HEADER ISOMERASE 18-JUL-06 2IYJ
TITLE CRYSTAL STRUCTURE OF THE N-TERMINAL DIMER DOMAIN OF E.COLI DSBC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: THIOL DISULFIDE INTERCHANGE PROTEIN DSBC;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: N-TERMINAL DOMAIN, RESIDUES 19-91;
COMPND 5 SYNONYM: NDSBC
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 562
KEYWDS DISULFIDE BOND ISOMERASE, ISOMERASE, DSBC, DSBG, PERIPLASMIC, REDOX-
KEYWDS 2 ACTIVE CENTER
EXPDTA X-RAY DIFFRACTION
AUTHOR S.-M.YEH,P.METCALF
REVDAT 4 13-DEC-23 2IYJ 1 REMARK
REVDAT 3 13-JUL-11 2IYJ 1 VERSN
REVDAT 2 24-FEB-09 2IYJ 1 VERSN
REVDAT 1 24-JUL-07 2IYJ 0
JRNL AUTH S.-M.YEH,N.KOON,C.SQUIRE,P.METCALF
JRNL TITL STRUCTURES OF DIMERIZATION DOMAINS OF THE ESCHERICHIA COLI
JRNL TITL 2 DISULFIDE-BOND ISOMERASE ENZYMES DSBC AND DSBG.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 63 465 2007
JRNL REFN ISSN 0907-4449
JRNL PMID 17372350
JRNL DOI 10.1107/S0907444907003320
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.77
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.3
REMARK 3 NUMBER OF REFLECTIONS : 9759
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) : 0.228
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.251
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 492
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 584
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 83.54
REMARK 3 BIN R VALUE (WORKING SET) : 0.2770
REMARK 3 BIN FREE R VALUE SET COUNT : 25
REMARK 3 BIN FREE R VALUE : 0.3880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 1034
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 5
REMARK 3 SOLVENT ATOMS : 62
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) : 22.40
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.94000
REMARK 3 B22 (A**2) : 0.94000
REMARK 3 B33 (A**2) : -1.41000
REMARK 3 B12 (A**2) : 0.47000
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): 0.211
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.173
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.122
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.406
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.925
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1049 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 644 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1431 ; 1.407 ; 1.983
REMARK 3 BOND ANGLES OTHERS (DEGREES): 1612 ; 0.965 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 143 ; 6.627 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 35 ;33.664 ;28.286
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 169 ;14.585 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 178 ; 0.074 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1169 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 155 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 163 ; 0.213 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 610 ; 0.183 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 512 ; 0.158 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 543 ; 0.088 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 48 ; 0.122 ; 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): 13 ; 0.215 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 18 ; 0.201 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 8 ; 0.285 ; 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): 769 ; 0.645 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 292 ; 0.132 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1154 ; 0.975 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 349 ; 1.740 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 277 ; 2.733 ; 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 : 2
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 1 A 70
REMARK 3 ORIGIN FOR THE GROUP (A): -12.2556 16.8351 9.2223
REMARK 3 T TENSOR
REMARK 3 T11: -0.1721 T22: -0.1542
REMARK 3 T33: -0.1060 T12: 0.0481
REMARK 3 T13: -0.0070 T23: -0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 7.2481 L22: 5.8409
REMARK 3 L33: 2.7107 L12: 1.2527
REMARK 3 L13: 0.3220 L23: -0.1329
REMARK 3 S TENSOR
REMARK 3 S11: -0.1541 S12: 0.0057 S13: 0.8932
REMARK 3 S21: 0.0208 S22: 0.2346 S23: 0.3375
REMARK 3 S31: -0.2394 S32: -0.0578 S33: -0.0805
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 : B 0 B 71
REMARK 3 ORIGIN FOR THE GROUP (A): -3.9723 2.8815 10.2812
REMARK 3 T TENSOR
REMARK 3 T11: -0.1248 T22: -0.0957
REMARK 3 T33: -0.2115 T12: 0.0824
REMARK 3 T13: -0.0407 T23: -0.0361
REMARK 3 L TENSOR
REMARK 3 L11: 2.2276 L22: 4.1439
REMARK 3 L33: 4.8026 L12: 0.9378
REMARK 3 L13: -1.6794 L23: -2.1057
REMARK 3 S TENSOR
REMARK 3 S11: -0.0760 S12: 0.0582 S13: -0.2463
REMARK 3 S21: -0.2210 S22: -0.0271 S23: -0.2200
REMARK 3 S31: 0.5675 S32: 0.2870 S33: 0.1031
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : 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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2IYJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-JUL-06.
