HEADER CHAPERONE 21-MAY-05 2BSH
TITLE CRYSTAL STRUCTURE OF THE TYPE III SECRETION CHAPERONE SYCT FROM
TITLE 2 YERSINIA ENTEROCOLITICA (CRYSTAL FORM 2)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SYCT;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: YERSINIA ENTEROCOLITICA;
SOURCE 3 ORGANISM_TAXID: 630;
SOURCE 4 STRAIN: W22703;
SOURCE 5 VARIANT: SEROTYPE O\:9;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-M-30;
SOURCE 10 OTHER_DETAILS: YERSINIA ENTEROCOLITICA VIRULENCE PLASMID PYVE227
KEYWDS TYPE III SECRETION, YERSINIA, CHAPERONE, EFFECTOR, YOPT
EXPDTA X-RAY DIFFRACTION
AUTHOR C.R.BUTTNER,G.R.CORNELIS,D.W.HEINZ,H.H.NIEMANN
REVDAT 4 27-FEB-19 2BSH 1 JRNL REMARK LINK
REVDAT 3 13-JUL-11 2BSH 1 VERSN
REVDAT 2 24-FEB-09 2BSH 1 VERSN
REVDAT 1 15-AUG-05 2BSH 0
JRNL AUTH C.R.BUTTNER,G.R.CORNELIS,D.W.HEINZ,H.H.NIEMANN
JRNL TITL CRYSTAL STRUCTURE OF YERSINIA ENTEROCOLITICA TYPE III
JRNL TITL 2 SECRETION CHAPERONE SYCT.
JRNL REF PROTEIN SCI. V. 14 1993 2005
JRNL REFN ISSN 0961-8368
JRNL PMID 16046625
JRNL DOI 10.1110/PS.051474605
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 79.81
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 20049
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) : 0.176
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.220
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 1085
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1461
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.87
REMARK 3 BIN R VALUE (WORKING SET) : 0.2000
REMARK 3 BIN FREE R VALUE SET COUNT : 67
REMARK 3 BIN FREE R VALUE : 0.2550
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1941
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 139
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.26
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.73000
REMARK 3 B22 (A**2) : -0.73000
REMARK 3 B33 (A**2) : 1.10000
REMARK 3 B12 (A**2) : -0.37000
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): 0.142
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.137
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.094
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.120
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1988 ; 0.022 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2700 ; 1.875 ; 1.919
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 234 ; 7.011 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 116 ;38.971 ;25.948
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 335 ;13.936 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 6 ;19.209 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 287 ; 0.162 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1561 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 939 ; 0.251 ; 0.300
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1363 ; 0.323 ; 0.500
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 251 ; 0.184 ; 0.500
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): 57 ; 0.232 ; 0.300
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 15 ; 0.172 ; 0.500
