HEADER ISOMERASE 04-JUN-04 1TJD
TITLE THE CRYSTAL STRUCTURE OF THE REDUCED DISULPHIDE BOND ISOMERASE, DSBC,
TITLE 2 FROM ESCHERICHIA COLI
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC;
COMPND 3 CHAIN: A;
COMPND 4 EC: 5.3.4.1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562;
SOURCE 4 GENE: DSBC, XPRA, B2893, Z4231, ECS3765;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21 (DE2);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PDM801
KEYWDS DIMER, ISOMERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR K.BANASZAK,I.MECHIN,G.FROST,W.RYPNIEWSKI
REVDAT 3 23-AUG-23 1TJD 1 REMARK
REVDAT 2 24-FEB-09 1TJD 1 VERSN
REVDAT 1 05-OCT-04 1TJD 0
JRNL AUTH K.BANASZAK,I.MECHIN,G.FROST,W.RYPNIEWSKI
JRNL TITL STRUCTURE OF THE REDUCED DISULFIDE-BOND ISOMERASE DSBC FROM
JRNL TITL 2 ESCHERICHIA COLI.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 60 1747 2004
JRNL REFN ISSN 0907-4449
JRNL PMID 15388920
JRNL DOI 10.1107/S0907444904018359
REMARK 2
REMARK 2 RESOLUTION. 2.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.24
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) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 16.74
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 7953
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) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.203
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.900
REMARK 3 FREE R VALUE TEST SET COUNT : 150
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) : 2.50
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.56
REMARK 3 REFLECTION IN BIN (WORKING SET) : 566
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.0
REMARK 3 BIN R VALUE (WORKING SET) : 0.2220
REMARK 3 BIN FREE R VALUE SET COUNT : 7
REMARK 3 BIN FREE R VALUE : 0.4200
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1640
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 71
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 42.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 35.05
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.38000
REMARK 3 B22 (A**2) : 0.59000
REMARK 3 B33 (A**2) : -0.98000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.576
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.310
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.190
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.374
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.933
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.896
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1621 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2203 ; 1.271 ; 1.961
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 214 ; 5.801 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 255 ; 0.075 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1208 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 703 ; 0.200 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 81 ; 0.147 ; 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): 58 ; 0.230 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.119 ; 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): 1070 ; 0.619 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1716 ; 1.213 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 551 ; 2.094 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 487 ; 3.280 ; 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 : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1TJD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUN-04.
REMARK 100 THE DEPOSITION ID IS D_1000022683.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-OCT-98
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : EMBL/DESY, HAMBURG
REMARK 200 BEAMLINE : X11
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.906
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7953
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 17.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 11.00
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : 0.08100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.54
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.00
REMARK 200 R MERGE FOR SHELL (I) : 0.38600
REMARK 200 R SYM FOR SHELL (I) : 0.38600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: AMORE
REMARK 200 STARTING MODEL: PDB ENTRY 1EEJ
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LISO4, 0.1 M TRIS PH 8.4 AND 20%
REMARK 280 W/V PEG 4000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
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 36.79100
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 36.79100
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 20.94850
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 72.89950
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 20.94850
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 72.89950
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 36.79100
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 20.94850
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 72.89950
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 36.79100
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 20.94850