REMARK 100 THE DEPOSITION ID IS D_1290029396.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-MAR-05
REMARK 200 TEMPERATURE (KELVIN) : 120.0
REMARK 200 PH : 4.50
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL9-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97929
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10340
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.070
REMARK 200 RESOLUTION RANGE LOW (A) : 44.770
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 12.90
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 36.6000
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) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 84.4
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.54000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: CCP4
REMARK 200 STARTING MODEL: PDB ENTRY 1EEJ
REMARK 200
REMARK 200 REMARK: TWO SETS OF DATA WERE MERAGED TO RESOLVE THE STRUCTURE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 31.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M LITHIUM SULPHATE,0.1M MAGNESIUM
REMARK 280 SULPHATE, 5%ISOPROPNOL (PH4.5), PH 4.50
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2
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+1/2
REMARK 290 5555 Y,-X+Y,Z+1/6
REMARK 290 6555 X-Y,X,Z+5/6
REMARK 290 7555 Y,X,-Z+2/3
REMARK 290 8555 X-Y,-Y,-Z
REMARK 290 9555 -X,-X+Y,-Z+1/3
REMARK 290 10555 -Y,-X,-Z+1/6
REMARK 290 11555 -X+Y,Y,-Z+1/2
REMARK 290 12555 X,X-Y,-Z+5/6
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 179.11800
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 89.55900
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 134.33850
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 44.77950
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 223.89750
REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 179.11800
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 89.55900
REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 44.77950
REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 134.33850
REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 223.89750
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 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 VAL A -3
REMARK 465 ASP A -2
REMARK 465 GLN A -1
REMARK 465 ALA A 0
REMARK 465 LEU A 71
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 LYS A 15 CG CD CE NZ
REMARK 470 SER A 16 CB OG
REMARK 470 LYS A 65 CD CE NZ
REMARK 470 LYS A 69 CG CD CE NZ
REMARK 470 GLN B -1 CD OE1 NE2
REMARK 470 LYS B 11 CD CE NZ
REMARK 470 MET B 12 CG SD CE
REMARK 470 LYS B 15 CB CG CD CE
REMARK 470 SER B 16 CB OG
REMARK 470 LYS B 44 CE NZ
REMARK 470 LYS B 69 CD CE NZ
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 NZ LYS B 15 O HOH B 2007 2.12
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 LYS B 15 -76.74 -99.47
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 ILE B 14 LYS B 15 -146.51