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): 1204 ; 2.289 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1884 ; 3.388 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 907 ; 2.751 ; 2.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 816 ; 3.646 ; 3.000
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 : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 3 A 93
REMARK 3 ORIGIN FOR THE GROUP (A): 57.6202 13.8417 -2.1721
REMARK 3 T TENSOR
REMARK 3 T11: 0.0510 T22: 0.0183
REMARK 3 T33: 0.0484 T12: -0.0262
REMARK 3 T13: 0.0349 T23: -0.0009
REMARK 3 L TENSOR
REMARK 3 L11: 4.7273 L22: 3.3314
REMARK 3 L33: 2.3421 L12: -0.4534
REMARK 3 L13: 0.3749 L23: -0.8756
REMARK 3 S TENSOR
REMARK 3 S11: 0.0479 S12: 0.1269 S13: -0.0777
REMARK 3 S21: 0.1384 S22: -0.1378 S23: 0.0480
REMARK 3 S31: -0.0691 S32: 0.0120 S33: 0.0899
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 94 A 122
REMARK 3 ORIGIN FOR THE GROUP (A): 55.7466 16.6612 3.4244
REMARK 3 T TENSOR
REMARK 3 T11: 0.1201 T22: 0.0834
REMARK 3 T33: 0.0383 T12: -0.0644
REMARK 3 T13: 0.0258 T23: -0.0376
REMARK 3 L TENSOR
REMARK 3 L11: 15.5612 L22: 1.4857
REMARK 3 L33: 1.6413 L12: -0.1075
REMARK 3 L13: 0.4677 L23: -0.3130
REMARK 3 S TENSOR
REMARK 3 S11: -0.0827 S12: 0.5860 S13: -0.4779
REMARK 3 S21: 0.2421 S22: -0.0035 S23: 0.0968
REMARK 3 S31: -0.1572 S32: 0.1214 S33: 0.0862
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B -2 B 33
REMARK 3 ORIGIN FOR THE GROUP (A): 81.1229 21.3229 -11.3036
REMARK 3 T TENSOR
REMARK 3 T11: -0.0430 T22: 0.1521
REMARK 3 T33: 0.1789 T12: -0.0598
REMARK 3 T13: 0.0889 T23: 0.1309
REMARK 3 L TENSOR
REMARK 3 L11: 6.2261 L22: 2.3028
REMARK 3 L33: 2.6402 L12: 1.6489
REMARK 3 L13: -0.5561 L23: -1.8057
REMARK 3 S TENSOR
REMARK 3 S11: 0.0867 S12: -0.7161 S13: -0.4237
REMARK 3 S21: -0.2350 S22: -0.4118 S23: -0.6488
REMARK 3 S31: -0.2965 S32: 0.3377 S33: 0.3252
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 34 B 114
REMARK 3 ORIGIN FOR THE GROUP (A): 62.4178 12.8547 -9.0314
REMARK 3 T TENSOR
REMARK 3 T11: 0.0186 T22: 0.0049
REMARK 3 T33: 0.0060 T12: -0.0119
REMARK 3 T13: 0.0294 T23: 0.0129
REMARK 3 L TENSOR
REMARK 3 L11: 3.6382 L22: 3.8104
REMARK 3 L33: 2.1924 L12: 1.1483
REMARK 3 L13: -1.2419 L23: -1.3787
REMARK 3 S TENSOR
REMARK 3 S11: 0.0262 S12: -0.0070 S13: -0.1338
REMARK 3 S21: 0.0021 S22: -0.1313 S23: -0.1047
REMARK 3 S31: 0.0298 S32: -0.0224 S33: 0.1052
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH 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 2BSH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1290023476.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-SEP-04
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : BESSY
REMARK 200 BEAMLINE : 14.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97957
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21134
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 79.810
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 11.20
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 16.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.4
REMARK 200 DATA REDUNDANCY IN SHELL : 11.20
REMARK 200 R MERGE FOR SHELL (I) : 0.40000
REMARK 200 R SYM FOR SHELL (I) : 0.07000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.530
