALUE TEST SET COUNT : 602
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 24.5460 - 4.2804 0.94 2964 139 0.2288 0.2510
REMARK 3 2 4.2804 - 3.4003 0.98 2953 150 0.2326 0.2463
REMARK 3 3 3.4003 - 2.9713 0.99 2933 157 0.2636 0.3621
REMARK 3 4 2.9713 - 2.7000 1.00 2950 156 0.3058 0.3355
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.73
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 51.04
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.770
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.240
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 72.96
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 18.68570
REMARK 3 B22 (A**2) : 2.46300
REMARK 3 B33 (A**2) : -21.14870
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.004 3032
REMARK 3 ANGLE : 1.044 4120
REMARK 3 CHIRALITY : 0.078 484
REMARK 3 PLANARITY : 0.006 550
REMARK 3 DIHEDRAL : 15.743 1124
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3VJP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-NOV-11.
REMARK 100 THE RCSB ID CODE IS RCSB095129.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-APR-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.2
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) : NULL
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97895
REMARK 200 MONOCHROMATOR : DOUBLE-CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 12420
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 40.630
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7
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) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7
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: SAD
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.52
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 6000, 0.1M CITRIC ACID, 1.0M
REMARK 280 LICL, PH 4.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
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+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
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 51.74250
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 51.74250
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 26.58400
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 81.25100
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 26.58400
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 81.25100
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 51.74250
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 26.58400
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 81.25100
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 51.74250
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 26.58400
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 81.25100
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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 350
REMARK 350 BIOMOLECULE: 2
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: 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 242 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 251 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 252 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 231 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 228 LIES ON A SPECIAL POSITION.
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 199
REMARK 465 PRO A 200
REMARK 465 ASN A 201
REMARK 465 SER A 202
REMARK 465 SER A 203
REMARK 465 SER A 204
REMARK 465 VAL A 205
REMARK 465 ASP A 206
REMARK 465 LYS A 207
REMARK 465 LEU A 208
REMARK 465 ALA A 209
REMARK 465 ALA A 210
REMARK 465 ALA A 211
REMARK 465 LEU A 212
REMARK 465 GLU A 213
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 465 ASP B 199
REMARK 465 PRO B 200
REMARK 465 ASN B 201
REMARK 465 SER B 202