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 72.89950
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER GENERATED FROM THE
REMARK 300 MONOMER IN THE ASYMMETRIC UNIT BY THE OPERATIONS: -X, Y, Z-1/2
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 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 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 145.79900
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ASP A 1 N CA CB CG OD1 OD2
REMARK 480 GLN A 6 CG CD OE1 NE2
REMARK 480 GLN A 7 CD OE1 NE2
REMARK 480 LEU A 9 CG CD1 CD2
REMARK 480 ILE A 14 CG1 CG2 CD1
REMARK 480 LYS A 15 CG CD CE NZ
REMARK 480 SER A 16 CB OG
REMARK 480 SER A 17 OG
REMARK 480 LYS A 28 CE NZ
REMARK 480 LYS A 44 CD CE NZ
REMARK 480 LYS A 69 CD CE NZ
REMARK 480 LYS A 82 NZ
REMARK 480 LYS A 87 CD CE NZ
REMARK 480 LYS A 103 NZ
REMARK 480 GLN A 126 CD OE1 NE2
REMARK 480 LYS A 143 CG CD CE NZ
REMARK 480 LYS A 147 NZ
REMARK 480 GLU A 208 CG CD OE1 OE2
REMARK 480 LYS A 211 NZ
REMARK 480 LYS A 216 OXT
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 OE1 GLU A 208 CE MET A 212 1.31
REMARK 500 CB ASP A 1 O ASP A 41 1.58
REMARK 500 CD1 ILE A 5 NZ LYS A 28 1.90
REMARK 500 O ASP A 2 NE2 GLN A 6 1.90
REMARK 500 O ILE A 5 CD1 LEU A 9 1.91
REMARK 500 O LEU A 128 OE1 GLU A 133 2.03
REMARK 500 NZ LYS A 103 O HOH A 282 2.13
REMARK 500 CB ASP A 1 C ASP A 41 2.18
REMARK 500
REMARK 500 REMARK: NULL
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 GLN A 6 CB GLN A 6 CG -0.201
REMARK 500 GLN A 7 CG GLN A 7 CD 0.190
REMARK 500 ILE A 14 CB ILE A 14 CG1 -0.247
REMARK 500 ILE A 14 CB ILE A 14 CG2 0.188
REMARK 500 SER A 17 CB SER A 17 OG -0.099
REMARK 500 LYS A 28 CD LYS A 28 CE 0.190
REMARK 500 LYS A 82 CE LYS A 82 NZ 0.233
REMARK 500 GLN A 126 CG GLN A 126 CD -0.152
REMARK 500 LYS A 216 C LYS A 216 OXT 0.174
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 ASP A 1 CB - CA - C ANGL. DEV. = 16.7 DEGREES
REMARK 500 GLN A 6 CA - CB - CG ANGL. DEV. = 16.1 DEGREES
REMARK 500 LEU A 9 CB - CG - CD1 ANGL. DEV. = 16.9 DEGREES
REMARK 500 LYS A 28 CG - CD - CE ANGL. DEV. = 24.2 DEGREES
REMARK 500 LYS A 44 CB - CG - CD ANGL. DEV. = 21.2 DEGREES
REMARK 500 LYS A 69 CB - CG - CD ANGL. DEV. = 22.7 DEGREES
REMARK 500 LEU A 104 CA - CB - CG ANGL. DEV. = 15.3 DEGREES
REMARK 500 LYS A 211 CD - CE - NZ ANGL. DEV. = 15.2 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 ALA A 10 41.38 -75.50
REMARK 500 LYS A 11 -3.09 -166.36
REMARK 500 LYS A 15 -87.81 -91.73
REMARK 500 VAL A 54 48.44 -108.16
REMARK 500 ASP A 129 68.89 -101.96
REMARK 500 CYS A 163 -167.88 -165.10
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 ASP A 1 ASP A 2 -129.79
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1TJD A 1 216 UNP P21892 DSBC_ECOLI 21 236
SEQRES 1 A 216 ASP ASP ALA ALA ILE GLN GLN THR LEU ALA LYS MET GLY
SEQRES 2 A 216 ILE LYS SER SER ASP ILE GLN PRO ALA PRO VAL ALA GLY
SEQRES 3 A 216 MET LYS THR VAL LEU THR ASN SER GLY VAL LEU TYR ILE
SEQRES 4 A 216 THR ASP ASP GLY LYS HIS ILE ILE GLN GLY PRO MET TYR
SEQRES 5 A 216 ASP VAL SER GLY THR ALA PRO VAL ASN VAL THR ASN LYS
SEQRES 6 A 216 MET LEU LEU LYS GLN LEU ASN ALA LEU GLU LYS GLU MET
SEQRES 7 A 216 ILE VAL TYR LYS ALA PRO GLN GLU LYS HIS VAL ILE THR
SEQRES 8 A 216 VAL PHE THR ASP ILE THR CYS GLY TYR CYS HIS LYS LEU
SEQRES 9 A 216 HIS GLU GLN MET ALA ASP TYR ASN ALA LEU GLY ILE THR
SEQRES 10 A 216 VAL ARG TYR LEU ALA PHE PRO ARG GLN GLY LEU ASP SER
SEQRES 11 A 216 ASP ALA GLU LYS GLU MET LYS ALA ILE TRP CYS ALA LYS
SEQRES 12 A 216 ASP LYS ASN LYS ALA PHE ASP ASP VAL MET ALA GLY LYS
SEQRES 13 A 216 SER VAL ALA PRO ALA SER CYS ASP VAL ASP ILE ALA ASP
SEQRES 14 A 216 HIS TYR ALA LEU GLY VAL GLN LEU GLY VAL SER GLY THR
SEQRES 15 A 216 PRO ALA VAL VAL LEU SER ASN GLY THR LEU VAL PRO GLY
SEQRES 16 A 216 TYR GLN PRO PRO LYS GLU MET LYS GLU PHE LEU ASP GLU
SEQRES 17 A 216 HIS GLN LYS MET THR SER GLY LYS
FORMUL 2 HOH *71(H2 O)
HELIX 1 1 ALA A 3 GLY A 13 1 11
HELIX 2 2 VAL A 62 LEU A 74 1 13
HELIX 3 3 GLU A 75 MET A 78 5 4
HELIX 4 4 CYS A 98 GLN A 107 1 10
HELIX 5 5 GLN A 107 LEU A 114 1 8
HELIX 6 6 SER A 130 CYS A 141 1 12
HELIX 7 7 ASP A 144 GLY A 155 1 12
HELIX 8 8 ASP A 166 LEU A 177 1 12
HELIX 9 9 PRO A 198 SER A 214 1 17
SHEET 1 A 4 ASP A 18 PRO A 21 0
SHEET 2 A 4 MET A 27 THR A 32 -1 O THR A 29 N GLN A 20
SHEET 3 A 4 GLY A 35 THR A 40 -1 O LEU A 37 N VAL A 30
SHEET 4 A 4 ILE A 46 ILE A 47 -1 O ILE A 47 N TYR A 38
SHEET 1 B 2 TYR A 52 ASP A 53 0
SHEET 2 B 2 VAL A 60 ASN A 61 -1 O VAL A 60 N ASP A 53
SHEET 1 C 5 ILE A 79 TYR A 81 0
SHEET 2 C 5 ILE A 116 ALA A 122 -1 O TYR A 120 N ILE A 79
SHEET 3 C 5 HIS A 88 THR A 94 1 N HIS A 88 O THR A 117
SHEET 4 C 5 ALA A 184 VAL A 186 -1 O VAL A 186 N THR A 91
SHEET 5 C 5 LEU A 192 PRO A 194 -1 O VAL A 193 N VAL A 185
SSBOND 1 CYS A 141 CYS A 163 1555 1555 2.05
CISPEP 1 GLY A 49 PRO A 50 0 0.26
CISPEP 2 THR A 182 PRO A 183 0 -3.53
CRYST1 41.897 145.799 73.582 90.00 90.00 90.00 C 2 2 21 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 0.023868 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006859 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013590 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