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELX, CDE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 45.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.8 M AMMONIUM SULFATE, 0.1 M SODIUM
REMARK 280 BICARBONATE PH 10.5, 50 MM MAGNESIUM CHLORIDE HANGING-DROP VAPOR
REMARK 280 DIFFUSION AT 4 CELSIUS DEGREE, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62
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 -X,-Y,Z
REMARK 290 5555 Y,-X+Y,Z+2/3
REMARK 290 6555 X-Y,X,Z+1/3
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 36.91333
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 18.45667
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 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 36.91333
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 18.45667
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: PQS
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 400
REMARK 400 COMPOUND
REMARK 400 IT IS A SPECIFIC CHAPERONE FOR YOPT
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 -2
REMARK 465 ALA A -1
REMARK 465 MSE A 0
REMARK 465 GLY A 1
REMARK 465 GLN A 2
REMARK 465 GLN B 115
REMARK 465 ASN B 116
REMARK 465 THR B 117
REMARK 465 LYS B 118
REMARK 465 PHE B 119
REMARK 465 GLN B 120
REMARK 465 PRO B 121
REMARK 465 ASN B 122
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 PRO B 114 CA C O CB CG CD
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 24 CD GLU A 24 OE1 0.100
REMARK 500 GLU A 24 CD GLU A 24 OE2 0.121
REMARK 500 ASP A 57 CG ASP A 57 OD2 0.174
REMARK 500 TRP A 84 CB TRP A 84 CG 0.109
REMARK 500 GLU B 96 CG GLU B 96 CD 0.097
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 THR A 4 N - CA - C ANGL. DEV. = -18.4 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 ASN A 19 -73.86 -66.64
REMARK 500 ASP A 33 27.50 31.31
REMARK 500 GLN A 45 17.47 59.68
REMARK 500 GLN A 46 -35.30 -144.99
REMARK 500 GLN A 120 -37.21 174.51
REMARK 500 ASP B 26 30.07 72.61
REMARK 500 GLN B 46 -23.14 -140.32
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PHE A 119 GLN A 120 141.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: SECONDARY STRUCTURE ASSIGNED BY STRIDE
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2BHO RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE YERSINIA ENTEROCOLITICA TYPE III SECRETION
REMARK 900 CHAPERONE SYCT
REMARK 900 RELATED ID: 2BSI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE YERSINIA ENTEROCOLITICA TYPE III SECRETION
REMARK 900 CHAPERONE SYCT (CRYSTAL FORM 1)
REMARK 900 RELATED ID: 2BSJ RELATED DB: PDB
REMARK 900 NATIVE CRYSTAL STRUCTURE OF THE YERSINIA ENTEROCOLITICA TYPE III
REMARK 900 SECRETION CHAPERONE SYCT
DBREF 2BSH A -2 1 PDB 2BSH 2BSH -2 1
DBREF 2BSH A 2 122 UNP O85243 SYCT_YEREN 2 122
DBREF 2BSH B -2 1 PDB 2BSH 2BSH -2 1
DBREF 2BSH B 2 122 UNP O85243 SYCT_YEREN 2 122
SEQRES 1 A 125 GLY ALA MSE GLY GLN THR THR PHE THR GLU LEU MSE GLN
SEQRES 2 A 125 GLN LEU PHE LEU LYS LEU GLY LEU ASN HIS GLN VAL ASN
SEQRES 3 A 125 GLU ASN ASP VAL TYR THR PHE GLU VAL ASP GLY HIS ILE
SEQRES 4 A 125 GLN VAL LEU ILE ALA CYS TYR HIS GLN GLN TRP VAL GLN