REMARK 465 SER B 203
REMARK 465 SER B 204
REMARK 465 VAL B 205
REMARK 465 ASP B 206
REMARK 465 LYS B 207
REMARK 465 LEU B 208
REMARK 465 ALA B 209
REMARK 465 ALA B 210
REMARK 465 ALA B 211
REMARK 465 LEU B 212
REMARK 465 GLU B 213
REMARK 465 HIS B 214
REMARK 465 HIS B 215
REMARK 465 HIS B 216
REMARK 465 HIS B 217
REMARK 465 HIS B 218
REMARK 465 HIS B 219
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 SG CYS B 36 CB CYS B 59 1.51
REMARK 500 O GLY A 155 O HOH A 246 2.01
REMARK 500 O HOH A 224 O HOH B 226 2.09
REMARK 500 O GLY B 87 O HOH B 229 2.11
REMARK 500 O ARG B 85 O HOH B 229 2.12
REMARK 500 N ILE B 83 O HOH B 231 2.19
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 THR A 44 56.92 -91.31
REMARK 500 ALA A 60 -68.30 61.88
REMARK 500 SER B 35 43.79 -71.52
REMARK 500 ALA B 60 84.48 60.95
REMARK 500 ASN B 61 -22.82 70.58
REMARK 500 ARG B 85 -121.65 32.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3TEE RELATED DB: PDB
REMARK 900 THE SAME PROTEIN
DBREF 3VJP A 1 198 UNP P40131 FLGA_SALTY 22 219
DBREF 3VJP B 1 198 UNP P40131 FLGA_SALTY 22 219
SEQADV 3VJP ASP A 199 UNP P40131 EXPRESSION TAG
SEQADV 3VJP PRO A 200 UNP P40131 EXPRESSION TAG
SEQADV 3VJP ASN A 201 UNP P40131 EXPRESSION TAG
SEQADV 3VJP SER A 202 UNP P40131 EXPRESSION TAG
SEQADV 3VJP SER A 203 UNP P40131 EXPRESSION TAG
SEQADV 3VJP SER A 204 UNP P40131 EXPRESSION TAG
SEQADV 3VJP VAL A 205 UNP P40131 EXPRESSION TAG
SEQADV 3VJP ASP A 206 UNP P40131 EXPRESSION TAG
SEQADV 3VJP LYS A 207 UNP P40131 EXPRESSION TAG
SEQADV 3VJP LEU A 208 UNP P40131 EXPRESSION TAG
SEQADV 3VJP ALA A 209 UNP P40131 EXPRESSION TAG
SEQADV 3VJP ALA A 210 UNP P40131 EXPRESSION TAG
SEQADV 3VJP ALA A 211 UNP P40131 EXPRESSION TAG
SEQADV 3VJP LEU A 212 UNP P40131 EXPRESSION TAG
SEQADV 3VJP GLU A 213 UNP P40131 EXPRESSION TAG
SEQADV 3VJP HIS A 214 UNP P40131 EXPRESSION TAG
SEQADV 3VJP HIS A 215 UNP P40131 EXPRESSION TAG
SEQADV 3VJP HIS A 216 UNP P40131 EXPRESSION TAG
SEQADV 3VJP HIS A 217 UNP P40131 EXPRESSION TAG
SEQADV 3VJP HIS A 218 UNP P40131 EXPRESSION TAG
SEQADV 3VJP HIS A 219 UNP P40131 EXPRESSION TAG
SEQADV 3VJP ASP B 199 UNP P40131 EXPRESSION TAG
SEQADV 3VJP PRO B 200 UNP P40131 EXPRESSION TAG
SEQADV 3VJP ASN B 201 UNP P40131 EXPRESSION TAG
SEQADV 3VJP SER B 202 UNP P40131 EXPRESSION TAG
SEQADV 3VJP SER B 203 UNP P40131 EXPRESSION TAG
SEQADV 3VJP SER B 204 UNP P40131 EXPRESSION TAG
SEQADV 3VJP VAL B 205 UNP P40131 EXPRESSION TAG
SEQADV 3VJP ASP B 206 UNP P40131 EXPRESSION TAG
SEQADV 3VJP LYS B 207 UNP P40131 EXPRESSION TAG
SEQADV 3VJP LEU B 208 UNP P40131 EXPRESSION TAG
SEQADV 3VJP ALA B 209 UNP P40131 EXPRESSION TAG
SEQADV 3VJP ALA B 210 UNP P40131 EXPRESSION TAG
SEQADV 3VJP ALA B 211 UNP P40131 EXPRESSION TAG
SEQADV 3VJP LEU B 212 UNP P40131 EXPRESSION TAG
SEQADV 3VJP GLU B 213 UNP P40131 EXPRESSION TAG
SEQADV 3VJP HIS B 214 UNP P40131 EXPRESSION TAG
SEQADV 3VJP HIS B 215 UNP P40131 EXPRESSION TAG
SEQADV 3VJP HIS B 216 UNP P40131 EXPRESSION TAG
SEQADV 3VJP HIS B 217 UNP P40131 EXPRESSION TAG
SEQADV 3VJP HIS B 218 UNP P40131 EXPRESSION TAG
SEQADV 3VJP HIS B 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 MSE 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 MSE 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 MSE ASN ASN ALA ALA
SEQRES 14 A 219 VAL ALA GLN ASN ALA ARG VAL ARG MSE 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
SEQRES 1 B 219 GLN ASP ILE ASN ALA GLN LEU THR THR TRP PHE SER GLN
SEQRES 2 B 219 ARG LEU ALA GLY PHE SER ASP GLU VAL VAL VAL THR LEU
SEQRES 3 B 219 ARG SER SER PRO ASN LEU LEU PRO SER CYS GLU GLN PRO
SEQRES 4 B 219 ALA PHE SER MSE THR GLY SER ALA LYS LEU TRP GLY ASN
SEQRES 5 B 219 VAL ASN VAL VAL ALA ARG CYS ALA ASN GLU LYS ARG TYR
SEQRES 6 B 219 LEU GLN VAL ASN VAL GLN ALA THR GLY ASN TYR VAL ALA