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 A2007 DISTANCE = 6.33 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1072
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1EEJ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE PROTEIN DISULFIDE BOND ISOMERASE,DSBC,
REMARK 900 FROM ESCHERICHIA COLI
REMARK 900 RELATED ID: 1G0T RELATED DB: PDB
REMARK 900 DSBC MUTANT C101S
REMARK 900 RELATED ID: 1JZD RELATED DB: PDB
REMARK 900 DSBC-DSBDALPHA COMPLEX
REMARK 900 RELATED ID: 1JZO RELATED DB: PDB
REMARK 900 DSBC C101S
REMARK 900 RELATED ID: 1TJD RELATED DB: PDB
REMARK 900 THE CRYSTAL STRUCTURE OF THE REDUCED DISULPHIDE BONDISOMERASE, DSBC,
REMARK 900 FROM ESCHERICHIA COLI
DBREF 2IYJ A -3 -2 PDB 2IYJ 2IYJ -3 -2
DBREF 2IYJ A -1 71 UNP P0AEG6 DSBC_ECOLI 19 91
DBREF 2IYJ B -3 -2 PDB 2IYJ 2IYJ -3 -2
DBREF 2IYJ B -1 71 UNP P0AEG6 DSBC_ECOLI 19 91
SEQRES 1 A 75 VAL ASP GLN ALA ASP ASP ALA ALA ILE GLN GLN THR LEU
SEQRES 2 A 75 ALA LYS MET GLY ILE LYS SER SER ASP ILE GLN PRO ALA
SEQRES 3 A 75 PRO VAL ALA GLY MET LYS THR VAL LEU THR ASN SER GLY
SEQRES 4 A 75 VAL LEU TYR ILE THR ASP ASP GLY LYS HIS ILE ILE GLN
SEQRES 5 A 75 GLY PRO MET TYR ASP VAL SER GLY THR ALA PRO VAL ASN
SEQRES 6 A 75 VAL THR ASN LYS MET LEU LEU LYS GLN LEU
SEQRES 1 B 75 VAL ASP GLN ALA ASP ASP ALA ALA ILE GLN GLN THR LEU
SEQRES 2 B 75 ALA LYS MET GLY ILE LYS SER SER ASP ILE GLN PRO ALA
SEQRES 3 B 75 PRO VAL ALA GLY MET LYS THR VAL LEU THR ASN SER GLY
SEQRES 4 B 75 VAL LEU TYR ILE THR ASP ASP GLY LYS HIS ILE ILE GLN
SEQRES 5 B 75 GLY PRO MET TYR ASP VAL SER GLY THR ALA PRO VAL ASN
SEQRES 6 B 75 VAL THR ASN LYS MET LEU LEU LYS GLN LEU
HET SO4 B1072 5
HETNAM SO4 SULFATE ION
FORMUL 3 SO4 O4 S 2-
FORMUL 4 HOH *62(H2 O)
HELIX 1 1 ASP A 1 MET A 12 1 12
HELIX 2 2 VAL A 62 GLN A 70 1 9
HELIX 3 3 ASP B -2 GLY B 13 1 16
HELIX 4 4 VAL B 62 LEU B 71 1 10
SHEET 1 AA 6 SER A 17 PRO A 21 0
SHEET 2 AA 6 MET A 27 THR A 32 -1 O THR A 29 N GLN A 20
SHEET 3 AA 6 GLY A 35 THR A 40 -1 O GLY A 35 N THR A 32
SHEET 4 AA 6 HIS A 45 ILE A 47 -1 O HIS A 45 N THR A 40
SHEET 5 AA 6 MET B 51 ASP B 53 -1 O TYR B 52 N ILE A 46
SHEET 6 AA 6 VAL B 60 ASN B 61 -1 O VAL B 60 N ASP B 53
SHEET 1 AB 6 VAL A 60 ASN A 61 0
SHEET 2 AB 6 MET A 51 ASP A 53 -1 O ASP A 53 N VAL A 60
SHEET 3 AB 6 HIS B 45 GLN B 48 -1 O ILE B 46 N TYR A 52
SHEET 4 AB 6 GLY B 35 THR B 40 -1 O TYR B 38 N ILE B 47
SHEET 5 AB 6 MET B 27 THR B 32 -1 O LYS B 28 N ILE B 39
SHEET 6 AB 6 ASP B 18 PRO B 21 -1 O ASP B 18 N LEU B 31
CISPEP 1 GLY A 49 PRO A 50 0 6.39
CISPEP 2 GLY B 49 PRO B 50 0 6.10
SITE 1 AC1 6 ALA A 25 GLY A 26 LYS A 28 ASP A 41
SITE 2 AC1 6 HOH A2008 LYS B 44
CRYST1 42.138 42.138 268.677 90.00 90.00 120.00 P 65 2 2 24
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 0.023732 0.013701 0.000000 0.00000
SCALE2 0.000000 0.027403 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003722 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