SEQRES 5 A 125 LEU PHE SER GLU LEU GLY ALA ASP LEU PRO THR ASN ASP
SEQRES 6 A 125 ASN LEU PHE GLY GLU HIS TRP PRO ALA HIS VAL GLN GLY
SEQRES 7 A 125 ARG LEU ASP GLY LYS SER ILE LEU TRP SER GLN GLN SER
SEQRES 8 A 125 LEU VAL GLY LEU ASP ILE ASP GLU MSE GLN ALA TRP LEU
SEQRES 9 A 125 GLU ARG PHE ILE ASP ASP ILE GLU GLN ARG LYS GLU PRO
SEQRES 10 A 125 GLN ASN THR LYS PHE GLN PRO ASN
SEQRES 1 B 125 GLY ALA MSE GLY GLN THR THR PHE THR GLU LEU MSE GLN
SEQRES 2 B 125 GLN LEU PHE LEU LYS LEU GLY LEU ASN HIS GLN VAL ASN
SEQRES 3 B 125 GLU ASN ASP VAL TYR THR PHE GLU VAL ASP GLY HIS ILE
SEQRES 4 B 125 GLN VAL LEU ILE ALA CYS TYR HIS GLN GLN TRP VAL GLN
SEQRES 5 B 125 LEU PHE SER GLU LEU GLY ALA ASP LEU PRO THR ASN ASP
SEQRES 6 B 125 ASN LEU PHE GLY GLU HIS TRP PRO ALA HIS VAL GLN GLY
SEQRES 7 B 125 ARG LEU ASP GLY LYS SER ILE LEU TRP SER GLN GLN SER
SEQRES 8 B 125 LEU VAL GLY LEU ASP ILE ASP GLU MSE GLN ALA TRP LEU
SEQRES 9 B 125 GLU ARG PHE ILE ASP ASP ILE GLU GLN ARG LYS GLU PRO
SEQRES 10 B 125 GLN ASN THR LYS PHE GLN PRO ASN
MODRES 2BSH MSE A 9 MET SELENOMETHIONINE
MODRES 2BSH MSE A 97 MET SELENOMETHIONINE
MODRES 2BSH MSE B 0 MET SELENOMETHIONINE
MODRES 2BSH MSE B 9 MET SELENOMETHIONINE
MODRES 2BSH MSE B 97 MET SELENOMETHIONINE
HET MSE A 9 8
HET MSE A 97 8
HET MSE B 0 8
HET MSE B 9 8
HET MSE B 97 8
HETNAM MSE SELENOMETHIONINE
FORMUL 1 MSE 5(C5 H11 N O2 SE)
FORMUL 3 HOH *139(H2 O)
HELIX 1 1 THR A 3 LEU A 16 1 14
HELIX 2 2 ILE A 94 LYS A 112 1 19
HELIX 3 3 ALA B -1 LEU B 16 1 18
HELIX 4 4 ILE B 94 LYS B 112 1 19
SHEET 1 AA 6 GLN A 21 ASN A 23 0
SHEET 2 AA 6 VAL A 27 VAL A 32 -1 O VAL A 27 N ASN A 23
SHEET 3 AA 6 ILE A 36 TYR A 43 -1 O ILE A 36 N VAL A 32
SHEET 4 AA 6 TRP A 47 GLY A 55 -1 O TRP A 47 N TYR A 43
SHEET 5 AA 6 HIS A 72 LEU A 77 -1 O VAL A 73 N TRP A 84
SHEET 6 AA 6 LYS A 80 SER A 88 -1 O SER A 81 N LEU A 54
SHEET 1 BA 6 GLN B 21 VAL B 22 0
SHEET 2 BA 6 VAL B 27 VAL B 32 -1 O THR B 29 N GLN B 21
SHEET 3 BA 6 ILE B 36 TYR B 43 -1 O ILE B 36 N VAL B 32
SHEET 4 BA 6 TRP B 47 ALA B 56 -1 O TRP B 47 N TYR B 43
SHEET 5 BA 6 VAL B 73 LEU B 77 -1 O VAL B 73 N TRP B 84
SHEET 6 BA 6 LYS B 80 SER B 88 -1 O LEU B 83 N SER B 52
LINK C LEU A 8 N MSE A 9 1555 1555 1.34
LINK C MSE A 9 N GLN A 10 1555 1555 1.33
LINK C GLU A 96 N MSE A 97 1555 1555 1.33
LINK C MSE A 97 N GLN A 98 1555 1555 1.34
LINK C ALA B -1 N MSE B 0 1555 1555 1.34
LINK C MSE B 0 N GLY B 1 1555 1555 1.34
LINK C LEU B 8 N MSE B 9 1555 1555 1.34
LINK C MSE B 9 N GLN B 10 1555 1555 1.33
LINK C GLU B 96 N MSE B 97 1555 1555 1.32
LINK C MSE B 97 N GLN B 98 1555 1555 1.33
CISPEP 1 THR A 3 THR A 4 0 -29.63
CISPEP 2 ASN A 19 HIS A 20 0 -17.30
CISPEP 3 TRP A 69 PRO A 70 0 -2.16
CISPEP 4 GLN A 120 PRO A 121 0 -20.56
CISPEP 5 PRO A 121 ASN A 122 0 -1.70
CISPEP 6 TRP B 69 PRO B 70 0 -1.26
CRYST1 92.040 92.040 55.370 90.00 90.00 120.00 P 62 12
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 0.010865 0.006273 0.000000 0.00000
SCALE2 0.000000 0.012546 0.000000 0.00000
SCALE3 0.000000 0.000000 0.018060 0.00000
MTRIX1 1 0.875030 0.433640 0.215130 2.79374 1
MTRIX2 1 0.434770 -0.899440 0.044590 -1.00649 1
MTRIX3 1 0.212830 0.054510 -0.975570 -22.34988 1
(ATOM LINES ARE NOT SHOWN.)
END