SEQRES 7 B 219 VAL ALA ALA PRO ILE ALA ARG GLY GLY LYS LEU THR PRO
SEQRES 8 B 219 ALA ASN VAL THR LEU LYS ARG GLY ARG LEU ASP GLN LEU
SEQRES 9 B 219 PRO PRO ARG THR VAL LEU ASP ILE ARG GLN ILE GLN ASP
SEQRES 10 B 219 ALA VAL SER LEU ARG ASP LEU ALA PRO GLY GLN PRO VAL
SEQRES 11 B 219 GLN LEU THR MSE ILE ARG GLN ALA TRP ARG VAL LYS ALA
SEQRES 12 B 219 GLY GLN ARG VAL GLN VAL ILE ALA ASN GLY GLU GLY PHE
SEQRES 13 B 219 SER VAL ASN ALA GLU GLY GLN ALA MSE ASN ASN ALA ALA
SEQRES 14 B 219 VAL ALA GLN ASN ALA ARG VAL ARG MSE THR SER GLY GLN
SEQRES 15 B 219 ILE VAL SER GLY THR VAL ASP SER ASP GLY ASN ILE LEU
SEQRES 16 B 219 ILE ASN LEU ASP PRO ASN SER SER SER VAL ASP LYS LEU
SEQRES 17 B 219 ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS HIS
MODRES 3VJP MSE A 43 MET SELENOMETHIONINE
MODRES 3VJP MSE A 134 MET SELENOMETHIONINE
MODRES 3VJP MSE A 165 MET SELENOMETHIONINE
MODRES 3VJP MSE A 178 MET SELENOMETHIONINE
MODRES 3VJP MSE B 43 MET SELENOMETHIONINE
MODRES 3VJP MSE B 134 MET SELENOMETHIONINE
MODRES 3VJP MSE B 165 MET SELENOMETHIONINE
MODRES 3VJP MSE B 178 MET SELENOMETHIONINE
HET MSE A 43 8
HET MSE A 134 8
HET MSE A 165 8
HET MSE A 178 8
HET MSE B 43 8
HET MSE B 134 8
HET MSE B 165 8
HET MSE B 178 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 8(C5 H11 N O2 SE)
FORMUL 3 HOH *45(H2 O)
HELIX 1 1 GLN A 1 LEU A 15 1 15
HELIX 2 2 ASP A 102 LEU A 104 5 3
HELIX 3 3 ASP B 2 LEU B 15 1 14
HELIX 4 4 ASP B 102 LEU B 104 5 3
SHEET 1 A 4 SER A 19 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 ASN A 54 CYS A 59 -1 N VAL A 55 O LEU A 66
SHEET 4 A 4 ALA A 40 MSE A 43 -1 N SER A 42 O VAL A 56
SHEET 1 B 3 SER A 19 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 GLY A 153 0
SHEET 2 D 6 PHE A 156 ALA A 164 -1 O VAL A 158 N ALA A 151
SHEET 3 D 6 ASN A 173 MSE 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 GLY A 153 1 N ILE A 150 O ILE A 194
SHEET 1 E 4 SER B 19 LEU B 26 0
SHEET 2 E 4 GLU B 62 VAL B 79 -1 O GLN B 71 N VAL B 23
SHEET 3 E 4 ASN B 54 CYS B 59 -1 N VAL B 55 O LEU B 66
SHEET 4 E 4 ALA B 40 SER B 42 -1 N ALA B 40 O ARG B 58
SHEET 1 F 3 SER B 19 LEU B 26 0
SHEET 2 F 3 GLU B 62 VAL B 79 -1 O GLN B 71 N VAL B 23
SHEET 3 F 3 VAL B 94 ARG B 100 -1 O THR B 95 N ALA B 78
SHEET 1 G 2 VAL B 119 SER B 120 0
SHEET 2 G 2 ILE B 135 ARG B 136 -1 O ARG B 136 N VAL B 119
SHEET 1 H 6 ARG B 146 GLY B 153 0
SHEET 2 H 6 PHE B 156 ALA B 164 -1 O ALA B 160 N VAL B 149
SHEET 3 H 6 ASN B 173 MSE B 178 -1 O ARG B 177 N GLN B 163
SHEET 4 H 6 ILE B 183 VAL B 188 -1 O VAL B 184 N VAL B 176
SHEET 5 H 6 ILE B 194 ASN B 197 -1 O LEU B 195 N THR B 187
SHEET 6 H 6 ARG B 146 GLY B 153 1 N ILE B 150 O ILE B 194
SSBOND 1 CYS A 36 CYS A 59 1555 1555 2.03
SSBOND 2 CYS B 36 CYS B 59 1555 1555 2.03
LINK C SER A 42 N MSE A 43 1555 1555 1.33
LINK C MSE A 43 N THR A 44 1555 1555 1.33
LINK C THR A 133 N MSE A 134 1555 1555 1.33
LINK C MSE A 134 N ILE A 135 1555 1555 1.33
LINK C ALA A 164 N MSE A 165 1555 1555 1.33
LINK C MSE A 165 N ASN A 166 1555 1555 1.33
LINK C ARG A 177 N MSE A 178 1555 1555 1.33
LINK C MSE A 178 N THR A 179 1555 1555 1.33
LINK C SER B 42 N MSE B 43 1555 1555 1.33
LINK C MSE B 43 N THR B 44 1555 1555 1.33
LINK C THR B 133 N MSE B 134 1555 1555 1.33
LINK C MSE B 134 N ILE B 135 1555 1555 1.33
LINK C ALA B 164 N MSE B 165 1555 1555 1.33
LINK C MSE B 165 N ASN B 166 1555 1555 1.33
LINK C ARG B 177 N MSE B 178 1555 1555 1.33
LINK C MSE B 178 N THR B 179 1555 1555 1.33
CRYST1 53.168 162.502 103.485 90.00 90.00 90.00 C 2 2 21 16
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 0.018808 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006154 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009663 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
